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Conserved domains on  [gi|31414737|gb|AAP50913|]
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pyridine nucleotide transhydrogenase, partial [Entamoeba dispar]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PNTB super family cl22917
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ...
1-145 1.59e-81

NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.


The actual alignment was detected with superfamily member pfam02233:

Pssm-ID: 473992  Cd Length: 454  Bit Score: 246.97  E-value: 1.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31414737     1 GGADMPVVVSMLNSYSGWATAASGFLLNNYAMIVGGALIGSSGAILSYIMCKAMNRSFLSVIFGGFGATPTVTSKHDDEG 80
Cdd:pfam02233 201 GGADMPVVISLLNSYSGWAAAAAGFVLGNPLLIIAGALVGASGAILTYIMCKAMNRSLTNVLFGGFGAAASAGAAGAAAA 280
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31414737    81 PREANPIQTQELAKLLIDAQNIAIVPGYGMAVAKAQHVVADLADQLIKSGKKVRFIIHPVAGRFP 145
Cdd:pfam02233 281 DGEVKEISAEDAAELLAYASSVIIVPGYGMAVAQAQHAVAELADLLEERGVEVRFAIHPVAGRMP 345
 
Name Accession Description Interval E-value
PNTB pfam02233
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ...
1-145 1.59e-81

NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.


Pssm-ID: 460502  Cd Length: 454  Bit Score: 246.97  E-value: 1.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31414737     1 GGADMPVVVSMLNSYSGWATAASGFLLNNYAMIVGGALIGSSGAILSYIMCKAMNRSFLSVIFGGFGATPTVTSKHDDEG 80
Cdd:pfam02233 201 GGADMPVVISLLNSYSGWAAAAAGFVLGNPLLIIAGALVGASGAILTYIMCKAMNRSLTNVLFGGFGAAASAGAAGAAAA 280
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31414737    81 PREANPIQTQELAKLLIDAQNIAIVPGYGMAVAKAQHVVADLADQLIKSGKKVRFIIHPVAGRFP 145
Cdd:pfam02233 281 DGEVKEISAEDAAELLAYASSVIIVPGYGMAVAQAQHAVAELADLLEERGVEVRFAIHPVAGRMP 345
PntB COG1282
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
1-145 5.08e-80

NAD/NADP transhydrogenase beta subunit [Energy production and conversion];


Pssm-ID: 440893  Cd Length: 458  Bit Score: 243.06  E-value: 5.08e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31414737   1 GGADMPVVVSMLNSYSGWATAASGFLLNNYAMIVGGALIGSSGAILSYIMCKAMNRSFLSVIFGGFGATPTVTSkhDDEG 80
Cdd:COG1282 206 GGADMPVVISLLNSYSGLAAAAAGFVLGNDLLIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAA--GAAE 283
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31414737  81 PREANPIQTQELAKLLIDAQNIAIVPGYGMAVAKAQHVVADLADQLIKSGKKVRFIIHPVAGRFP 145
Cdd:COG1282 284 QGEVKEISAEDAAILLAYASSVIIVPGYGMAVAQAQHAVRELADLLEERGVEVKFAIHPVAGRMP 348
pntB PRK09444
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
1-145 2.43e-69

Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;


Pssm-ID: 236520  Cd Length: 462  Bit Score: 215.73  E-value: 2.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31414737    1 GGADMPVVVSMLNSYSGWATAASGFLLNNYAMIVGGALIGSSGAILSYIMCKAMNRSFLSVIFGGFGATPTVTSKHDDEG 80
Cdd:PRK09444 210 GGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIVTGALVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGSSTGDDEEVG 289
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31414737   81 -PREANPiqtQELAKLLIDAQNIAIVPGYGMAVAKAQHVVADLADQLIKSGKKVRFIIHPVAGRFP 145
Cdd:PRK09444 290 eHRETTA---EEVAEMLKNSHSVIITPGYGMAVAQAQYPVAEITEKLRARGINVRFGIHPVAGRLP 352
 
Name Accession Description Interval E-value
PNTB pfam02233
NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP ...
1-145 1.59e-81

NAD(P) transhydrogenase beta subunit; This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.


Pssm-ID: 460502  Cd Length: 454  Bit Score: 246.97  E-value: 1.59e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31414737     1 GGADMPVVVSMLNSYSGWATAASGFLLNNYAMIVGGALIGSSGAILSYIMCKAMNRSFLSVIFGGFGATPTVTSKHDDEG 80
Cdd:pfam02233 201 GGADMPVVISLLNSYSGWAAAAAGFVLGNPLLIIAGALVGASGAILTYIMCKAMNRSLTNVLFGGFGAAASAGAAGAAAA 280
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31414737    81 PREANPIQTQELAKLLIDAQNIAIVPGYGMAVAKAQHVVADLADQLIKSGKKVRFIIHPVAGRFP 145
Cdd:pfam02233 281 DGEVKEISAEDAAELLAYASSVIIVPGYGMAVAQAQHAVAELADLLEERGVEVRFAIHPVAGRMP 345
PntB COG1282
NAD/NADP transhydrogenase beta subunit [Energy production and conversion];
1-145 5.08e-80

NAD/NADP transhydrogenase beta subunit [Energy production and conversion];


Pssm-ID: 440893  Cd Length: 458  Bit Score: 243.06  E-value: 5.08e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31414737   1 GGADMPVVVSMLNSYSGWATAASGFLLNNYAMIVGGALIGSSGAILSYIMCKAMNRSFLSVIFGGFGATPTVTSkhDDEG 80
Cdd:COG1282 206 GGADMPVVISLLNSYSGLAAAAAGFVLGNDLLIIAGALVGASGAILTYIMCKAMNRSLINVLFGGFGGGGAAAA--GAAE 283
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31414737  81 PREANPIQTQELAKLLIDAQNIAIVPGYGMAVAKAQHVVADLADQLIKSGKKVRFIIHPVAGRFP 145
Cdd:COG1282 284 QGEVKEISAEDAAILLAYASSVIIVPGYGMAVAQAQHAVRELADLLEERGVEVKFAIHPVAGRMP 348
pntB PRK09444
Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;
1-145 2.43e-69

Re/Si-specific NAD(P)(+) transhydrogenase subunit beta;


Pssm-ID: 236520  Cd Length: 462  Bit Score: 215.73  E-value: 2.43e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31414737    1 GGADMPVVVSMLNSYSGWATAASGFLLNNYAMIVGGALIGSSGAILSYIMCKAMNRSFLSVIFGGFGATPTVTSKHDDEG 80
Cdd:PRK09444 210 GGADMPVVVSMLNSYSGWAAAAAGFMLSNDLLIVTGALVGSSGAILSYIMCKAMNRSFISVIAGGFGTDGSSTGDDEEVG 289
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31414737   81 -PREANPiqtQELAKLLIDAQNIAIVPGYGMAVAKAQHVVADLADQLIKSGKKVRFIIHPVAGRFP 145
Cdd:PRK09444 290 eHRETTA---EEVAEMLKNSHSVIITPGYGMAVAQAQYPVAEITEKLRARGINVRFGIHPVAGRLP 352
 
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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