NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1679863885|gb|TNC93898|]
View 

MAG: F-type H+-transporting ATPase subunit b, partial [Gallionellaceae bacterium]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05759 super family cl32090
F0F1 ATP synthase subunit B; Validated
 2-61 2.58e-17

F0F1 ATP synthase subunit B; Validated


The actual alignment was detected with superfamily member PRK05759:

Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 70.19  E-value: 2.58e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:PRK05759   97 EAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 2-61 2.58e-17

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 70.19  E-value: 2.58e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:PRK05759   97 EAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 2-61 8.83e-11

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 53.18  E-value: 8.83e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:TIGR01144  88 EREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 2-61 3.97e-09

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 48.63  E-value: 3.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:COG0711    93 EAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 2-42 5.08e-05

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.80  E-value: 5.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILG 42
Cdd:cd06503    92 EAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
 
Name Accession Description Interval E-value
PRK05759 PRK05759
F0F1 ATP synthase subunit B; Validated
 2-61 2.58e-17

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180240 [Multi-domain]  Cd Length: 156  Bit Score: 70.19  E-value: 2.58e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:PRK05759   97 EAARIKAQAQAEIEQERKRAREELRKQVADLAVAGAEKILGRELDAAAQSDLIDKLIAEL 156
ATP_synt_b TIGR01144
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ...
 2-61 8.83e-11

ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130214 [Multi-domain]  Cd Length: 147  Bit Score: 53.18  E-value: 8.83e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:TIGR01144  88 EREKIKAQARAEIEAEKEQAREELRKQVADLSVLGAEKIIERNIDKQAQKDLIDKLVAEL 147
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 2-61 3.97e-09

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 48.63  E-value: 3.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:COG0711    93 EAERIIAQAEAEIEQERAKALAELRAEVADLAVAIAEKILGKELDAAAQAALVDRFIAEL 152
PRK14472 PRK14472
F0F1 ATP synthase subunit B; Provisional
 1-61 6.61e-07

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172947 [Multi-domain]  Cd Length: 175  Bit Score: 43.26  E-value: 6.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1679863885   1 VEGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:PRK14472  110 TEAKKMIASAKEEIEQEKRRALDVLRNEVADLAVKGAEKIIRTSLDADKQKKVVDSMIQDL 170
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 2-42 5.08e-05

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.80  E-value: 5.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILG 42
Cdd:cd06503    92 EAERILEQAKAEIEQEKEKALAELRKEVADLAVEAAEKILG 132
PRK13461 PRK13461
F0F1 ATP synthase subunit B; Provisional
 1-61 4.93e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184064 [Multi-domain]  Cd Length: 159  Bit Score: 35.41  E-value: 4.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1679863885   1 VEGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:PRK13461   97 EEADLIIERAKLEAQREKEKAEYEIKNQAVDLAVLLSSKALEESIDESEHRRLIKDFISKV 157
PRK06231 PRK06231
F0F1 ATP synthase subunit B; Validated
 4-61 6.29e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180481 [Multi-domain]  Cd Length: 205  Bit Score: 35.20  E-value: 6.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1679863885   4 DRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:PRK06231  143 NLIIFQARQEIEKERRELKEQLQKESVELAMLAAEELIKKKVDREDDDKLVDEFIREL 200
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 2-61 6.90e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 32.20  E-value: 6.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679863885   2 EGDRIIAGAKAEIDQEVFRAKEQLRTQVSAIALAGAGKILGREIDAKAHNDLLDKLVAEI 61
Cdd:PRK14473  101 EAEKIKEEARAQAEQERQRMLSELKSQIADLVTLTASRVLGAELQARGHDALIAESLAAL 160
 
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