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Conserved domains on  [gi|2459390574|ref|NP_001405032|]
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nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 isoform 3 [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 ...
 60-181 8.79e-55

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: 173.26  E-value: 8.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  60 NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDD 139
Cdd:cd09286   108 AAKRVLDGSRREVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDW 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2459390574 140 INHpmsVVSSTKSRLALQHGdGHVVDYLSQPVIDYILKSQLY 181
Cdd:cd09286   188 IPN---DISSTKVRRALRRG-MSVKYLLPDPVIEYIEQHQLY 225
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 60-181 8.79e-55

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: 173.26  E-value: 8.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  60 NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDD 139
Cdd:cd09286   108 AAKRVLDGSRREVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDW 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2459390574 140 INHpmsVVSSTKSRLALQHGdGHVVDYLSQPVIDYILKSQLY 181
Cdd:cd09286   188 IPN---DISSTKVRRALRRG-MSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 72-181 2.66e-23

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 92.44  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  72 LRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDInhPMSvVSSTK 151
Cdd:PLN02945  130 VRVMLLCGSDLLESFSTPGVWIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLV--PNS-ISSTR 206

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2459390574 152 SRLALQHGDGhvVDYL-SQPVIDYILKSQLY 181
Cdd:PLN02945  207 VRECISRGLS--VKYLtPDGVIDYIKEHGLY 235
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 60-181 8.79e-55

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: 173.26  E-value: 8.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  60 NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDD 139
Cdd:cd09286   108 AAKRVLDGSRREVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDW 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2459390574 140 INHpmsVVSSTKSRLALQHGdGHVVDYLSQPVIDYILKSQLY 181
Cdd:cd09286   188 IPN---DISSTKVRRALRRG-MSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 72-181 2.66e-23

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 92.44  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  72 LRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDInhPMSvVSSTK 151
Cdd:PLN02945  130 VRVMLLCGSDLLESFSTPGVWIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLV--PNS-ISSTR 206

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2459390574 152 SRLALQHGDGhvVDYL-SQPVIDYILKSQLY 181
Cdd:PLN02945  207 VRECISRGLS--VKYLtPDGVIDYIKEHGLY 235
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
79-181 2.18e-05

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 43.28  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  79 GSDLLESFciPGlWNEADMevIVGDFGIVVVPRDAADTDRIMNHS-SILRKYKNNIMVVkddiNHPMSVVSSTKSRLALQ 157
Cdd:PRK00071  108 GADALAQL--PR-WKRWEE--ILDLVHFVVVPRPGYPLEALALPAlQQLLEAAGAITLL----DVPLLAISSTAIRERIK 178

                          90       100
                  ....*....|....*....|....
gi 2459390574 158 HGdGHVVDYLSQPVIDYILKSQLY 181
Cdd:PRK00071  179 EG-RPIRYLLPEAVLDYIEKHGLY 201
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 73-181 2.68e-05

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: 43.00  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  73 RILLLCGSDLLESFCIpglWNEADMevIVGDFGIVVVPRDAADtdriMNHSSILRKYKNNIMVVKDDINHPmsVVSSTKS 152
Cdd:cd02165    96 ELYFIIGSDNLIRLPK---WYDWEE--LLSLVHLVVAPRPGYP----IEDASLEKLLLPGGRIILLDNPLL--NISSTEI 164

                          90       100
                  ....*....|....*....|....*....
gi 2459390574 153 RLALQHGDGhVVDYLSQPVIDYILKSQLY 181
Cdd:cd02165   165 RERLKNGKS-IRYLLPPAVADYIKEHGLY 192
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
66-183 1.38e-04

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 41.47  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2459390574  66 RYEEIElrILLLCGSDLLESFcipGLWNEADMevIVGDFGIVVVPRDAadtdrimNHSSI-LRKYknNIMVVKDDINHpm 144
Cdd:PRK07152   94 KYPNDE--IYFIIGSDNLEKF---KKWKNIEE--ILKKVQIVVFKRKK-------NINKKnLKKY--NVLLLKNKNLN-- 155

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2459390574 145 svVSSTKSRlalqhgDGHVVDYLSQPVIDYILKSQLYIN 183
Cdd:PRK07152  156 --ISSTKIR------KGNLLGKLDPKVNDYINENFLYLE 186
 
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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