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Conserved domains on  [gi|2254949673|gb|USH35900|]
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glycerol-3-phosphate cytidylyltransferase [Staphylococcus pseudintermedius]

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 1.04e-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: 202.64  E-value: 1.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGqKETDV 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2254949673  82 EKYEIDTFVMGHDWEGEFDFLKDK-------CEVIYLKRTEGISTTQIKQEL 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 1.04e-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: 202.64  E-value: 1.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGqKETDV 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2254949673  82 EKYEIDTFVMGHDWEGEFDFLKDK-------CEVIYLKRTEGISTTQIKQEL 126
Cdd:COG0615    80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-129 5.34e-64

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: 190.77  E-value: 5.34e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETD 80
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2254949673  81 VEKYEIDTFVMGHDWEGEFDFLKDKCEVIYLKRTEGISTTQIKQELYGK 129
Cdd:cd02171    81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 7.68e-57

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: 172.74  E-value: 7.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   4 VITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETDVEK 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2254949673  84 YEIDTFVMGHDWEGEFDFLKDKC--EVIYLKRTEGISTTQIKQEL 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 2.26e-30

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: 105.86  E-value: 2.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   5 ITYGTYDLLHYGHIELLRRAREMGDY-LVVALSSDEFNRiKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETDVEK 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPH-KLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2254949673  84 YEIDTFVMGHD--------WEGEFDFLKDKCEV-----IYLKRTEGISTTQIKQ 124
Cdd:pfam01467  80 LNPDVLVIGADslldfwyeLDEILGNVKLVVVVrpvffIPLKPTNGISSTDIRE 133
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-122 8.21e-17

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 74.82  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   3 RVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEfNRIKNK-KSYYNFEQRKMMLESIRYVDLVIPENDWGQKETDV 81
Cdd:PTZ00308   13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDE-EIMRNKgPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2254949673  82 EKYEIDTFVMGHD------WEGEFDFLKDKCEVIYLKRTEGISTTQI 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 1.04e-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: 202.64  E-value: 1.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGqKETDV 81
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFVASKGRKPIIPEEQRKEIVEALKYVDEVILGEEWD-KFEDI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2254949673  82 EKYEIDTFVMGHDWEGEFDFLKDK-------CEVIYLKRTEGISTTQIKQEL 126
Cdd:COG0615    80 EEIKPDVIVLGDDWKGDFDFLKEElekrgigCEVVYLPRTEGISSTKIKKRI 131
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 1-129 5.34e-64

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: 190.77  E-value: 5.34e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETD 80
Cdd:cd02171     1 MKVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTDEFNAGKGKKAVIPYEQRAEILESIRYVDLVIPETNWEQKIED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2254949673  81 VEKYEIDTFVMGHDWEGEFDFLKDKCEVIYLKRTEGISTTQIKQELYGK 129
Cdd:cd02171    81 IKKYNVDVFVMGDDWEGKFDFLKEYCEVVYLPRTKGISSTQLKEMLKKL 129
g3p_cytidyltrns TIGR01518
glycerol-3-phosphate cytidylyltransferase; This model describes glycerol-3-phosphate ...
 4-126 7.68e-57

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: 172.74  E-value: 7.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   4 VITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETDVEK 83
Cdd:TIGR01518   1 VLTYGTFDLLHWGHINLLERAKQLGDYLIVALSTDEFNLQKQKKAYHSYEHRKLILETIRYVDLVIPEKSWEQKKQDIID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2254949673  84 YEIDTFVMGHDWEGEFDFLKDKC--EVIYLKRTEGISTTQIKQEL 126
Cdd:TIGR01518  81 FNIDVFVMGDDWEGKFDFLKDECplKVVYLPRTEGVSTTKIKKEI 125
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 1-125 1.48e-36

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: 121.63  E-value: 1.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETD 80
Cdd:cd02170     1 MKRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKRRPILPEEQRAEVVEALKYVDEVILGHPWSYFKPL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2254949673  81 VEKYEiDTFVMGHDWEG------EFDFLKDKCEVIYL--KRTEGISTTQIKQE 125
Cdd:cd02170    81 EELKP-DVIVLGDDQKNgvdeeeVYEELKKRGKVIEVprKKTEGISSSDIIKR 132
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 5-124 2.26e-30

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: 105.86  E-value: 2.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   5 ITYGTYDLLHYGHIELLRRAREMGDY-LVVALSSDEFNRiKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETDVEK 83
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEdLIVGVPSDEPPH-KLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2254949673  84 YEIDTFVMGHD--------WEGEFDFLKDKCEV-----IYLKRTEGISTTQIKQ 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 4.71e-23

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: 85.05  E-value: 4.71e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2254949673   3 RVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLV 68
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKGEPVFSLEERLEMLKALKYVDEV 66
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 3-122 8.53e-18

