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Conserved domains on  [gi|1958775808|ref|XP_038965630|]
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nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 isoform X4 [Rattus norvegicus]

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 ...
1-187 6.73e-85

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: 251.07  E-value: 6.73e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWESLQKEWVETVKVLRHHQEKLATGSrshpqsspvlerpgrkrkwadqKQDSSPQKPQEPKPTG 80
Cdd:cd09286    61 MCRLAVQSSDWIRVDDWESLQPEWMRTAKVLRHHREEINNKY----------------------GGIEGAAKRVLDGSRR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  81 VPRVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVTEWITNDISSTKIR 160
Cdd:cd09286   119 EVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDWIPNDISSTKVR 198
                         170       180
                  ....*....|....*....|....*..
gi 1958775808 161 RALRRGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:cd09286   199 RALRRGMSVKYLLPDPVIEYIEQHQLY 225
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
1-187 6.73e-85

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: 251.07  E-value: 6.73e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWESLQKEWVETVKVLRHHQEKLATGSrshpqsspvlerpgrkrkwadqKQDSSPQKPQEPKPTG 80
Cdd:cd09286    61 MCRLAVQSSDWIRVDDWESLQPEWMRTAKVLRHHREEINNKY----------------------GGIEGAAKRVLDGSRR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  81 VPRVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVTEWITNDISSTKIR 160
Cdd:cd09286   119 EVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDWIPNDISSTKVR 198
                         170       180
                  ....*....|....*....|....*..
gi 1958775808 161 RALRRGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:cd09286   199 RALRRGMSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
1-188 2.12e-44

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 148.30  E-value: 2.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWESLQKEWVETVKVLRhhqeklatgsrshpqsspvleRPgrkrkwaDQKQDSSPQKPQEPkptg 80
Cdd:PLN02945   82 MCQLACEDSDFIMVDPWEARQSTYQRTLTVLA---------------------RV-------ETSLNNNGLASEES---- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  81 vPRVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVTEWITNDISSTKIR 160
Cdd:PLN02945  130 -VRVMLLCGSDLLESFSTPGVWIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLVPNSISSTRVR 208
                         170       180
                  ....*....|....*....|....*...
gi 1958775808 161 RALRRGQSIRYLVPDLVQEYIEEHDLYN 188
Cdd:PLN02945  209 ECISRGLSVKYLTPDGVIDYIKEHGLYM 236
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
1-187 1.49e-35

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: 123.97  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWESLQKEWVETVKVLRHHQEKlatgsrsHPQSspvlerpgrkrkwadqkqdsspqkpqepkptg 80
Cdd:TIGR00482  54 MLKLAIEDNPKFEVDDFEIKRGGPSYTIDTLKHLKKK-------YPDV-------------------------------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  81 vpRVKLLCGADLLESFSvpnLWKmeDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVtEWITNDISSTKIR 160
Cdd:TIGR00482  95 --ELYFIIGADALRSFP---LWK--DWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTLL-HNPRVPISSTEIR 166
                         170       180
                  ....*....|....*....|....*..
gi 1958775808 161 RALRRGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:TIGR00482 167 QRIRQGKSIEYLLPDPVIKYIKQHGLY 193
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
1-187 1.62e-22

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: 90.18  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWEsLQKEW----VETVKVLRHHqeklatgsrsHPQSSPVLerpgrkrkwadqkqdsspqkpqep 76
Cdd:COG1057    59 MLRLAIADNPRFEVSDIE-LERPGpsytIDTLRELREE----------YPDAELYF------------------------ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  77 kptgvprvklLCGADLLESFSvpnLWKmeDITQIVANFGLICVTRAGSDAQKFIYESDvlWRHQSNIHLVtEWITNDISS 156
Cdd:COG1057   104 ----------IIGADALLQLP---KWK--RWEELLELAHLVVVPRPGYELDELEELEA--LKPGGRIILL-DVPLLDISS 165
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958775808 157 TKIRRALRRGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:COG1057   166 TEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
 
Name Accession Description Interval E-value
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
1-187 6.73e-85

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: 251.07  E-value: 6.73e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWESLQKEWVETVKVLRHHQEKLATGSrshpqsspvlerpgrkrkwadqKQDSSPQKPQEPKPTG 80
Cdd:cd09286    61 MCRLAVQSSDWIRVDDWESLQPEWMRTAKVLRHHREEINNKY----------------------GGIEGAAKRVLDGSRR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  81 VPRVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVTEWITNDISSTKIR 160
Cdd:cd09286   119 EVKIMLLCGADLLESFGIPGLWKDADLEEILGEFGLVVVERTGSDPENFIASSDILRKYQDNIHLVKDWIPNDISSTKVR 198
                         170       180
                  ....*....|....*....|....*..
gi 1958775808 161 RALRRGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:cd09286   199 RALRRGMSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
1-188 2.12e-44

