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Conserved domains on  [gi|1969410693|ref|WP_202796000|]
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adenylyltransferase/cytidyltransferase family protein [Opitutus terrae]

Protein Classification

nucleotidyl transferase family protein( domain architecture ID 117)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 13-157 1.88e-57

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


The actual alignment was detected with superfamily member TIGR02199:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 144  Bit Score: 176.34  E-value: 1.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  13 ARVRDALGRGaQKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERAYALAALECVHT 92
Cdd:TIGR02199   1 ALVARARARG-KKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDY 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1969410693  93 IVLFEQPRLVTEIRALRPDIYVKAGDYSLNSLdrSEREALREVGAEIRFLPFLPDLSTTALLQRI 157
Cdd:TIGR02199  80 VVIFDEDTPEELIGELKPDILVKGGDYKVETL--VGAELVESYGGQVVLLPFVEGRSTTAIIEKI 142
 
Name Accession Description Interval E-value
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 13-157 1.88e-57

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: 176.34  E-value: 1.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  13 ARVRDALGRGaQKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERAYALAALECVHT 92
Cdd:TIGR02199   1 ALVARARARG-KKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDY 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1969410693  93 IVLFEQPRLVTEIRALRPDIYVKAGDYSLNSLdrSEREALREVGAEIRFLPFLPDLSTTALLQRI 157
Cdd:TIGR02199  80 VVIFDEDTPEELIGELKPDILVKGGDYKVETL--VGAELVESYGGQVVLLPFVEGRSTTAIIEKI 142
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 15-157 2.44e-41

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: 143.82  E-value: 2.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  15 VRDALGRGaQKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERAYALAALECVHTIV 94
Cdd:PRK11316  332 VAQARARG-EKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVLAALEAVDWVV 410

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1969410693  95 LFEQ--P-RLVTEIralRPDIYVKAGDYSLNSLDRSErealrEV---GAEIRFLPFLPDLSTTALLQRI 157
Cdd:PRK11316  411 PFEEdtPqRLIAEI---LPDLLVKGGDYKPEEIAGSK-----EVwanGGEVKVLNFEDGCSTTNIIKKI 471
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 24-157 9.99e-39

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: 128.69  E-value: 9.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  24 QKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRalKGPTRPIQPAIERAYALAALECVHTIVLFEQPRLVT 103
Cdd:cd02172     4 KTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVLFDNPTALE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1969410693 104 EIRALRPDIYVKAGDYSLNSLD-----RSEREALREVGAEIRFLPFLPdLSTTALLQRI 157
Cdd:cd02172    82 IIDALQPNIYVKGGDYENPENDvtgkiAPEAEAVKAYGGKIVFTGEIV-FSSSALINRI 139
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 25-157 2.10e-33

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: 114.82  E-value: 2.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  25 KVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVrALKGPtRPIQPAIERAYALAALECVHTIVLFEQPRLVTE 104
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFV-ASKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1969410693 105 IRALRPDIYVKAGDYSLNSLDRSEREALREVGAEIRFLPFLPDLSTTALLQRI 157
Cdd:COG0615    79 IEEIKPDVIVLGDDWKGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 28-156 6.59e-12

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: 59.64  E-value: 6.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  28 LTNGCFDLLHAGHIYFLQHARREGD-ALFVALNSDASVRALKgptRPIQPAIERAYALAALECVHTIVLFEQPRLVTE-I 105
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDeDLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRElL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1969410693 106 RALRPDIYVKAGDySLNSLDRSEREALREVG--AEIRFLPFLP-----DLSTTALLQR 156
Cdd:pfam01467  78 KELNPDVLVIGAD-SLLDFWYELDEILGNVKlvVVVRPVFFIPlkptnGISSTDIRER 134
 
Name Accession Description Interval E-value
rfaE_dom_II TIGR02199
rfaE bifunctional protein, domain II; RfaE is a protein involved in the biosynthesis of ...
 13-157 1.88e-57

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: 176.34  E-value: 1.88e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  13 ARVRDALGRGaQKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERAYALAALECVHT 92
Cdd:TIGR02199   1 ALVARARARG-KKIVFTNGCFDILHAGHVSYLQQARALGDRLVVGVNSDASVKRLKGETRPINPEEDRAEVLAALSSVDY 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1969410693  93 IVLFEQPRLVTEIRALRPDIYVKAGDYSLNSLdrSEREALREVGAEIRFLPFLPDLSTTALLQRI 157
Cdd:TIGR02199  80 VVIFDEDTPEELIGELKPDILVKGGDYKVETL--VGAELVESYGGQVVLLPFVEGRSTTAIIEKI 142
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
 15-157 2.44e-41

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: 143.82  E-value: 2.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  15 VRDALGRGaQKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERAYALAALECVHTIV 94
Cdd:PRK11316  332 VAQARARG-EKIVMTNGCFDILHAGHVSYLANARKLGDRLIVAVNSDASVKRLKGEGRPVNPLEQRMAVLAALEAVDWVV 410

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1969410693  95 LFEQ--P-RLVTEIralRPDIYVKAGDYSLNSLDRSErealrEV---GAEIRFLPFLPDLSTTALLQRI 157
Cdd:PRK11316  411 PFEEdtPqRLIAEI---LPDLLVKGGDYKPEEIAGSK-----EVwanGGEVKVLNFEDGCSTTNIIKKI 471
RfaE_N cd02172
N-terminal domain of RfaE; RfaE is a protein involved in the biosynthesis of ...
 24-157 9.99e-39

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: 128.69  E-value: 9.99e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  24 QKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRalKGPTRPIQPAIERAYALAALECVHTIVLFEQPRLVT 103
Cdd:cd02172     4 KTVVLCHGVFDLLHPGHVRHLQAARSLGDILVVSLTSDRYVN--KGPGRPIFPEDLRAEVLAALGFVDYVVLFDNPTALE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1969410693 104 EIRALRPDIYVKAGDYSLNSLD-----RSEREALREVGAEIRFLPFLPdLSTTALLQRI 157
Cdd:cd02172    82 IIDALQPNIYVKGGDYENPENDvtgkiAPEAEAVKAYGGKIVFTGEIV-FSSSALINRI 139
TagD COG0615
Glycerol-3-phosphate cytidylyltransferase, cytidylyltransferase family [Cell wall/membrane ...
 25-157 2.10e-33

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: 114.82  E-value: 2.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  25 KVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVrALKGPtRPIQPAIERAYALAALECVHTIVLFEQPRLVTE 104
Cdd:COG0615     1 KRVITYGTFDLLHPGHINLLKRAKALGDELIVGVATDEFV-ASKGR-KPIIPEEQRKEIVEALKYVDEVILGEEWDKFED 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1969410693 105 IRALRPDIYVKAGDYSLNSLDRSEREALREVGAEIRFLPFLPDLSTTALLQRI 157
Cdd:COG0615    79 IEEIKPDVIVLGDDWKGDFDFLKEELEKRGIGCEVVYLPRTEGISSTKIKKRI 131
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 25-157 5.75e-22

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: 85.81  E-value: 5.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  25 KVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGptRPIQPAIERAYALAALECVHTIVLFEQPRLVTE 104
Cdd:cd02170     2 KRVYAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETVAKIKR--RPILPEEQRAEVVEALKYVDEVILGHPWSYFKP 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1969410693 105 IRALRPDIYVKAGDYSLNSLDRSEREALREVGAEIRF-LPFLPDLSTTALLQRI 157
Cdd:cd02170    80 LEELKPDVIVLGDDQKNGVDEEEVYEELKKRGKVIEVpRKKTEGISSSDIIKRI 133
ECT cd02173
CTP:phosphoethanolamine cytidylyltransferase (ECT); CTP:phosphoethanolamine ...
 24-159 1.74e-17

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: 74.60  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  24 QKVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERayALAALEC--VHTIVlFEQPRL 101
Cdd:cd02173     2 DKVVYVDGAFDLFHIGHIEFLEKARELGDYLIVGVHDDQTVNEYKGSNYPIMNLHER--VLSVLACryVDEVV-IGAPYV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1969410693 102 VTE--IRALRPDIYV----KAGDYSLNSLDR----SEREALREVGAEirflpflPDLSTTALLQRIVA 159
Cdd:cd02173    79 ITKelIEHFKIDVVVhgktEETPDSLDGEDPyavpKEMGIFKEIDSG-------SDLTTRDIVNRIIK 139
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 26-87 1.00e-13

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: 62.32  E-value: 1.00e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1969410693  26 VVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGptRPIQPAIERAYALAAL 87
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQFVNPLKG--EPVFSLEERLEMLKAL 60
G3P_Cytidylyltransferase cd02171
glycerol-3-phosphate cytidylyltransferase; Glycerol-3-phosphate cytidylyltransferase, ...
 25-158 2.45e-13

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: 63.27  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  25 KVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDaSVRALKGpTRPIQPAIERAYALAALECVHTIV---LFEQPrl 101
Cdd:cd02171     2 KVVITYGTFDLLHIGHLNLLERAKALGDKLIVAVSTD-EFNAGKG-KKAVIPYEQRAEILESIRYVDLVIpetNWEQK-- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1969410693 102 VTEIRALRPDIYVKAGDYslnsldRSEREALREVgAEIRFLPFLPDLSTTALLQRIV 158
Cdd:cd02171    78 IEDIKKYNVDVFVMGDDW------EGKFDFLKEY-CEVVYLPRTKGISSTQLKEMLK 127
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 28-156 6.59e-12

