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Conserved domains on  [gi|2039085818|emb|CAG5337844|]
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putative nicotinate-nucleotide adenylyltransferase [Streptococcus pneumoniae]

Protein Classification

nicotinate-nucleotide adenylyltransferase( domain architecture ID 10011203)

nicotinate-nucleotide adenylyltransferase catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide

EC:  2.7.7.18
Gene Ontology:  GO:0004515|GO:0005524|GO:0009435
PubMed:  19273075
SCOP:  4003834

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
21-209 3.86e-94

nicotinate-nucleotide adenylyltransferase;


:

Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 273.25  E-value: 3.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  21 KKRKQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELE 100
Cdd:PRK00071    1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 101 RKGISYTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGT------------SYPVIW 168
Cdd:PRK00071   81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2039085818 169 VDVPLMDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:PRK00071  161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLY 201
 
Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
21-209 3.86e-94

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 273.25  E-value: 3.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  21 KKRKQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELE 100
Cdd:PRK00071    1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 101 RKGISYTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGT------------SYPVIW 168
Cdd:PRK00071   81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2039085818 169 VDVPLMDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:PRK00071  161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLY 201
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 23-209 1.52e-92

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 268.91  E-value: 1.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  23 RKQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERK 102
Cdd:COG1057     1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 103 GISYTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKV---------GTSYPVIWVDVPL 173
Cdd:COG1057    81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELdeleelealKPGGRIILLDVPL 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2039085818 174 MDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:COG1057   161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 26-209 3.62e-79

Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 234.83  E-value: 3.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  26 VGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVdKKETIPEHHRLKMLELAIEGIDGLVIETIELERKGIS 105
Cdd:cd02165     1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHK-PPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 106 YTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGTSYP---------VIWVDVPLMDI 176
Cdd:cd02165    80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2039085818 177 SSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:cd02165   160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 28-209 7.06e-67

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 203.70  E-value: 7.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  28 ILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERKGISYT 107
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 108 YDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGTSYPVIW-----------VDVPLMDI 176
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmhhgnltlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2039085818 177 SSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 28-182 3.49e-36

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: 123.58  E-value: 3.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  28 ILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERkgisyt 107
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2039085818 108 ydtmKILTEKNPDtdyYFIIGADMVDYLpkWYRIDELVDMVQFVGVQRPRYkvgtsypvIWVDVPLMDISSSMVR 182
Cdd:pfam01467  75 ----ELLKELNPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF--------FIPLKPTNGISSTDIR 132
 
Name Accession Description Interval E-value
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
21-209 3.86e-94

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 273.25  E-value: 3.86e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  21 KKRKQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELE 100
Cdd:PRK00071    1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 101 RKGISYTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGT------------SYPVIW 168
Cdd:PRK00071   81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2039085818 169 VDVPLMDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:PRK00071  161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLY 201
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 23-209 1.52e-92

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 268.91  E-value: 1.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  23 RKQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERK 102
Cdd:COG1057     1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 103 GISYTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKV---------GTSYPVIWVDVPL 173
Cdd:COG1057    81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELdeleelealKPGGRIILLDVPL 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2039085818 174 MDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:COG1057   161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 26-209 3.62e-79

Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 234.83  E-value: 3.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  26 VGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVdKKETIPEHHRLKMLELAIEGIDGLVIETIELERKGIS 105
Cdd:cd02165     1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHK-PPKPASFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 106 YTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGTSYP---------VIWVDVPLMDI 176
Cdd:cd02165    80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2039085818 177 SSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:cd02165   160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 28-209 7.06e-67

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 203.70  E-value: 7.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  28 ILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERKGISYT 107
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 108 YDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGTSYPVIW-----------VDVPLMDI 176
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmhhgnltlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2039085818 177 SSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
24-209 3.17e-43

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 147.79  E-value: 3.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  24 KQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERKG 103
Cdd:PRK07152    1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALKNLPKMEVSDFEIKRQN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 104 ISYTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGTS---YPVIWVDVPLMDISSSM 180
Cdd:PRK07152   81 VSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKKNlkkYNVLLLKNKNLNISSTK 160

                         170       180
                  ....*....|....*....|....*....
gi 2039085818 181 VRDflaqgRKPNFLLPQPVLDYIEKEGLY 209
Cdd:PRK07152  161 IRK-----GNLLGKLDPKVNDYINENFLY 184
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 28-182 3.49e-36

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: 123.58  E-value: 3.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  28 ILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIETIELERkgisyt 107
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2039085818 108 ydtmKILTEKNPDtdyYFIIGADMVDYLpkWYRIDELVDMVQFVGVQRPRYkvgtsypvIWVDVPLMDISSSMVR 182
Cdd:pfam01467  75 ----ELLKELNPD---VLVIGADSLLDF--WYELDEILGNVKLVVVVRPVF--------FIPLKPTNGISSTDIR 132
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
25-209 1.45e-27

