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Conserved domains on  [gi|1270533023|ref|NP_001344374|]
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nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 isoform b [Mus musculus]

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 ...
1-166 2.05e-84

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 cd09286:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 225  Bit Score: 247.99  E-value: 2.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELLRSSAQMDGPDPSKTPSaSAALPELKLLCGADVLKTFQTPNL 80
Cdd:cd09286    61 MCRLAVQSSDWIRVDDWESLQPEWMRTAKVLRHHREEINNKYGGIEGAAKRVLDG-SRREVKIMLLCGADLLESFGIPGL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKDTHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNEISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:cd09286   140 WKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDWIPNDISSTKVRRALRRGMSVKYLLPDPVIEYI 219

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:cd09286   220 EQHQLY 225
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
1-166 2.05e-84

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: 247.99  E-value: 2.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELLRSSAQMDGPDPSKTPSaSAALPELKLLCGADVLKTFQTPNL 80
Cdd:cd09286    61 MCRLAVQSSDWIRVDDWESLQPEWMRTAKVLRHHREEINNKYGGIEGAAKRVLDG-SRREVKIMLLCGADLLESFGIPGL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKDTHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNEISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:cd09286   140 WKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDWIPNDISSTKVRRALRRGMSVKYLLPDPVIEYI 219

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:cd09286   220 EQHQLY 225
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
1-166 2.92e-49

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: 157.87  E-value: 2.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELlrssaqmdgPDPsktpsasaalpELKLLCGADVLKTFQtpnL 80
Cdd:TIGR00482  54 MLKLAIEDNPKFEVDDFEIKRGGPSYTIDTLKHLKKKY---------PDV-----------ELYFIIGADALRSFP---L 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKdtHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNeISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:TIGR00482 111 WK--DWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTLLHNPRVP-ISSTEIRQRIRQGKSIEYLLPDPVIKYI 187

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:TIGR00482 188 KQHGLY 193
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
1-166 6.74e-42

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 140.21  E-value: 6.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELLRSSAQMDGPdpsktpsasaalPELKLLCGADVLKTFQTPNL 80
Cdd:PLN02945   82 MCQLACEDSDFIMVDPWEARQSTYQRTLTVLARVETSLNNNGLASEES------------VRVMLLCGSDLLESFSTPGV 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKDTHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNEISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:PLN02945  150 WIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLVPNSISSTRVRECISRGLSVKYLTPDGVIDYI 229

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:PLN02945  230 KEHGLY 235
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
1-166 2.22e-27

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: 101.74  E-value: 2.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQ--WM-ETVKVLRHHHrellrssaqmdgpdpsktPSAsaalpELKLLCGADVLKTFQT 77
Cdd:COG1057    59 MLRLAIADNPRFEVSDIELERPGpsYTiDTLRELREEY------------------PDA-----ELYFIIGADALLQLPK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  78 pnlWKDthIQEIVEKFGLVCVSRSGHDPERYISDSPIlqQFQHNIHLAREPVLnEISATYVRKALGQGQSVKYLLPEAVI 157
Cdd:COG1057   116 ---WKR--WEELLELAHLVVVPRPGYELDELEELEAL--KPGGRIILLDVPLL-DISSTEIRERLAEGKSIRYLVPDAVE 187

                  ....*....
gi 1270533023 158 TYIRDQGLY 166
Cdd:COG1057   188 DYIREHGLY 196
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
1-166 2.05e-84

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: 247.99  E-value: 2.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELLRSSAQMDGPDPSKTPSaSAALPELKLLCGADVLKTFQTPNL 80
Cdd:cd09286    61 MCRLAVQSSDWIRVDDWESLQPEWMRTAKVLRHHREEINNKYGGIEGAAKRVLDG-SRREVKIMLLCGADLLESFGIPGL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKDTHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNEISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:cd09286   140 WKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDWIPNDISSTKVRRALRRGMSVKYLLPDPVIEYI 219

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:cd09286   220 EQHQLY 225
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
1-166 2.92e-49

