NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|10764847|ref|NP_004137|]
View 

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 [Homo sapiens]

Protein Classification

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7( domain architecture ID 10529369)

NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7 is an accessory subunit, not involved in catalysis, of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that functions in the transfer of electrons from NADH to the respiratory chain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
NDUF_B7 pfam05676
NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7); This family consists of several ...
41-102 1.03e-28

NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7); This family consists of several NADH-ubiquinone oxidoreductase B18 subunit proteins from different eukaryotic organizms. Oxidative phosphorylation is the well-characterized process in which ATP, the principal carrier of chemical energy of individual cells, is produced due to a mitochondrial proton gradient formed by the transfer of electrons from NADH and FADH2 to molecular oxygen. The oxidative phosphorylation (OXPHOS) system is located in the mitochondrial inner membrane and consists of five multi-subunit enzyme complexes and two small electron carriers: coenzyme Q10 and cytochrome C. At least 70 structural proteins involved in the formation of the whole OXPHOS system are encoded by nuclear genes, whereas 13 structural proteins are encoded by the mitochondrial genome. Deficiency of NADH ubiquinone oxidoreductase, the first enzyme complex of the mitochondrial respiratory chain, is one of the most frequent causes of human mitochondrial encephalomyopathies.


:

Pssm-ID: 461710  Cd Length: 62  Bit Score: 99.57  E-value: 1.03e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10764847    41 ATQQEMMDAQLRLQLRDYCAHHLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEF 102
Cdd:pfam05676   1 ATQEEMEAAKLPLEYRDYCAHLLIPLNKCRRDNFPLPWKCEHERHAYEKCQYDDYVRRMKEY 62
 
Name Accession Description Interval E-value
NDUF_B7 pfam05676
NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7); This family consists of several ...
41-102 1.03e-28

NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7); This family consists of several NADH-ubiquinone oxidoreductase B18 subunit proteins from different eukaryotic organizms. Oxidative phosphorylation is the well-characterized process in which ATP, the principal carrier of chemical energy of individual cells, is produced due to a mitochondrial proton gradient formed by the transfer of electrons from NADH and FADH2 to molecular oxygen. The oxidative phosphorylation (OXPHOS) system is located in the mitochondrial inner membrane and consists of five multi-subunit enzyme complexes and two small electron carriers: coenzyme Q10 and cytochrome C. At least 70 structural proteins involved in the formation of the whole OXPHOS system are encoded by nuclear genes, whereas 13 structural proteins are encoded by the mitochondrial genome. Deficiency of NADH ubiquinone oxidoreductase, the first enzyme complex of the mitochondrial respiratory chain, is one of the most frequent causes of human mitochondrial encephalomyopathies.


Pssm-ID: 461710  Cd Length: 62  Bit Score: 99.57  E-value: 1.03e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10764847    41 ATQQEMMDAQLRLQLRDYCAHHLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEF 102
Cdd:pfam05676   1 ATQEEMEAAKLPLEYRDYCAHLLIPLNKCRRDNFPLPWKCEHERHAYEKCQYDDYVRRMKEY 62
 
Name Accession Description Interval E-value
NDUF_B7 pfam05676
NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7); This family consists of several ...
41-102 1.03e-28

NADH-ubiquinone oxidoreductase B18 subunit (NDUFB7); This family consists of several NADH-ubiquinone oxidoreductase B18 subunit proteins from different eukaryotic organizms. Oxidative phosphorylation is the well-characterized process in which ATP, the principal carrier of chemical energy of individual cells, is produced due to a mitochondrial proton gradient formed by the transfer of electrons from NADH and FADH2 to molecular oxygen. The oxidative phosphorylation (OXPHOS) system is located in the mitochondrial inner membrane and consists of five multi-subunit enzyme complexes and two small electron carriers: coenzyme Q10 and cytochrome C. At least 70 structural proteins involved in the formation of the whole OXPHOS system are encoded by nuclear genes, whereas 13 structural proteins are encoded by the mitochondrial genome. Deficiency of NADH ubiquinone oxidoreductase, the first enzyme complex of the mitochondrial respiratory chain, is one of the most frequent causes of human mitochondrial encephalomyopathies.


Pssm-ID: 461710  Cd Length: 62  Bit Score: 99.57  E-value: 1.03e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10764847    41 ATQQEMMDAQLRLQLRDYCAHHLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEF 102
Cdd:pfam05676   1 ATQEEMEAAKLPLEYRDYCAHLLIPLNKCRRDNFPLPWKCEHERHAYEKCQYDDYVRRMKEY 62
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH