ATPase [Actinobacteria bacterium HGW-Actinobacteria-1]
ATP synthase F0 subunit C; ATP synthase subunit C( domain architecture ID 13031261)
ATP synthase Fo subunit c is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain; ATP synthase subunit C is a component of membrane-bound Vo/Ao complexes of V/A-type ATP synthases that produce ATP from ADP in the presence of a proton gradient across the membrane
List of domain hits
Name | Accession | Description | Interval | E-value | ||
ATP-synt_Vo_Ao_c_TtATPase_like | cd18181 | Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of ... |
24-85 | 3.90e-12 | ||
Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of uncharacterized ATPase similar to Thermus thermophilus V/A-ATPase, which is homologous to the eukaryotic V-ATPase, but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. : Pssm-ID: 349421 Cd Length: 62 Bit Score: 55.63 E-value: 3.90e-12
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Name | Accession | Description | Interval | E-value | ||
ATP-synt_Vo_Ao_c_TtATPase_like | cd18181 | Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of ... |
24-85 | 3.90e-12 | ||
Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of uncharacterized ATPase similar to Thermus thermophilus V/A-ATPase, which is homologous to the eukaryotic V-ATPase, but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. Pssm-ID: 349421 Cd Length: 62 Bit Score: 55.63 E-value: 3.90e-12
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ATP-synt_C | pfam00137 | ATP synthase subunit C; |
26-85 | 2.33e-07 | ||
ATP synthase subunit C; Pssm-ID: 459687 Cd Length: 60 Bit Score: 43.47 E-value: 2.33e-07
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PRK06271 | PRK06271 | V-type ATP synthase subunit K; Validated |
25-85 | 1.83e-03 | ||
V-type ATP synthase subunit K; Validated Pssm-ID: 180501 [Multi-domain] Cd Length: 213 Bit Score: 35.17 E-value: 1.83e-03
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Name | Accession | Description | Interval | E-value | ||
ATP-synt_Vo_Ao_c_TtATPase_like | cd18181 | Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of ... |
24-85 | 3.90e-12 | ||
Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of uncharacterized ATPase similar to Thermus thermophilus V/A-ATPase, which is homologous to the eukaryotic V-ATPase, but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. Pssm-ID: 349421 Cd Length: 62 Bit Score: 55.63 E-value: 3.90e-12
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ATP-synt_Vo_Ao_c | cd18120 | Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase ... |
24-85 | 6.49e-08 | ||
Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase subunit c. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and functions like the 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. The V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. The V1 complex consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The Vo complex consists of five different subunits: a, c, c', c'', and d. The Ao/A1 complexes are composed of nine subunits in a stoichiometry of A(3):B(3):C:D:E:F:H(2):a:c(x). ATP is synthesized on the A3:B3 hexamer and the energy released during that process is transferred to the Ao complex, which consists of the C-terminal segment of subunit a and subunit c. Pssm-ID: 349413 Cd Length: 62 Bit Score: 44.82 E-value: 6.49e-08
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ATP-synt_C | pfam00137 | ATP synthase subunit C; |
26-85 | 2.33e-07 | ||
ATP synthase subunit C; Pssm-ID: 459687 Cd Length: 60 Bit Score: 43.47 E-value: 2.33e-07
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ATP-synt_Vo_Ao_c_NTPK_rpt2 | cd18180 | V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+) ... |
25-85 | 1.42e-06 | ||
V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+)-translocating ATPase subunit K, or sodium ATPase proteolipid component) is involved in ATP-driven sodium extrusion. Pssm-ID: 349420 Cd Length: 64 Bit Score: 41.29 E-value: 1.42e-06
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ATP-synt_Vo_Ao_c_NTPK_rpt1 | cd18179 | V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+) ... |
25-85 | 4.94e-05 | ||
V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+)-translocating ATPase subunit K, or sodium ATPase proteolipid component) is involved in ATP-driven sodium extrusion. Pssm-ID: 349419 [Multi-domain] Cd Length: 63 Bit Score: 37.48 E-value: 4.94e-05
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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 ... |
25-85 | 6.35e-04 | ||
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: 34.67 E-value: 6.35e-04
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PRK06271 | PRK06271 | V-type ATP synthase subunit K; Validated |
25-85 | 1.83e-03 | ||
V-type ATP synthase subunit K; Validated Pssm-ID: 180501 [Multi-domain] Cd Length: 213 Bit Score: 35.17 E-value: 1.83e-03
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PRK06558 | PRK06558 | V-type ATP synthase subunit K; Validated |
26-84 | 2.06e-03 | ||
V-type ATP synthase subunit K; Validated Pssm-ID: 235830 [Multi-domain] Cd Length: 159 Bit Score: 34.97 E-value: 2.06e-03
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PRK06558 | PRK06558 | V-type ATP synthase subunit K; Validated |
25-85 | 5.00e-03 | ||
V-type ATP synthase subunit K; Validated Pssm-ID: 235830 [Multi-domain] Cd Length: 159 Bit Score: 33.81 E-value: 5.00e-03
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Blast search parameters | ||||
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