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Conserved domains on  [gi|2541256504|ref|WP_297368986|]
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F0F1 ATP synthase subunit C [Acidocella sp.]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATP-synt_Fo_Vo_Ao_c super family cl38906
ATP synthase, membrane-bound Fo/Vo/Ao complexes, subunit c; Subunit c of the Fo/Vo/Ao complex ...
11-75 9.16e-12

ATP synthase, membrane-bound Fo/Vo/Ao complexes, subunit c; Subunit c of the Fo/Vo/Ao complex is the main transmembrane subunit of F-, V- or A-type family of ATP synthases with rotary motors. These ion-transporting rotary ATP synthases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contains three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao (oligomycin sensitive) complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases 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. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and function like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes.


The actual alignment was detected with superfamily member cd18182:

Pssm-ID: 365782  Cd Length: 65  Bit Score: 54.44  E-value: 9.16e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541256504 11 KDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVI 75
Cdd:cd18182    1 KYIGAGLATIGLAGAGIGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI 65
 
Name Accession Description Interval E-value
ATP-synt_Fo_c_ATP5G3 cd18182
ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP ...
11-75 9.16e-12

ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP synthase lipid-binding protein, ATP synthase proteolipid P3, ATP synthase proton-transporting mitochondrial F(o) complex subunit C3, ATPase protein 9, or ATPase subunit c) transports protons across the inner mitochondrial membrane to the F1-ATPase protruding on the matrix side, resulting in the generation of ATP.


Pssm-ID: 349422  Cd Length: 65  Bit Score: 54.44  E-value: 9.16e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541256504 11 KDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVI 75
Cdd:cd18182    1 KYIGAGLATIGLAGAGIGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI 65
PRK07558 PRK07558
F0F1 ATP synthase subunit C; Validated
10-78 7.62e-09

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 181027  Cd Length: 74  Bit Score: 47.27  E-value: 7.62e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541256504 10 AKDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILFA 78
Cdd:PRK07558   6 LKFIGAGLACIGMAGAALGVGNIFGNYLSGALRNPSAADSQFGYLLIGAALAEALGIFSFLIALLLLFA 74
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
31-78 9.48e-08

FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440401  Cd Length: 75  Bit Score: 44.34  E-value: 9.48e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 2541256504 31 NLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILFA 78
Cdd:COG0636   27 LAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFA 74
 
Name Accession Description Interval E-value
ATP-synt_Fo_c_ATP5G3 cd18182
ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP ...
11-75 9.16e-12

ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP synthase lipid-binding protein, ATP synthase proteolipid P3, ATP synthase proton-transporting mitochondrial F(o) complex subunit C3, ATPase protein 9, or ATPase subunit c) transports protons across the inner mitochondrial membrane to the F1-ATPase protruding on the matrix side, resulting in the generation of ATP.


Pssm-ID: 349422  Cd Length: 65  Bit Score: 54.44  E-value: 9.16e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541256504 11 KDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVI 75
Cdd:cd18182    1 KYIGAGLATIGLAGAGIGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI 65
PRK07558 PRK07558
F0F1 ATP synthase subunit C; Validated
10-78 7.62e-09

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 181027  Cd Length: 74  Bit Score: 47.27  E-value: 7.62e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541256504 10 AKDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILFA 78
Cdd:PRK07558   6 LKFIGAGLACIGMAGAALGVGNIFGNYLSGALRNPSAADSQFGYLLIGAALAEALGIFSFLIALLLLFA 74
PRK07159 PRK07159
F0F1 ATP synthase subunit C; Validated
5-77 2.92e-08

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 235949  Cd Length: 100  Bit Score: 46.43  E-value: 2.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541256504   5 SAALLAKDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILF 77
Cdd:PRK07159   26 SSGLKAAYIGAGLAMIGVIGVGLGQGYAFGKAVEAIARNPEAQKQVFKLLFIGSAISETSSIYALLVAFILIF 98
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
31-78 9.48e-08

FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440401  Cd Length: 75  Bit Score: 44.34  E-value: 9.48e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 2541256504 31 NLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILFA 78
Cdd:COG0636   27 LAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFA 74
PRK13469 PRK13469
F0F1 ATP synthase subunit C; Provisional
1-78 2.37e-07

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184068  Cd Length: 79  Bit Score: 43.49  E-value: 2.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541256504  1 MDPQSAALLAKDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILFA 78
Cdd:PRK13469   1 IDGKAFVMGMSAIGAGIAALAGIGAGIGIGIATGKAVEAVGRQPEASGKIMSTMLLGAALAEATAIYGLVIAIILLFV 78
ATP9 MTH00222
ATP synthase F0 subunit 9; Provisional
10-78 1.23e-06

ATP synthase F0 subunit 9; Provisional


Pssm-ID: 164765 [Multi-domain]  Cd Length: 77  Bit Score: 41.76  E-value: 1.23e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541256504 10 AKDVGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILFA 78
Cdd:MTH00222   8 AKFVGAGAATIGAAGSGAGIGTVFGNLIIGYARNPSLKQQLFTYAILGFAISEAMGLFCLMMAFLILFA 76
ATP-synt_Fo_c_NaATPase cd18184
F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type ...
13-75 5.24e-06

F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type Na(+)-coupled ATP synthase and similar proteins.


Pssm-ID: 349424 [Multi-domain]  Cd Length: 65  Bit Score: 39.87  E-value: 5.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541256504 13 VGAGLATIGVAGAGVGIGNLFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVI 75
Cdd:cd18184    3 IGAGLAMIAGIGPGIGQGYAAGKAVEAVGRNPEAEGKIRSTMILGAAVAETTAIYGLIIALLL 65
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
32-75 8.67e-06

membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or proteolipid) of the Fo complex of F-ATP synthase. The F-ATP synthase (also called FoF1-ATPase) consists of two structural domains: the F1 (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, beta, gamma, delta, and epsilon 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 though 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 Methanosarcina acetivorans.


Pssm-ID: 349414  Cd Length: 65  Bit Score: 38.91  E-value: 8.67e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 2541256504 32 LFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVI 75
Cdd:cd18121   22 AAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIALIL 65
ATP-synt_Fo_Vo_Ao_c cd00313
ATP synthase, membrane-bound Fo/Vo/Ao complexes, subunit c; Subunit c of the Fo/Vo/Ao complex ...
32-75 5.71e-05

ATP synthase, membrane-bound Fo/Vo/Ao complexes, subunit c; Subunit c of the Fo/Vo/Ao complex is the main transmembrane subunit of F-, V- or A-type family of ATP synthases with rotary motors. These ion-transporting rotary ATP synthases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contains three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao (oligomycin sensitive) complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases 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. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and function like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes.


Pssm-ID: 349412 [Multi-domain]  Cd Length: 65  Bit Score: 36.98  E-value: 5.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 2541256504 32 LFGAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVI 75
Cdd:cd00313   22 AGAAALEAIARQPEAAGKIFTTMLIGLALIESLAIYGLVIAFLL 65
atpH CHL00061
ATP synthase CF0 C subunit
34-78 5.44e-03

ATP synthase CF0 C subunit


Pssm-ID: 177001  Cd Length: 81  Bit Score: 32.38  E-value: 5.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 2541256504 34 GAFVSAVGRNPAARDAMFRDVLLGFALTEAVALYALVIALVILFA 78
Cdd:CHL00061  33 GQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFA 77
 
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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