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Conserved domains on  [gi|1693805209|dbj|BBC11250|]
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Qns1 protein, partial [Tapinella sp. (in: Fungi)]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02339 super family cl31864
NAD+ synthase (glutamine-hydrolysing)
 1-72 3.48e-25

NAD+ synthase (glutamine-hydrolysing)


The actual alignment was detected with superfamily member PLN02339:

Pssm-ID: 177973 [Multi-domain]  Cd Length: 700  Bit Score: 96.29  E-value: 3.48e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693805209   1 LRRSRTQGYFVPLSGGVDSCATAVIVFSMCRLVVEAAGRGDKQVIADARRIVGEPEGSdyVPTDPREFCNRL 72
Cdd:PLN02339  343 LRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADGE--VPTDSKEFAKRI 412
 
Name Accession Description Interval E-value
PLN02339 PLN02339
NAD+ synthase (glutamine-hydrolysing)
 1-72 3.48e-25

NAD+ synthase (glutamine-hydrolysing)


Pssm-ID: 177973 [Multi-domain]  Cd Length: 700  Bit Score: 96.29  E-value: 3.48e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693805209   1 LRRSRTQGYFVPLSGGVDSCATAVIVFSMCRLVVEAAGRGDKQVIADARRIVGEPEGSdyVPTDPREFCNRL 72
Cdd:PLN02339  343 LRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADGE--VPTDSKEFAKRI 412
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 1-46 8.54e-09

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 49.48  E-value: 8.54e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1693805209   1 LRRSRTQGYFVPLSGGVDSCATAVIVFSMCrlvveaagrGDKQVIA 46
Cdd:cd00553    18 LRKSGAKGFVLGLSGGIDSAVVAALAVRAL---------GAENVLA 54
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 1-39 4.98e-03

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 33.28  E-value: 4.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1693805209   1 LRRSRTQGYFVPLSGGVDSCATAVivfsmcrLVVEAAGR 39
Cdd:COG0171   281 VRKNGFKGVVLGLSGGIDSALVAA-------LAVDALGP 312
 
Name Accession Description Interval E-value
PLN02339 PLN02339
NAD+ synthase (glutamine-hydrolysing)
 1-72 3.48e-25

NAD+ synthase (glutamine-hydrolysing)


Pssm-ID: 177973 [Multi-domain]  Cd Length: 700  Bit Score: 96.29  E-value: 3.48e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1693805209   1 LRRSRTQGYFVPLSGGVDSCATAVIVFSMCRLVVEAAGRGDKQVIADARRIVGEPEGSdyVPTDPREFCNRL 72
Cdd:PLN02339  343 LRRSGASGFLLPLSGGADSSSVAAIVGSMCQLVVKAIREGDEQVKADARRIGNYADGE--VPTDSKEFAKRI 412
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 1-46 8.54e-09

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 49.48  E-value: 8.54e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1693805209   1 LRRSRTQGYFVPLSGGVDSCATAVIVFSMCrlvveaagrGDKQVIA 46
Cdd:cd00553    18 LRKSGAKGFVLGLSGGIDSAVVAALAVRAL---------GAENVLA 54
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 1-39 4.98e-03

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 33.28  E-value: 4.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1693805209   1 LRRSRTQGYFVPLSGGVDSCATAVivfsmcrLVVEAAGR 39
Cdd:COG0171   281 VRKNGFKGVVLGLSGGIDSALVAA-------LAVDALGP 312
 
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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