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 148.30  E-value: 2.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWESLQKEWVETVKVLRhhqeklatgsrshpqsspvleRPgrkrkwaDQKQDSSPQKPQEPkptg 80
Cdd:PLN02945   82 MCQLACEDSDFIMVDPWEARQSTYQRTLTVLA---------------------RV-------ETSLNNNGLASEES---- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  81 vPRVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVTEWITNDISSTKIR 160
Cdd:PLN02945  130 -VRVMLLCGSDLLESFSTPGVWIPDQVRTICRDYGVVCIRREGQDVEKLVSQDEILNENRGNILVVDDLVPNSISSTRVR 208
                         170       180
                  ....*....|....*....|....*...
gi 1958775808 161 RALRRGQSIRYLVPDLVQEYIEEHDLYN 188
Cdd:PLN02945  209 ECISRGLSVKYLTPDGVIDYIKEHGLYM 236
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
1-187 1.49e-35

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: 123.97  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWESLQKEWVETVKVLRHHQEKlatgsrsHPQSspvlerpgrkrkwadqkqdsspqkpqepkptg 80
Cdd:TIGR00482  54 MLKLAIEDNPKFEVDDFEIKRGGPSYTIDTLKHLKKK-------YPDV-------------------------------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  81 vpRVKLLCGADLLESFSvpnLWKmeDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQSNIHLVtEWITNDISSTKIR 160
Cdd:TIGR00482  95 --ELYFIIGADALRSFP---LWK--DWQELLELVHLVIVPRPGYTLDKALLEKAILRMHHGNLTLL-HNPRVPISSTEIR 166
                         170       180
                  ....*....|....*....|....*..
gi 1958775808 161 RALRRGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:TIGR00482 167 QRIRQGKSIEYLLPDPVIKYIKQHGLY 193
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
1-187 1.62e-22

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: 90.18  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808   1 MAELATKNSHWVEVDTWEsLQKEW----VETVKVLRHHqeklatgsrsHPQSSPVLerpgrkrkwadqkqdsspqkpqep 76
Cdd:COG1057    59 MLRLAIADNPRFEVSDIE-LERPGpsytIDTLRELREE----------YPDAELYF------------------------ 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  77 kptgvprvklLCGADLLESFSvpnLWKmeDITQIVANFGLICVTRAGSDAQKFIYESDvlWRHQSNIHLVtEWITNDISS 156
Cdd:COG1057   104 ----------IIGADALLQLP---KWK--RWEELLELAHLVVVPRPGYELDELEELEA--LKPGGRIILL-DVPLLDISS 165
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958775808 157 TKIRRALRRGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:COG1057   166 TEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
86-187 1.28e-15

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: 71.89  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  86 LLCGADLLESFSVpnlWKmeDITQIVANFGLICVTRAGSDAQKfiYESDVLWRHQSNIHLV-TEWItnDISSTKIRRALR 164
Cdd:cd02165    99 FIIGSDNLIRLPK---WY--DWEELLSLVHLVVAPRPGYPIED--ASLEKLLLPGGRIILLdNPLL--NISSTEIRERLK 169
                          90       100
                  ....*....|....*....|...
gi 1958775808 165 RGQSIRYLVPDLVQEYIEEHDLY 187
Cdd:cd02165   170 NGKSIRYLLPPAVADYIKEHGLY 192
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
89-187 5.46e-15

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 70.63  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  89 GADLLESFsvPNlWKmeDITQIVANFGLICVTRAGSDAQKFIYESDVLWRHQS-NIHLVteWIT-NDISSTKIRRALRRG 166
Cdd:PRK00071  108 GADALAQL--PR-WK--RWEEILDLVHFVVVPRPGYPLEALALPALQQLLEAAgAITLL--DVPlLAISSTAIRERIKEG 180
                          90       100
                  ....*....|....*....|.
gi 1958775808 167 QSIRYLVPDLVQEYIEEHDLY 187
Cdd:PRK00071  181 RPIRYLLPEAVLDYIEKHGLY 201
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
86-187 1.18e-05

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 44.94  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958775808  86 LLCGADLLESFsvpNLWKmeDITQIVANFGLICVTRAGsdaqkfIYESDVLWRHqsNIHLVTEWItNDISSTKIRRALRR 165
Cdd:PRK07152  102 FIIGSDNLEKF---KKWK--NIEEILKKVQIVVFKRKK------NINKKNLKKY--NVLLLKNKN-LNISSTKIRKGNLL 167
                          90       100
                  ....*....|....*....|..
gi 1958775808 166 GQsirylVPDLVQEYIEEHDLY 187
Cdd:PRK07152  168 GK-----LDPKVNDYINENFLY 184
NadR COG1056
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ...
152-183 1.40e-04

Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440676 [Multi-domain]  Cd Length: 162  Bit Score: 40.95  E-value: 1.40e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958775808 152 NDISSTKIRRALRRGQSIRYLVPDLVQEYIEE 183
Cdd:COG1056   125 EEYSGTEIRRLMLEGEDWESLVPPAVAEVIEE 156
 
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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