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: 157.87  E-value: 2.92e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELlrssaqmdgPDPsktpsasaalpELKLLCGADVLKTFQtpnL 80
Cdd:TIGR00482  54 MLKLAIEDNPKFEVDDFEIKRGGPSYTIDTLKHLKKKY---------PDV-----------ELYFIIGADALRSFP---L 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKdtHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNeISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:TIGR00482 111 WK--DWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTLLHNPRVP-ISSTEIRQRIRQGKSIEYLLPDPVIKYI 187

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:TIGR00482 188 KQHGLY 193
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
1-166 6.74e-42

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 140.21  E-value: 6.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELLRSSAQMDGPdpsktpsasaalPELKLLCGADVLKTFQTPNL 80
Cdd:PLN02945   82 MCQLACEDSDFIMVDPWEARQSTYQRTLTVLARVETSLNNNGLASEES------------VRVMLLCGSDLLESFSTPGV 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKDTHIQEIVEKFGLVCVSRSGHDPERYISDSPILQQFQHNIHLAREPVLNEISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:PLN02945  150 WIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLVPNSISSTRVRECISRGLSVKYLTPDGVIDYI 229

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:PLN02945  230 KEHGLY 235
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
1-166 2.22e-27

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: 101.74  E-value: 2.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQ--WM-ETVKVLRHHHrellrssaqmdgpdpsktPSAsaalpELKLLCGADVLKTFQT 77
Cdd:COG1057    59 MLRLAIADNPRFEVSDIELERPGpsYTiDTLRELREEY------------------PDA-----ELYFIIGADALLQLPK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  78 pnlWKDthIQEIVEKFGLVCVSRSGHDPERYISDSPIlqQFQHNIHLAREPVLnEISATYVRKALGQGQSVKYLLPEAVI 157
Cdd:COG1057   116 ---WKR--WEELLELAHLVVVPRPGYELDELEELEAL--KPGGRIILLDVPLL-DISSTEIRERLAEGKSIRYLVPDAVE 187

                  ....*....
gi 1270533023 158 TYIRDQGLY 166
Cdd:COG1057   188 DYIREHGLY 196
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-166 1.24e-18

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 79.11  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQA--QWM-ETVKVLRHHHrellrssaqmdgpdpsktPSAsaalpELKLLCGADVLKTFQT 77
Cdd:PRK00071   61 MLELAIADNPRFSVSDIELERPgpSYTiDTLRELRARY------------------PDV-----ELVFIIGADALAQLPR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  78 pnlWKDthIQEIVEKFGLVCVSRSGHDPERyiSDSPILQQFQH---NIHLAREPVLnEISATYVRKALGQGQSVKYLLPE 154
Cdd:PRK00071  118 ---WKR--WEEILDLVHFVVVPRPGYPLEA--LALPALQQLLEaagAITLLDVPLL-AISSTAIRERIKEGRPIRYLLPE 189
                         170
                  ....*....|..
gi 1270533023 155 AVITYIRDQGLY 166
Cdd:PRK00071  190 AVLDYIEKHGLY 201
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
1-166 2.04e-18

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: 78.44  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023   1 MARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHRELlrssaqmdgpdpsktPSAsaalpELKLLCGADVLKTFQTpnl 80
Cdd:cd02165    55 MLKLAIEDNPKFEVSDIEIKRDGPSYTIDTLEELRERY---------------PNA-----ELYFIIGSDNLIRLPK--- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270533023  81 WKDthIQEIVEKFGLVCVSRSGHDPEryISDSPILQQFQHNIHLAREPVLNeISATYVRKALGQGQSVKYLLPEAVITYI 160
Cdd:cd02165   112 WYD--WEELLSLVHLVVAPRPGYPIE--DASLEKLLLPGGRIILLDNPLLN-ISSTEIRERLKNGKSIRYLLPPAVADYI 186

                  ....*.
gi 1270533023 161 RDQGLY 166
Cdd:cd02165   187 KEHGLY 192
 
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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