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Conserved domains on  [gi|917632671|gb|AIM64573|]
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putative nicotinate-nucleotide adenylyltransferase [Weissella ceti]

Protein Classification

nicotinate-nicotinamide nucleotide adenylyltransferase( domain architecture ID 10003000)

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

CATH:  3.40.50.620
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 COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 16-202 3.08e-91

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: 265.45  E-value: 3.08e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  16 RKRVGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRG 95
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  96 GKSYTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEAPY---------PVQWVDVPQ 166
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEelealkpggRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 917632671 167 LEISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 16-202 3.08e-91

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: 265.45  E-value: 3.08e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  16 RKRVGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRG 95
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  96 GKSYTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEAPY---------PVQWVDVPQ 166
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEelealkpggRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 917632671 167 LEISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
14-202 2.99e-88

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 258.23  E-value: 2.99e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  14 APRKRVGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQ 93
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  94 RGGKSYTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEA------------PYPVQW 161
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 917632671 162 VDVPQLEISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLY 201
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 19-202 6.41e-73

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: 219.04  E-value: 6.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  19 VGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAiDPLERAAMVQAAVHDNHLFALEMLEIQRGGKS 98
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPA-SFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  99 YTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEAPYP---------VQWVDVPQLEI 169
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 917632671 170 SSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 21-202 5.08e-60

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: 186.37  E-value: 5.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671   21 ILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRGGKSYT 100
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  101 YDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEAPYPVQW-----------VDVPQLEI 169
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmhhgnltlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 917632671  170 SSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 21-177 5.70e-27

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: 99.70  E-value: 5.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671   21 ILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRggksyt 100
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917632671  101 ydsiIALREQNPDtdfYFIIGGDevAYLPTWYRIDELINLVHFVGVNRPGVVkeapypvqWVDVPQLEISSTEIRQR 177
Cdd:pfam01467  75 ----ELLKELNPD---VLVIGAD--SLLDFWYELDEILGNVKLVVVVRPVFF--------IPLKPTNGISSTDIRER 134
 
Name Accession Description Interval E-value
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 16-202 3.08e-91

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: 265.45  E-value: 3.08e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  16 RKRVGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRG 95
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLGLDEVIFVPAGQPPHKKHKPLASAEHRLAMLRLAIADNPRFEVSDIELERP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  96 GKSYTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEAPY---------PVQWVDVPQ 166
Cdd:COG1057   81 GPSYTIDTLRELREEYPDAELYFIIGADALLQLPKWKRWEELLELAHLVVVPRPGYELDELEelealkpggRIILLDVPL 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 917632671 167 LEISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:COG1057  161 LDISSTEIRERLAEGKSIRYLVPDAVEDYIREHGLY 196
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
14-202 2.99e-88

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 258.23  E-value: 2.99e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  14 APRKRVGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQ 93
Cdd:PRK00071   1 EMMKRIGLFGGTFDPPHYGHLAIAEEAAERLGLDEVWFLPNPGPPHKPQKPLAPLEHRLAMLELAIADNPRFSVSDIELE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  94 RGGKSYTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEA------------PYPVQW 161
Cdd:PRK00071  81 RPGPSYTIDTLRELRARYPDVELVFIIGADALAQLPRWKRWEEILDLVHFVVVPRPGYPLEAlalpalqqlleaAGAITL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 917632671 162 VDVPQLEISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:PRK00071 161 LDVPLLAISSTAIRERIKEGRPIRYLLPEAVLDYIEKHGLY 201
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 19-202 6.41e-73

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: 219.04  E-value: 6.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  19 VGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAiDPLERAAMVQAAVHDNHLFALEMLEIQRGGKS 98
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELGLDRVLLLPSANPPHKPPKPA-SFEHRLEMLKLAIEDNPKFEVSDIEIKRDGPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  99 YTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEAPYP---------VQWVDVPQLEI 169
Cdd:cd02165   80 YTIDTLEELRERYPNAELYFIIGSDNLIRLPKWYDWEELLSLVHLVVAPRPGYPIEDASLeklllpggrIILLDNPLLNI 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 917632671 170 SSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:cd02165  160 SSTEIRERLKNGKSIRYLLPPAVADYIKEHGLY 192
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 21-202 5.08e-60

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: 186.37  E-value: 5.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671   21 ILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRGGKSYT 100
Cdd:TIGR00482   1 LFGGSFDPIHYGHLLLAEEALDHLDLDKVIFVPTANPPHKKTYEAASSHHRLAMLKLAIEDNPKFEVDDFEIKRGGPSYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  101 YDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKEAPYPVQW-----------VDVPQLEI 169
Cdd:TIGR00482  81 IDTLKHLKKKYPDVELYFIIGADALRSFPLWKDWQELLELVHLVIVPRPGYTLDKALLEKAilrmhhgnltlLHNPRVPI 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 917632671  170 SSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:TIGR00482 161 SSTEIRQRIRQGKSIEYLLPDPVIKYIKQHGLY 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
17-205 3.90e-37

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 131.99  E-value: 3.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  17 KRVGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRGG 96
Cdd:PRK07152   1 MKIAIFGGSFDPIHKGHINIAKKAIKKLKLDKLFFVPTYINPFKKKQKASNGEHRLNMLKLALKNLPKMEVSDFEIKRQN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  97 KSYTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGVVKE---APYPVQWVDVPQLEISSTE 173
Cdd:PRK07152  81 VSYTIDTIKYFKKKYPNDEIYFIIGSDNLEKFKKWKNIEEILKKVQIVVFKRKKNINKknlKKYNVLLLKNKNLNISSTK 160

