Chain 9, V-type proton ATPase 16 kDa proteolipid subunit
V-type proton ATPase 16 kDa proteolipid subunit( domain architecture ID 12852231)
V-type proton ATPase 16 kDa proteolipid subunit is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase
List of domain hits
Name | Accession | Description | Interval | E-value | |||
V_ATP_synt_C | TIGR01100 | vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP ... |
13-118 | 3.41e-45 | |||
vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP synthase 16 kDa proteolipid subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. The principal role V-ATPases are the acidification of intracellular compartments of eukaryotic cells. [Transport and binding proteins, Cations and iron carrying compounds] : Pssm-ID: 130170 Cd Length: 108 Bit Score: 143.68 E-value: 3.41e-45
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ATP-synt_Vo_c_ATP6C_rpt2 | cd18176 | V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ... |
86-153 | 2.05e-30 | |||
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins; ATP6C (also called V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. : Pssm-ID: 349416 Cd Length: 68 Bit Score: 104.89 E-value: 2.05e-30
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Name | Accession | Description | Interval | E-value | |||
V_ATP_synt_C | TIGR01100 | vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP ... |
13-118 | 3.41e-45 | |||
vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP synthase 16 kDa proteolipid subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. The principal role V-ATPases are the acidification of intracellular compartments of eukaryotic cells. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 130170 Cd Length: 108 Bit Score: 143.68 E-value: 3.41e-45
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ATP-synt_Vo_c_ATP6C_rpt2 | cd18176 | V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ... |
86-153 | 2.05e-30 | |||
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins; ATP6C (also called V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Pssm-ID: 349416 Cd Length: 68 Bit Score: 104.89 E-value: 2.05e-30
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ATP-synt_Vo_c_ATP6C_rpt1 | cd18175 | V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ... |
13-80 | 1.01e-28 | |||
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins; ATP6C (also called the V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Pssm-ID: 349415 [Multi-domain] Cd Length: 68 Bit Score: 100.30 E-value: 1.01e-28
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PRK06558 | PRK06558 | V-type ATP synthase subunit K; Validated |
13-152 | 1.38e-12 | |||
V-type ATP synthase subunit K; Validated Pssm-ID: 235830 [Multi-domain] Cd Length: 159 Bit Score: 61.55 E-value: 1.38e-12
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ATP-synt_C | pfam00137 | ATP synthase subunit C; |
93-152 | 3.80e-11 | |||
ATP synthase subunit C; Pssm-ID: 459687 Cd Length: 60 Bit Score: 55.02 E-value: 3.80e-11
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ATP-synt_C | pfam00137 | ATP synthase subunit C; |
17-76 | 5.96e-08 | |||
ATP synthase subunit C; Pssm-ID: 459687 Cd Length: 60 Bit Score: 46.93 E-value: 5.96e-08
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AtpE | COG0636 | FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ... |
93-152 | 1.07e-05 | |||
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: 41.26 E-value: 1.07e-05
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PRK13469 | PRK13469 | F0F1 ATP synthase subunit C; Provisional |
93-152 | 5.74e-03 | |||
F0F1 ATP synthase subunit C; Provisional Pssm-ID: 184068 Cd Length: 79 Bit Score: 33.86 E-value: 5.74e-03
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Name | Accession | Description | Interval | E-value | |||
V_ATP_synt_C | TIGR01100 | vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP ... |
13-118 | 3.41e-45 | |||
vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP synthase 16 kDa proteolipid subunit in eukaryotes and includes members from diverse groups e.g., fungi, plants, parasites etc. The principal role V-ATPases are the acidification of intracellular compartments of eukaryotic cells. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 130170 Cd Length: 108 Bit Score: 143.68 E-value: 3.41e-45
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ATP-synt_Vo_c_ATP6C_rpt2 | cd18176 | V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ... |
86-153 | 2.05e-30 | |||
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins; ATP6C (also called V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Pssm-ID: 349416 Cd Length: 68 Bit Score: 104.89 E-value: 2.05e-30
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ATP-synt_Vo_c_ATP6C_rpt1 | cd18175 | V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ... |
13-80 | 1.01e-28 | |||