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: 74.14  E-value: 8.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   3 RVITYGTYDLLHYGHIELLRRAREMG--DYLVVALSSDEfNRIKNK-KSYYNFEQRKMMLESIRYVDLVIPENDWGQKET 79
Cdd:cd02174     4 RVYVDGCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDE-EIHKHKgPPVMTEEERYEAVRHCKWVDEVVEGAPYVTTPE 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2254949673  80 DVEKYEIDTFVMGHD----WEGE--FDFLKDKCEVIYLKRTEGISTTQI 122
Cdd:cd02174    83 FLDKYKCDYVAHGDDiyldADGEdcYQEVKDAGRFKEVKRTEGVSTTDL 131
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 3-122 8.21e-17

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 74.82  E-value: 8.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   3 RVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEfNRIKNK-KSYYNFEQRKMMLESIRYVDLVIPENDWGQKETDV 81
Cdd:PTZ00308   13 RVWVDGCFDMLHFGHANALRQARALGDELFVGCHSDE-EIMRNKgPPVMHQEERYEALRACKWVDEVVEGYPYTTRLEDL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2254949673  82 EKYEIDTFVMGHD------WEGEFDFLKDKCEVIYLKRTEGISTTQI 122
Cdd:PTZ00308   92 ERLECDFVVHGDDisvdlnGRNSYQEIIDAGKFKVVKRTEGISTTDL 138
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 3-122 1.19e-15

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 71.64  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   3 RVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKE---- 78
Cdd:PLN02406   55 RVYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGPPVTPMHERMIMVSGVKWVDEVIPDAPYAITEefmn 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2254949673  79 TDVEKYEIDTFVMGHD------WEGEFDFLKDKCEVIYLKRTEGISTTQI 122
Cdd:PLN02406  135 KLFNEYNIDYIIHGDDpcllpdGTDAYALAKKAGRYKQIKRTEGVSSTDI 184
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 3-124 2.97e-14

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: 64.77  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   3 RVITYGTYDLLHYGHIELLRRAREMG-DYLVVALSSDEFNRiKNKKSYYNFEQRKMMLESIRY-VDLVIPENDWGQKETD 80
Cdd:cd02039     1 VGIIIGRFEPFHLGHLKLIKEALEEAlDEVIIIIVSNPPKK-KRNKDPFSLHERVEMLKEILKdRLKVVPVDFPEVKILL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2254949673  81 V--------EKYEIDTFVMGHDWEGEFD--------FLKDKCEVIYLKRTEG---ISTTQIKQ 124
Cdd:cd02039    80 AvvfilkilLKVGPDKVVVGEDFAFGKNasynkdlkELFLDIEIVEVPRVRDgkkISSTLIRE 142
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 5-92 1.31e-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: 63.43  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   5 ITY--GTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSY--YNFEQRKMMLESIRYVDLVIPENDWGQKETD 80
Cdd:cd02173     4 VVYvdGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYpiMNLHERVLSVLACRYVDEVVIGAPYVITKEL 83

                          90
                  ....*....|..
gi 2254949673  81 VEKYEIDTFVMG 92
Cdd:cd02173    84 IEHFKIDVVVHG 95
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 4-96 1.99e-13

N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ADP-L-glycero-D-manno-heptose, a precursor for LPS inner core biosynthesis. RfaE is a bifunctional protein in Escherichia coli, and separate proteins in other organisms. Domain I is suggested to act in D-glycero-D-manno-heptose 1-phosphate biosynthesis, while domain II (this family) adds ADP to yield ADP-D-glycero-D-manno-heptose .


Pssm-ID: 173923 [Multi-domain]  Cd Length: 144  Bit Score: 62.82  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   4 VITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEF-NRIKNkKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETdVE 82
Cdd:cd02172     7 VLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYvNKGPG-RPIFPEDLRAEVLAALGFVDYVVLFDNPTALEI-ID 84

                          90
                  ....*....|....
gi 2254949673  83 KYEIDTFVMGHDWE 96
Cdd:cd02172    85 ALQPNIYVKGGDYE 98
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 4-69 4.37e-12

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 61.34  E-value: 4.37e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2254949673   4 VITY--GTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRiKNKKSYY---NFEQRKMMLESIRYVDLVI 69
Cdd:PTZ00308  193 RIVYvdGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVN-EQKGSNYpimNLNERVLGVLSCRYVDEVV 262
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 2-122 4.39e-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: 4.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDE-FNRIKNKKSYYN-FEQRKMMLESIRYVDLVIP-ENDWGQKE 78
Cdd:PRK11316  341 KIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDAsVKRLKGEGRPVNpLEQRMAVLAALEAVDWVVPfEEDTPQRL 420

