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Conserved domains on  [gi|1622824896|ref|XP_028693498|]
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V-type proton ATPase 21 kDa proteolipid subunit isoform X3 [Macaca mulatta]

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 ...
 56-118 2.91e-33

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: 113.90  E-value: 2.91e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622824896  56 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 118
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 ...
 140-204 1.24e-27

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: 99.50  E-value: 1.24e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622824896 140 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQ 204
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 ...
 56-118 2.91e-33

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: 113.90  E-value: 2.91e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622824896  56 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 118
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 ...
 140-204 1.24e-27

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: 99.50  E-value: 1.24e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622824896 140 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQ 204
Cdd:cd18178     1 AGYALFGAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM 65
ATP-synt_C pfam00137
ATP synthase subunit C;
145-203 3.55e-11

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 56.56  E-value: 3.55e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622824896 145 FGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALL 59
ATP-synt_C pfam00137
ATP synthase subunit C;
59-118 1.05e-10

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 55.02  E-value: 1.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896  59 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 118
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
PRK06271 PRK06271
V-type ATP synthase subunit K; Validated
 35-203 9.97e-07

V-type ATP synthase subunit K; Validated


Pssm-ID: 180501 [Multi-domain]  Cd Length: 213  Bit Score: 47.49  E-value: 9.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896  35 GLNCFLLCLHNRFLTETSPfMWSNLGIGLAISLSVVgAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIM 114
Cdd:PRK06271   52 GLYGFLVAILILFVFKTAP-EWAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896 115 AIVIsnMAEPFSATDPKAIGhrnyhagysMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIG 194
Cdd:PRK06271  130 AILL--LVGVFASPGVETIA---------ALGAGLAVGFAGL-SGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFA 197


                  ....*....
gi 1622824896 195 LFGVIVAIL 203
Cdd:PRK06271  198 IFGLLIAIL 206
PRK06251 PRK06251
V-type ATP synthase subunit K; Validated
 146-203 3.11e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 235752  Cd Length: 102  Bit Score: 35.87  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824896 146 GAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:PRK06251   39 GAGLAVGLAAIGAGIAVGMAAAAGIGVLTERRDMFGTVLIFVAIGEGIAVYGILFAVL 96
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 140-203 6.18e-03

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: 34.33  E-value: 6.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824896 140 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSA----IGLFGVIVAIL 203
Cdd:COG0636     3 AAASAIGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAAlieaLAIYALVIALI 70
 
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 ...
 56-118 2.91e-33

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: 113.90  E-value: 2.91e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622824896  56 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 118
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 ...
 140-204 1.24e-27

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: 99.50  E-value: 1.24e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622824896 140 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQ 204
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 ...
 140-203 9.79e-14

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: 63.68  E-value: 9.79e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622824896 140 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:cd18176     3 KGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALI 66
ATP-synt_C pfam00137
ATP synthase subunit C;
145-203 3.55e-11

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 56.56  E-value: 3.55e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622824896 145 FGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALL 59
ATP-synt_C pfam00137
ATP synthase subunit C;
59-118 1.05e-10

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 55.02  E-value: 1.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896  59 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 118
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 ...
 144-203 1.12e-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: 55.22  E-value: 1.12e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896 144 MFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:cd18120     2 YLGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAIL 61
ATP-synt_Vo_Ao_c cd18120
Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase ...
 58-118 1.33e-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: 54.84  E-value: 1.33e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622824896  58 NLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 118
Cdd:cd18120     2 YLGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI 62
ATP-synt_Vo_c_ATP6C_rpt1 cd18175
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 56-120 1.76e-07

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: 46.76  E-value: 1.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622824896  56 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVISN 120
Cdd:cd18175     2 FGYMGAAAALVFSNLGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISN 66
PRK06271 PRK06271
V-type ATP synthase subunit K; Validated
 35-203 9.97e-07

V-type ATP synthase subunit K; Validated


Pssm-ID: 180501 [Multi-domain]  Cd Length: 213  Bit Score: 47.49  E-value: 9.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896  35 GLNCFLLCLHNRFLTETSPfMWSNLGIGLAISLSVVgAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIM 114
Cdd:PRK06271   52 GLYGFLVAILILFVFKTAP-EWAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896 115 AIVIsnMAEPFSATDPKAIGhrnyhagysMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIG 194
Cdd:PRK06271  130 AILL--LVGVFASPGVETIA---------ALGAGLAVGFAGL-SGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFA 197