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar proteins; ATP6C (also called the V-ATPase 16 kDa proteolipid subunit, or vacuolar proton pump 16 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Pssm-ID: 349415 [Multi-domain] Cd Length: 68 Bit Score: 100.30 E-value: 1.01e-28
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PRK06558 | PRK06558 | V-type ATP synthase subunit K; Validated |
13-152 | 1.38e-12 | |||
V-type ATP synthase subunit K; Validated Pssm-ID: 235830 [Multi-domain] Cd Length: 159 Bit Score: 61.55 E-value: 1.38e-12
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ATP-synt_C | pfam00137 | ATP synthase subunit C; |
93-152 | 3.80e-11 | |||
ATP synthase subunit C; Pssm-ID: 459687 Cd Length: 60 Bit Score: 55.02 E-value: 3.80e-11
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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 ... |
93-152 | 9.40e-10 | |||
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: 51.76 E-value: 9.40e-10
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ATP-synt_Vo_c_ATP6F_rpt2 | cd18178 | V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ... |
89-152 | 2.64e-08 | |||
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Pssm-ID: 349418 Cd Length: 65 Bit Score: 47.89 E-value: 2.64e-08
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ATP-synt_C | pfam00137 | ATP synthase subunit C; |
17-76 | 5.96e-08 | |||
ATP synthase subunit C; Pssm-ID: 459687 Cd Length: 60 Bit Score: 46.93 E-value: 5.96e-08
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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 ... |
93-152 | 1.83e-07 | |||
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: 45.46 E-value: 1.83e-07
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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 ... |
15-76 | 3.02e-07 | |||
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: 45.21 E-value: 3.02e-07
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ATP-synt_Fo_c | cd18121 | membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ... |
93-152 | 5.89e-07 | |||
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: 44.30 E-value: 5.89e-07
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AtpE | COG0636 | FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ... |
93-152 | 1.07e-05 | |||
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: 41.26 E-value: 1.07e-05
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PRK06271 | PRK06271 | V-type ATP synthase subunit K; Validated |
17-152 | 1.87e-04 | |||
V-type ATP synthase subunit K; Validated Pssm-ID: 180501 [Multi-domain] Cd Length: 213 Bit Score: 39.79 E-value: 1.87e-04
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ATP-synt_Vo_c_ATP6F_rpt1 | cd18177 | V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ... |
93-152 | 4.06e-04 | |||
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Pssm-ID: 349417 Cd Length: 63 Bit Score: 36.86 E-value: 4.06e-04
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PRK06251 | PRK06251 | V-type ATP synthase subunit K; Validated |
64-152 | 5.98e-04 | |||
V-type ATP synthase subunit K; Validated Pssm-ID: 235752 Cd Length: 102 Bit Score: 37.03 E-value: 5.98e-04
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PRK14893 | PRK14893 | V-type ATP synthase subunit K; Provisional |
12-152 | 1.12e-03 | |||
V-type ATP synthase subunit K; Provisional Pssm-ID: 184887 [Multi-domain] Cd Length: 161 Bit Score: 37.53 E-value: 1.12e-03
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ATP-synt_Vo_c_ATP6F_rpt1 | cd18177 | V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ... |
14-76 | 1.67e-03 | |||
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. Pssm-ID: 349417 Cd Length: 63 Bit Score: 34.93 E-value: 1.67e-03
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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(+) ... |
14-76 | 2.57e-03 | |||
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: 34.40 E-value: 2.57e-03
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PRK13469 | PRK13469 | F0F1 ATP synthase subunit C; Provisional |
93-152 | 5.74e-03 | |||
F0F1 ATP synthase subunit C; Provisional Pssm-ID: 184068 Cd Length: 79 Bit Score: 33.86 E-value: 5.74e-03
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ATP-synt_Vo_Ao_c_TtATPase_like | cd18181 | Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of ... |
93-152 | 6.05e-03 | |||
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: 33.68 E-value: 6.05e-03
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PRK08344 | PRK08344 | V-type ATP synthase subunit K; Validated |
14-152 | 9.74e-03 | |||
V-type ATP synthase subunit K; Validated Pssm-ID: 236246 [Multi-domain] Cd Length: 157 Bit Score: 34.75 E-value: 9.74e-03
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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(+) ... |
93-152 | 9.90e-03 | |||
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: 32.86 E-value: 9.90e-03
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Blast search parameters | ||||
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