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 104.48  E-value: 1.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  25 QVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPphVDKKETIPEHHRLKMLELAIEGIDG----LVIETIELE 100
Cdd:PRK06973   23 RIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQP--WQKADVSAAEHRLAMTRAAAASLVLpgvtVRVATDEIE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 101 RKGISYTYDTMKILTEK-NPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRPRYKVGTSYPVI------------ 167
Cdd:PRK06973  101 HAGPTYTVDTLARWRERiGPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFDLGAASPAVaaeiaarqadad 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2039085818 168 ----------WVDVPL-MDISSSMVRDFLAQGRKPNFLLPQP--------VLDYIEKEGLY 209
Cdd:PRK06973  181 vlqatpaghlLIDTTLaFDLSATDIRAHLRACIARRAQVPDAsaehvpaaVWAYILQHRLY 241
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 26-164 9.16e-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: 9.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  26 VGILGGNFNPVHNAHLIVADQVRQQlGLDQVLLMP-EYQPPHVDKKETIPEHHRLKMLELAIEGIDGLVIetIELERKGI 104
Cdd:cd02039     1 VGIIIGRFEPFHLGHLKLIKEALEE-ALDEVIIIIvSNPPKKKRNKDPFSLHERVEMLKEILKDRLKVVP--VDFPEVKI 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2039085818 105 SYTYDTMKILTEKNPDTdyYFIIGADMVDYLPKWY--RIDELVDMVQFVGVQRPR--YKVGTSY 164
Cdd:cd02039    78 LLAVVFILKILLKVGPD--KVVVGEDFAFGKNASYnkDLKELFLDIEIVEVPRVRdgKKISSTL 139
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 31-209 1.03e-10

Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis. This subfamily consists strictly of eukaryotic members and includes secondary structural elements not found in all NMNATs.


Pssm-ID: 185681 [Multi-domain]  Cd Length: 225  Bit Score: 58.85  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  31 GNFNPVHNAHL----IVADQVRQQlGLDQVLlmPEYQPPHVD---KKETIPEHHRLKMLELAIEGIDGLVIETIELERKG 103
Cdd:cd09286     7 GSFNPITNMHLrmfeLARDHLHET-GRYEVV--GGIISPVNDaygKKGLASAKHRVAMCRLAVQSSDWIRVDDWESLQPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 104 ISYTYDTMK------------ILTEKNPDTDY-------YFIIGADMVDYL--PKWYRIDELVDMVQFVGV-------QR 155
Cdd:cd09286    84 WMRTAKVLRhhreeinnkyggIEGAAKRVLDGsrrevkiMLLCGADLLESFgiPGLWKDADLEEILGEFGLvvvertgSD 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2039085818 156 PRyKVGTSYPVIWV----------DVPlMDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:cd09286   164 PE-NFIASSDILRKyqdnihlvkdWIP-NDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
24-209 6.81e-10

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 55.89  E-value: 6.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  24 KQVGILGGNFNPVHNAHLIVADQVRQqlgLDQVLLMPEYQppHVDKKETIPEHHRLKMLELAIE--GIDGLVIETIE--L 99
Cdd:PRK08887    2 KKIAVFGSAFNPPSLGHKSVIESLSH---FDLVLLVPSIA--HAWGKTMLDYETRCQLVDAFIQdlGLSNVQRSDIEqeL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818 100 ERKGIS-YTYDTMKILTEKNPDTDYYFIIGADMVDYLPKWYRIDELVDMVQFVGVQRpryKVgtsypviwvdvplmDISS 178
Cdd:PRK08887   77 YAPDESvTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEITQRWTVMACPE---KV--------------PIRS 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2039085818 179 SMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:PRK08887  140 TDIRNALQNGKDISHLTTPGVARLLKEHQLY 170
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 26-90 3.20e-07

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: 46.15  E-value: 3.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2039085818  26 VGILGGNFNPVHNAHLIVADQVRQQlgLDQVLL---MPEYQPPHvDKKETIPEHHRLKMLELAIEGID 90
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKEL--FDELIVgvgSDQFVNPL-KGEPVFSLEERLEMLKALKYVDE 65
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 8-209 9.81e-07

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 47.76  E-value: 9.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818   8 PFTKVELEPEIKEKKRKQVGILGGNFNPVHNAHLIVADQVRQQLGLDQVLLMPEYQPPHVD---KKETIPEHHRLKMLEL 84
Cdd:PLN02945    6 PTEKLSCGANSTGPRTRVVLVATGSFNPPTYMHLRMFELARDALMSEGYHVLGGYMSPVNDaykKKGLASAEHRIQMCQL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2039085818  85 AIEGIDGLVIETIELERKGISYTYDTMK----ILTEKNPDTD----YYFIIGADMVDYL--PKWYRIDELVDMVQFVGV- 153
Cdd:PLN02945   86 ACEDSDFIMVDPWEARQSTYQRTLTVLArvetSLNNNGLASEesvrVMLLCGSDLLESFstPGVWIPDQVRTICRDYGVv 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2039085818 154 ------QRPRYKVGTSY-------PVIWVD--VPlMDISSSMVRDFLAQGRKPNFLLPQPVLDYIEKEGLY 209
Cdd:PLN02945  166 cirregQDVEKLVSQDEilnenrgNILVVDdlVP-NSISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLY 235
 
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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