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Conserved domains on  [gi|17535901|ref|NP_495659|]
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V-type proton ATPase 21 kDa proteolipid subunit c'' [Caenorhabditis elegans]

Protein Classification

V-type proton ATPase 21 kDa proteolipid subunit( domain architecture ID 13031245)

V-type proton ATPase 21 kDa proteolipid subunit is the proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase that is responsible for acidifying a variety of intracellular compartments in eukaryotic cells; three proteolipid subunits (known as c, c' and c'' in yeast) are part of the proton-conducting pore, each containing a buried glutamic acid residue that is essential for proton transport, together they form a hexameric ring spanning the membrane.

Gene Ontology:  GO:1902600|GO:0046961|GO:0033179|GO:0046961
PubMed:  9442887|15951435|9210392

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Vo_c_ATP6F_rpt1 cd18177
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 51-113 4.05e-30

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: 105.81  E-value: 4.05e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535901  51 WAGLGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVF 113
Cdd:cd18177   1 WAALGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63
ATP-synt_Vo_c_ATP6F_rpt2 cd18178
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 141-205 2.73e-17

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: 72.92  E-value: 2.73e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535901 141 SGYMIFGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIVQ 205
Cdd:cd18178   1 AGYALFGAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM 65
 
Name Accession Description Interval E-value
ATP-synt_Vo_c_ATP6F_rpt1 cd18177
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 51-113 4.05e-30

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: 105.81  E-value: 4.05e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535901  51 WAGLGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVF 113
Cdd:cd18177   1 WAALGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63
ATP-synt_Vo_c_ATP6F_rpt2 cd18178
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 141-205 2.73e-17

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: 72.92  E-value: 2.73e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535901 141 SGYMIFGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIVQ 205
Cdd:cd18178   1 AGYALFGAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM 65
ATP-synt_C pfam00137
ATP synthase subunit C;
54-113 1.01e-07

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 47.32  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535901    54 LGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVF 113
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
ATP-synt_C pfam00137
ATP synthase subunit C;
146-204 1.18e-04

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 38.84  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17535901   146 FGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIV 204
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALL 59
 
Name Accession Description Interval E-value
ATP-synt_Vo_c_ATP6F_rpt1 cd18177
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 51-113 4.05e-30

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: 105.81  E-value: 4.05e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17535901  51 WAGLGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVF 113
Cdd:cd18177   1 WAALGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63
ATP-synt_Vo_c_ATP6F_rpt2 cd18178
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 141-205 2.73e-17

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: 72.92  E-value: 2.73e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535901 141 SGYMIFGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIVQ 205
Cdd:cd18178   1 AGYALFGAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM 65
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 139-204 5.01e-10

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: 53.66  E-value: 5.01e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17535901 139 LASGYMIFGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIV 204
Cdd:cd18176   1 LFKGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALI 66
ATP-synt_C pfam00137
ATP synthase subunit C;
54-113 1.01e-07

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 47.32  E-value: 1.01e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535901    54 LGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVF 113
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
ATP-synt_Vo_Ao_c cd18120
Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase ...
 52-113 2.30e-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: 46.36  E-value: 2.30e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17535901  52 AGLGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVF 113
Cdd:cd18120   1 AYLGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI 62
ATP-synt_Vo_Ao_c cd18120
Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase ...
 144-204 2.47e-05

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: 40.59  E-value: 2.47e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17535901 144 MIFGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIV 204
Cdd:cd18120   1 AYLGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAIL 61
ATP-synt_C pfam00137
ATP synthase subunit C;
146-204 1.18e-04

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 38.84  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17535901   146 FGGGLTVGLSNLVCGLAVGIVGSGAAIADAANPALFVKILIIEIFASAIGLFGMIIGIV 204
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALL 59
ATP-synt_Vo_c_ATP6C_rpt1 cd18175
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 51-117 3.98e-04

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: 37.51  E-value: 3.98e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17535901  51 WAGLGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAPRIRTKNLVSIIFCEAVAIFGIIMAFVFVGKL 117
Cdd:cd18175   2 FGYMGAAAALVFSNLGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISNNI 68
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 ...
 53-113 2.11e-03

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: 35.44  E-value: 2.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17535901  53 GLGIGFSLSLSVLGAGWGIFTTGSSILGGGVKAP----RIRTKNLVSIIFCEAVAIFGIIMAFVF 113
Cdd:cd00313   1 ALGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPeaagKIFTTMLIGLALIESLAIYGLVIAFLL 65
 
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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