                  ....*....
gi 1622824896 195 LFGVIVAIL 203
Cdd:PRK06271  198 IFGLLIAIL 206
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 ...
 59-118 8.40e-06

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: 41.99  E-value: 8.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622824896  59 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAP----RIKTKNLVSIIFCEAVAIYGIIMAIVI 118
Cdd:cd00313     2 LGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPeaagKIFTTMLIGLALIESLAIYGLVIAFLL 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 ...
 144-203 1.66e-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: 38.52  E-value: 1.66e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622824896 144 MFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPS----LFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:cd00313     1 ALGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPEaagkIFTTMLIGLALIESLAIYGLVIAFL 64
PRK06271 PRK06271
V-type ATP synthase subunit K; Validated
 59-203 5.34e-04

V-type ATP synthase subunit K; Validated


Pssm-ID: 180501 [Multi-domain]  Cd Length: 213  Bit Score: 39.79  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896  59 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVISNMAEPfsatdpkaighrny 138
Cdd:PRK06271    3 IGAGLAVGIAGLGSGIGAGITGASGAGVVAEDPNKFGTAIVFQALPQTQGLYGFLVAILILFVFKT-------------- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622824896 139 HAGYSMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:PRK06271   69 APEWAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAIL 132
PRK08344 PRK08344
V-type ATP synthase subunit K; Validated
 55-206 1.18e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 236246 [Multi-domain]  Cd Length: 157  Bit Score: 38.22  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896  55 MWSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGII----MAIVISNMAEPFSATDP 130
Cdd:PRK08344    1 VYVALGAALAAGLAGAASSFGVGIAGSAAAGAVAEDEKNFRNALILAGLPMTQTIYGLItlflILMYAGILGGGFKFAEP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622824896 131 KAIghrNYHAGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNP-SLFVKILIVEIFGSAIGLFGVIVAILQTS 206
Cdd:PRK08344   81 DTI---NLGKALALLGAGLLVGLAELLSAIPQGIICASGIGALPRTPgKTFTQTIILAAYAELMGIFGLVFAILGLS 154
ATP-synt_Vo_Ao_c_NTPK_rpt1 cd18179
V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+) ...
 142-203 1.20e-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: 35.94  E-value: 1.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622824896 142 YSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:cd18179     1 LALIGAALAVGLAGIGSAIGVGIAGQAAAGVLAEKPEKFGKLLVLQALPGTQGIYGFVIAFL 62
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 58-119 2.31e-03

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: 35.56  E-value: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622824896  58 NLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVIS 119
Cdd:cd18176     7 HLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALILS 68
PRK06251 PRK06251
V-type ATP synthase subunit K; Validated
 146-203 3.11e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 235752  Cd Length: 102  Bit Score: 35.87  E-value: 3.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824896 146 GAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 203
Cdd:PRK06251   39 GAGLAVGLAAIGAGIAVGMAAAAGIGVLTERRDMFGTVLIFVAIGEGIAVYGILFAVL 96
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 59-118 3.67e-03

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: 34.67  E-value: 3.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622824896  59 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAP----RIKTKNLVSIIFCEAVAIYGIIMAIVI 118
Cdd:cd18121     2 LGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPeaagKIRTTMIIGLALIESLAIYALVIALIL 65
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 140-203 6.18e-03

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: 34.33  E-value: 6.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622824896 140 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSA----IGLFGVIVAIL 203
Cdd:COG0636     3 AAASAIGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAAlieaLAIYALVIALI 70
PRK06558 PRK06558
V-type ATP synthase subunit K; Validated
 47-209 8.37e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 235830 [Multi-domain]  Cd Length: 159  Bit Score: 35.74  E-value: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896  47 FLTETSPFMWSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI-SNMAEPF 125
Cdd:PRK06558    7 FFTQNGGAFFAALGAALAVGLSGIGSAKGVGKAGEAAAGLLTEEPEKFGKALILQLLPGTQGLYGFVIGFLIwQKITPEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622824896 126 SatdpkaighrnYHAGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQT 205
Cdd:PRK06558   87 S-----------LAQGLAYFAACLPIAIVGLFSAISQGKVAAAGIQILAKRPEEFTKGIILAAMVETYAILAFVVSFLLL 155


                  ....
gi 1622824896 206 SRVK 209
Cdd:PRK06558  156 NGVK 159
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 144-203 8.88e-03

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: 33.51  E-value: 8.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622824896 144 MFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSA----IGLFGVIVAIL 203
Cdd:cd18121     1 ALGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLAliesLAIYALVIALI 64
 
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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