                        170       180       190
                 ....*....|....*....|....*....|..
gi 917632671 174 IRQRVAKHnsiryMVPDMVAAYIFKKGLYLDE 205
Cdd:PRK07152 161 IRKGNLLG-----KLDPKVNDYINENFLYLED 187
PRK06973 PRK06973
nicotinate-nucleotide adenylyltransferase;
4-202 5.13e-30

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 180781 [Multi-domain]  Cd Length: 243  Bit Score: 111.03  E-value: 5.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671   4 QVKTQTTVQTAPR-KRVGILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHvdtKVAIDPLE-RAAMVQAAVHD 81
Cdd:PRK06973   8 PTPNAEPAPPLARpRRIGILGGTFDPIHDGHLALARRFADVLDLTELVLIPAGQPWQ---KADVSAAEhRLAMTRAAAAS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  82 NHLFALEM----LEIQRGGKSYTYDSIIALREQ-NPDTDFYFIIGGDEVAYLPTWYRIDELINLVHFVGVNRPGV-VKEA 155
Cdd:PRK06973  85 LVLPGVTVrvatDEIEHAGPTYTVDTLARWRERiGPDASLALLIGADQLVRLDTWRDWRRLFDYAHLCAATRPGFdLGAA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917632671 156 PYPVQ---------------------WVDVP-QLEISSTEIRQRVAKHNSIRYMVPDM--------VAAYIFKKGLY 202
Cdd:PRK06973 165 SPAVAaeiaarqadadvlqatpaghlLIDTTlAFDLSATDIRAHLRACIARRAQVPDAsaehvpaaVWAYILQHRLY 241
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 21-177 5.70e-27

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: 99.70  E-value: 5.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671   21 ILGGTFNPPHLGHLMIGEQVVHQLQLDEVRFMPNALPPHVDTKVAIDPLERAAMVQAAVHDNHLFALEMLEIQRggksyt 100
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDEDLIVGVPSDEPPHKLKRPLFSAEERLEMLELAKWVDEVIVVAPWELTR------ 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 917632671  101 ydsiIALREQNPDtdfYFIIGGDevAYLPTWYRIDELINLVHFVGVNRPGVVkeapypvqWVDVPQLEISSTEIRQR 177
Cdd:pfam01467  75 ----ELLKELNPD---VLVIGAD--SLLDFWYELDEILGNVKLVVVVRPVFF--------IPLKPTNGISSTDIRER 134
PRK08887 PRK08887
nicotinate-nicotinamide nucleotide adenylyltransferase;
17-202 3.12e-16

nicotinate-nicotinamide nucleotide adenylyltransferase;


Pssm-ID: 181576 [Multi-domain]  Cd Length: 174  Bit Score: 72.84  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  17 KRVGILGGTFNPPHLGHLMIGEQVVHqlqLDEVRFMPNAlpPHVDTKVAIDPLERAAMVQAAVHDNHLFALEM----LEI 92
Cdd:PRK08887   2 KKIAVFGSAFNPPSLGHKSVIESLSH---FDLVLLVPSI--AHAWGKTMLDYETRCQLVDAFIQDLGLSNVQRsdieQEL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  93 QRGGKS-YTYDSIIALREQNPDTDFYFIIGGDEVAYLPTWYRIDELINlvhfvgvnrpgvvkeapypvQW--VDVPQ-LE 168
Cdd:PRK08887  77 YAPDESvTTYALLTRLQELYPEADLTFVIGPDNFLKFAKFYKADEITQ--------------------RWtvMACPEkVP 136

                        170       180       190
                 ....*....|....*....|....*....|....
gi 917632671 169 ISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:PRK08887 137 IRSTDIRNALQNGKDISHLTTPGVARLLKEHQLY 170
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 19-177 1.65e-12

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: 62.46  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  19 VGILGGTFNPPHLGHLMIGEQVVHQLqLDEVRFMP-NALPPHVDTKVAIDPLERAAMVQAAVhdNHLFALEMLEIQRGGK 97
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEA-LDEVIIIIvSNPPKKKRNKDPFSLHERVEMLKEIL--KDRLKVVPVDFPEVKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 917632671  98 SYTYDSIIALREQNPDTdfYFIIGGDEVAYLPTWY--RIDELINLVHFVGVNRPGvvkeapypvqwvdvPQLEISSTEIR 175
Cdd:cd02039   78 LLAVVFILKILLKVGPD--KVVVGEDFAFGKNASYnkDLKELFLDIEIVEVPRVR--------------DGKKISSTLIR 141


                 ..
gi 917632671 176 QR 177
Cdd:cd02039  142 EL 143
NMNAT_Eukarya cd09286
Nicotinamide/nicotinate mononucleotide adenylyltransferase, Eukaryotic; Nicotinamide ...
 160-202 1.09e-05

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: 44.60  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 917632671 160 QWVdvpQLEISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:cd09286  186 DWI---PNDISSTKVRRALRRGMSVKYLLPDPVIEYIEQHQLY 225
PLN02945 PLN02945
nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase
 169-202 1.78e-05

nicotinamide-nucleotide adenylyltransferase/nicotinate-nucleotide adenylyltransferase


Pssm-ID: 178531 [Multi-domain]  Cd Length: 236  Bit Score: 43.91  E-value: 1.78e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 917632671 169 ISSTEIRQRVAKHNSIRYMVPDMVAAYIFKKGLY 202
Cdd:PLN02945 202 ISSTRVRECISRGLSVKYLTPDGVIDYIKEHGLY 235
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 19-79 4.42e-03

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: 34.59  E-value: 4.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 917632671   19 VGILGGTFNPPHLGHLMIGEQVvhqLQL-DEVR---FMPNALPPHvDTKVAIDPLERAAMVQAAV 79
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERA---KELfDELIvgvGSDQFVNPL-KGEPVFSLEERLEMLKALK 61
 
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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