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Conserved domains on  [gi|15236659|ref|NP_194120|]
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NAD(P)H-quinone oxidoreductase subunit S [Arabidopsis thaliana]

Protein Classification

NdhS domain-containing protein( domain architecture ID 10569217)

NdhS domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NdhS pfam11623
NAD(P)H dehydrogenase subunit S; This family is found in Bacteria and Streptophyta includes ...
169-220 1.64e-31

NAD(P)H dehydrogenase subunit S; This family is found in Bacteria and Streptophyta includes members such as NdhS (NAD(P)H-quinone oxidoreductase subunit S). NdhS, also known as CRR31 (chlororespiratory reduction 31), is a subunit of the chloroplast NADH dehydrogenase-like (NDH) complex. It is also a subunit of the cyanobacterial NDH-1 complex. NAD(P)H-oxidizing subunits have not been found in chloroplasts or cyanobacteria, where ferredoxin is probably the electron donor. NdhS contributes to the formation of a ferredoxin binding site of NDH and is necessary for high affinity binding of ferredoxin. The cyanobacterial NDH-1 complex, also known as NADPH:plastoquinone oxidoreductase or type I NAD(P)H dehydrogenase, is involved in plastoquinone reduction and cyclic electron transfer (CET) around photosystem I. The chloroplast NDH is more similar to cyanobacterial NDH-1, which is believed to be the origin of chloroplast NDH, than to mitochondrial NADH dehydrogenase present in the same species. The NDH complexes of chloroplasts, however, contain many subunits that are absent from cyanobacterial NDH-1 complexes.


:

Pssm-ID: 431964  Cd Length: 52  Bit Score: 110.45  E-value: 1.64e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15236659   169 LMPGMIAIVKNQNSPYHMYCGIVQRITDGKAGVLFEGGNWDRLITFRLEELE 220
Cdd:pfam11623   1 ILPGMTVKVKNPNDIYYGFEGQVQRVTDGKAAVLFEGGNWDKLVTFRLSELE 52
 
Name Accession Description Interval E-value
NdhS pfam11623
NAD(P)H dehydrogenase subunit S; This family is found in Bacteria and Streptophyta includes ...
169-220 1.64e-31

NAD(P)H dehydrogenase subunit S; This family is found in Bacteria and Streptophyta includes members such as NdhS (NAD(P)H-quinone oxidoreductase subunit S). NdhS, also known as CRR31 (chlororespiratory reduction 31), is a subunit of the chloroplast NADH dehydrogenase-like (NDH) complex. It is also a subunit of the cyanobacterial NDH-1 complex. NAD(P)H-oxidizing subunits have not been found in chloroplasts or cyanobacteria, where ferredoxin is probably the electron donor. NdhS contributes to the formation of a ferredoxin binding site of NDH and is necessary for high affinity binding of ferredoxin. The cyanobacterial NDH-1 complex, also known as NADPH:plastoquinone oxidoreductase or type I NAD(P)H dehydrogenase, is involved in plastoquinone reduction and cyclic electron transfer (CET) around photosystem I. The chloroplast NDH is more similar to cyanobacterial NDH-1, which is believed to be the origin of chloroplast NDH, than to mitochondrial NADH dehydrogenase present in the same species. The NDH complexes of chloroplasts, however, contain many subunits that are absent from cyanobacterial NDH-1 complexes.


Pssm-ID: 431964  Cd Length: 52  Bit Score: 110.45  E-value: 1.64e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15236659   169 LMPGMIAIVKNQNSPYHMYCGIVQRITDGKAGVLFEGGNWDRLITFRLEELE 220
Cdd:pfam11623   1 ILPGMTVKVKNPNDIYYGFEGQVQRVTDGKAAVLFEGGNWDKLVTFRLSELE 52
NdhS COG5790
NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific subunit S (CRR31) [Energy production ...
169-220 1.10e-22

NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific subunit S (CRR31) [Energy production and conversion];


Pssm-ID: 444500  Cd Length: 59  Bit Score: 87.77  E-value: 1.10e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15236659 169 LMPGMIAIVKNQNSPYHMYCGIVQRITDGKAGVLFEGGNWDRLITFRLEELE 220
Cdd:COG5790   1 ILPGSTVKVINPDDTYYGFEGLVQRVSDGKVAVLFEGGNWDKLVTFRLSELE 52
 
Name Accession Description Interval E-value
NdhS pfam11623
NAD(P)H dehydrogenase subunit S; This family is found in Bacteria and Streptophyta includes ...
169-220 1.64e-31

NAD(P)H dehydrogenase subunit S; This family is found in Bacteria and Streptophyta includes members such as NdhS (NAD(P)H-quinone oxidoreductase subunit S). NdhS, also known as CRR31 (chlororespiratory reduction 31), is a subunit of the chloroplast NADH dehydrogenase-like (NDH) complex. It is also a subunit of the cyanobacterial NDH-1 complex. NAD(P)H-oxidizing subunits have not been found in chloroplasts or cyanobacteria, where ferredoxin is probably the electron donor. NdhS contributes to the formation of a ferredoxin binding site of NDH and is necessary for high affinity binding of ferredoxin. The cyanobacterial NDH-1 complex, also known as NADPH:plastoquinone oxidoreductase or type I NAD(P)H dehydrogenase, is involved in plastoquinone reduction and cyclic electron transfer (CET) around photosystem I. The chloroplast NDH is more similar to cyanobacterial NDH-1, which is believed to be the origin of chloroplast NDH, than to mitochondrial NADH dehydrogenase present in the same species. The NDH complexes of chloroplasts, however, contain many subunits that are absent from cyanobacterial NDH-1 complexes.


Pssm-ID: 431964  Cd Length: 52  Bit Score: 110.45  E-value: 1.64e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15236659   169 LMPGMIAIVKNQNSPYHMYCGIVQRITDGKAGVLFEGGNWDRLITFRLEELE 220
Cdd:pfam11623   1 ILPGMTVKVKNPNDIYYGFEGQVQRVTDGKAAVLFEGGNWDKLVTFRLSELE 52
NdhS COG5790
NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific subunit S (CRR31) [Energy production ...
169-220 1.10e-22

NAD(P)H dehydrogenase cyanobacteria/chloroplast-specific subunit S (CRR31) [Energy production and conversion];


Pssm-ID: 444500  Cd Length: 59  Bit Score: 87.77  E-value: 1.10e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15236659 169 LMPGMIAIVKNQNSPYHMYCGIVQRITDGKAGVLFEGGNWDRLITFRLEELE 220
Cdd:COG5790   1 ILPGSTVKVINPDDTYYGFEGLVQRVSDGKVAVLFEGGNWDKLVTFRLSELE 52
 
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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