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: 59.64  E-value: 6.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  28 LTNGCFDLLHAGHIYFLQHARREGD-ALFVALNSDASVRALKgptRPIQPAIERAYALAALECVHTIVLFEQPRLVTE-I 105
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDeDLIVGVPSDEPPHKLK---RPLFSAEERLEMLELAKWVDEVIVVAPWELTRElL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1969410693 106 RALRPDIYVKAGDySLNSLDRSEREALREVG--AEIRFLPFLP-----DLSTTALLQR 156
Cdd:pfam01467  78 KELNPDVLVIGAD-SLLDFWYELDEILGNVKlvVVVRPVFFIPlkptnGISSTDIRER 134
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 25-158 8.26e-12

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 62.11  E-value: 8.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  25 KVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERayALAALECVHTI-VLFEQPRLVT 103
Cdd:PTZ00308  193 RIVYVDGSFDLFHIGHIRVLQKARELGDYLIVGVHEDQVVNEQKGSNYPIMNLNER--VLGVLSCRYVDeVVIGAPFDVT 270

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1969410693 104 E--IRALRPDIyVKAGDYS--LNSLDRSEREAL-------REVGAEirflpflPDLSTTALLQRIV 158
Cdd:PTZ00308  271 KevIDSLHINV-VVGGKFSdlVNEEGGSDPYEVpkamgifKEVDSG-------CDLTTDSIVDRVV 328
PTZ00308 PTZ00308
ethanolamine-phosphate cytidylyltransferase; Provisional
 27-158 2.44e-11

ethanolamine-phosphate cytidylyltransferase; Provisional


Pssm-ID: 140329 [Multi-domain]  Cd Length: 353  Bit Score: 60.57  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  27 VLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPtrPIQPAIERAYALAALECVHTIVlfEQPRLVT--- 103
Cdd:PTZ00308   14 VWVDGCFDMLHFGHANALRQARALGDELFVGCHSDEEIMRNKGP--PVMHQEERYEALRACKWVDEVV--EGYPYTTrle 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1969410693 104 EIRALRPDIYVKAGDYSLNSLDRSEREALREVGaEIRFLPFLPDLSTTALLQRIV 158
Cdd:PTZ00308   90 DLERLECDFVVHGDDISVDLNGRNSYQEIIDAG-KFKVVKRTEGISTTDLVGRML 143
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 25-95 5.22e-10

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 57.00  E-value: 5.22e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1969410693  25 KVVLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPTRPIQPAIERAYALAALECVHTIVL 95
Cdd:PLN02406  252 RIVYIDGAFDLFHAGHVEILRLARALGDFLLVGIHTDQTVSAHRGAHRPIMNLHERSLSVLACRYVDEVII 322
CCT cd02174
CTP:phosphocholine cytidylyltransferase; CTP:phosphocholine cytidylyltransferase (CCT) ...
 31-158 5.79e-10

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: 54.50  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  31 GCFDLLHAGHIYFLQHARREG--DALFVALNSDASVRALKGPtrPIQPAIERAYALAALECVHTIVLfEQPRLVTE--IR 106
Cdd:cd02174     9 GCFDLFHYGHANALRQAKKLGpnDYLIVGVHSDEEIHKHKGP--PVMTEEERYEAVRHCKWVDEVVE-GAPYVTTPefLD 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1969410693 107 ALRPDiYVKAGDysLNSLDRSEREALREVGAEIRFLPF--LPDLSTTALLQRIV 158
Cdd:cd02174    86 KYKCD-YVAHGD--DIYLDADGEDCYQEVKDAGRFKEVkrTEGVSTTDLIGRIL 136
PLN02406 PLN02406
ethanolamine-phosphate cytidylyltransferase
 27-104 1.05e-09

ethanolamine-phosphate cytidylyltransferase


Pssm-ID: 215227 [Multi-domain]  Cd Length: 418  Bit Score: 55.84  E-value: 1.05e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1969410693  27 VLTNGCFDLLHAGHIYFLQHARREGDALFVALNSDASVRALKGPtrPIQPAIERAYALAALECVHTiVLFEQPRLVTE 104
Cdd:PLN02406   56 VYMDGCFDMMHYGHANALRQARALGDELVVGVVSDEEIIANKGP--PVTPMHERMIMVSGVKWVDE-VIPDAPYAITE 130
NMNAT_NadR cd02167
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ...
 31-119 7.80e-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: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1969410693  31 GCFDLLHAGHIYFLQHARREGDALFVALNSDAsvrALKGPTRPIQPAIERAYALAALECVHTIV--LFEQPR-------- 100
Cdd:cd02167     6 GKFAPLHTGHVYLIYKALSQVDELLIIVGSDD---TRDDARTGLPLEKRLRWLREIFPDQENIVvhTLNEPDipeypngw 82

                          90       100
                  ....*....|....*....|....*...
gi 1969410693 101 ---------LVTEIRALRPDIYVKAGDY 119
Cdd:cd02167    83 diwsnrvktLIAENTRCRPDIVFTAEEY 110
 
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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