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2254949673  79 tdVEKYEIDTFVMGHDWEGEfDFLKDKC------EVIYLKRTEGISTTQI 122
Cdd:PRK11316  421 --IAEILPDLLVKGGDYKPE-EIAGSKEvwanggEVKVLNFEDGCSTTNI 467
PRK00777 PRK00777
pantetheine-phosphate adenylyltransferase;
1-74 5.10e-12

pantetheine-phosphate adenylyltransferase;


Pssm-ID: 234834  Cd Length: 153  Bit Score: 59.08  E-value: 5.10e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2254949673   1 MKRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLEsiRYVDLVIPENDW 74
Cdd:PRK00777    1 MMKVAVGGTFDPLHDGHRALLRKAFELGKRVTIGLTSDEFAKSYKKHKVRPYEVRLKNLK--KFLKAVEYDREY 72
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 8-117 8.85e-12

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 60.85  E-value: 8.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   8 GTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRIKNKKSY--YNFEQRKMMLESIRYVDLVIPENDWGQKETDVEKYE 85
Cdd:PLN02406  258 GAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRpiMNLHERSLSVLACRYVDEVIIGAPWEVSKDMITTFN 337

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2254949673  86 IDTFVMGHDWEGEfDFLKDKCEVIYLKRTEGI 117
Cdd:PLN02406  338 ISLVVHGTVAENN-DFLKGEDDPYAVPKSMGI 368
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-120 1.35e-11

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: 56.78  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   4 VITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDefNRIKNKKSYYNFEQRKMMLESiryvdlvipendwgqketdvek 83
Cdd:cd02156     2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDN--PPVKVWQDPHELEERKESIEE---------------------- 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2254949673  84 yeiDTFVMGHDWEGEFD---------FLKDKCEVIYLKR----TEGISTT 120
Cdd:cd02156    58 ---DISVCGEDFQQNRElyrwvkdniTLPVDPEQVELPRlnleTTVMSKR 104
PLN02413 PLN02413
choline-phosphate cytidylyltransferase
 3-122 4.07e-11

choline-phosphate cytidylyltransferase


Pssm-ID: 215229  Cd Length: 294  Bit Score: 58.42  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2254949673   3 RVITYGTYDLLHYGHIELLRRAREM--GDYLVVALSSDEFNRIKNKKSYYNFEQRKMMLESIRYVDLVIPENDWGQKETD 80
Cdd:PLN02413   29 RVYADGIYDLFHFGHARSLEQAKKLfpNTYLLVGCCNDELTHKYKGKTVMTEDERYESLRHCKWVDEVIPDAPWVITQEF 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2254949673  81 VEKYEIDtfVMGHD----------WEGEFDFLKDKCEVIYLKRTEGISTTQI 122
Cdd:PLN02413  109 LDKHRID--YVAHDalpyadasgaGKDVYEFVKKIGKFKETKRTDGISTSDI 158
PRK01170 PRK01170
bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;
2-60 2.16e-10

bifunctional pantetheine-phosphate adenylyltransferase/NTP phosphatase;


Pssm-ID: 234912 [Multi-domain]  Cd Length: 322  Bit Score: 56.75  E-value: 2.16e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949673   2 KRVITYGTYDLLHYGHIELLRRAREMGDYLVVALSSDEFNRiKNKKSYYNFEQRKMMLE 60
Cdd:PRK01170    1 MITVVGGTFSKLHKGHKALLKKAIETGDEVVIGLTSDEYVR-KNKVYPIPYEDRKRKLE 58
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 8-60 1.38e-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: 44.76  E-value: 1.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2254949673   8 GTYDLLHYGHIELLRRAREMGDYLVVALSSDefnriKNKKSYYNFEQRKMMLE 60
Cdd:cd02163     6 GSFDPITNGHLDIIERASKLFDEVIVAVAVN-----PSKKPLFSLEERVELIR 53
PPAT_CoAS cd02164
phosphopantetheine adenylyltransferase domain of eukaryotic and archaeal bifunctional enzymes; ...
 8-71 2.78e-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: 41.11  E-value: 2.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2254949673   8 GTYDLLHYGHIELLRRAREMG-DYLVVALSSDEFNRiknKKSYYN----FEQRKMMLEsiRYVDLVIPE 71
Cdd:cd02164     6 GTFDRLHDGHKILLSVAFLLAgEKLIIGVTSDELLK---NKSLKEliepYEERIANLH--EFLVDLKPT 69
Pantoate_ligase pfam02569
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ...
 13-33 5.93e-03

Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.


Pssm-ID: 460595 [Multi-domain]  Cd Length: 277  Bit Score: 35.09  E-value: 5.93e-03
                          10        20
                  ....*....|....*....|.
gi 2254949673  13 LHYGHIELLRRAREMGDYLVV 33
Cdd:pfam02569  32 LHEGHLSLVRRARAENDVVVV 52
 
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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