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Conserved domains on  [gi|1720407049|ref|XP_030108954|]
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V-type proton ATPase 21 kDa proteolipid subunit c'' isoform X1 [Mus musculus]

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 ...
 2-64 5.79e-31

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: 106.19  E-value: 5.79e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720407049   2 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 64
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 ...
 86-150 1.87e-26

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: 94.50  E-value: 1.87e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720407049  86 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQ 150
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 ...
 2-64 5.79e-31

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: 106.19  E-value: 5.79e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720407049   2 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 64
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 ...
 86-150 1.87e-26

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: 94.50  E-value: 1.87e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720407049  86 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQ 150
Cdd:cd18178     1 AGYALFGAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM 65
ATP-synt_C pfam00137
ATP synthase subunit C;
91-149 1.45e-09

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 51.17  E-value: 1.45e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720407049  91 FGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALL 59
ATP-synt_C pfam00137
ATP synthase subunit C;
5-64 3.77e-09

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 50.01  E-value: 3.77e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720407049   5 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 64
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
PRK06271 PRK06271
V-type ATP synthase subunit K; Validated
 2-149 5.88e-05

V-type ATP synthase subunit K; Validated


Pssm-ID: 180501 [Multi-domain]  Cd Length: 213  Bit Score: 41.33  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720407049   2 WSNLGIGLAISLSVVgAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVIsnMAEPFSATEPKAIGh 81
Cdd:PRK06271   72 WAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAILL--LVGVFASPGVETIA- 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720407049  82 rnyhagysMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:PRK06271  148 --------ALGAGLAVGFAGL-SGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFAIFGLLIAIL 206
 
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 ...
 2-64 5.79e-31

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: 106.19  E-value: 5.79e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720407049   2 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 64
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 ...
 86-150 1.87e-26

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: 94.50  E-value: 1.87e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720407049  86 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAILQ 150
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 ...
 86-149 2.31e-13

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: 61.37  E-value: 2.31e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720407049  86 AGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:cd18176     3 KGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALI 66
ATP-synt_C pfam00137
ATP synthase subunit C;
91-149 1.45e-09

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 51.17  E-value: 1.45e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720407049  91 FGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALL 59
ATP-synt_C pfam00137
ATP synthase subunit C;
5-64 3.77e-09

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 50.01  E-value: 3.77e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720407049   5 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 64
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 ...
 90-149 3.77e-09

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: 50.22  E-value: 3.77e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720407049  90 MFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
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 ...
 4-64 4.47e-09

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: 49.83  E-value: 4.47e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720407049   4 NLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVI 64
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 ...
 2-66 1.32e-06

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: 43.68  E-value: 1.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720407049   2 WSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVISN 66
Cdd:cd18175     2 FGYMGAAAALVFSNLGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISN 66
PRK06271 PRK06271
V-type ATP synthase subunit K; Validated
 2-149 5.88e-05

V-type ATP synthase subunit K; Validated


Pssm-ID: 180501 [Multi-domain]  Cd Length: 213  Bit Score: 41.33  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720407049   2 WSNLGIGLAISLSVVgAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVIsnMAEPFSATEPKAIGh 81
Cdd:PRK06271   72 WAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAILL--LVGVFASPGVETIA- 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720407049  82 rnyhagysMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:PRK06271  148 --------ALGAGLAVGFAGL-SGIGQGITAAGAIGATARDPDAMGKGLVLAVMPETFAIFGLLIAIL 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 ...
 5-64 1.49e-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: 38.14  E-value: 1.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720407049   5 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAP----RIKTKNLVSIIFCEAVAIYGIIMAIVI 64
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 ...
 90-149 2.31e-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: 34.67  E-value: 2.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720407049  90 MFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPS----LFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:cd00313     1 ALGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPEaagkIFTTMLIGLALIESLAIYGLVIAFL 64
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 4-65 3.77e-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: 34.40  E-value: 3.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720407049   4 NLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVIS 65
Cdd:cd18176     7 HLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALILS 68
ATP-synt_Vo_Ao_c_NTPK_rpt1 cd18179
V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+) ...
 88-149 4.27e-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: 34.01  E-value: 4.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720407049  88 YSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:cd18179     1 LALIGAALAVGLAGIGSAIGVGIAGQAAAGVLAEKPEKFGKLLVLQALPGTQGIYGFVIAFL 62
PRK06271 PRK06271
V-type ATP synthase subunit K; Validated
 5-149 5.19e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 180501 [Multi-domain]  Cd Length: 213  Bit Score: 35.94  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720407049   5 LGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGIIMAIVISNMAEPfsatepkaighrny 84
Cdd:PRK06271    3 IGAGLAVGIAGLGSGIGAGITGASGAGVVAEDPNKFGTAIVFQALPQTQGLYGFLVAILILFVFKT-------------- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720407049  85 HAGYSMFGAGLTVGLSNLfCGVCVGIVGSGAALADAQNPSLFVKILIVEIFGSAIGLFGVIVAIL 149
Cdd:PRK06271   69 APEWAMLAAGLAVGLAGL-SAIGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAIL 132
PRK08344 PRK08344
V-type ATP synthase subunit K; Validated
 1-152 8.61e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 236246 [Multi-domain]  Cd Length: 157  Bit Score: 34.75  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720407049   1 MWSNLGIGLAISLSVVGAAWGIYITGSSIIGGGVKAPRIKTKNLVSIIFCEAVAIYGII----MAIVISNMAEPFSATEP 76
Cdd:PRK08344    1 VYVALGAALAAGLAGAASSFGVGIAGSAAAGAVAEDEKNFRNALILAGLPMTQTIYGLItlflILMYAGILGGGFKFAEP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720407049  77 KAIghrNYHAGYSMFGAGLTVGLSNLFCGVCVGIVGSGAALADAQNP-SLFVKILIVEIFGSAIGLFGVIVAILQTS 152
Cdd:PRK08344   81 DTI---NLGKALALLGAGLLVGLAELLSAIPQGIICASGIGALPRTPgKTFTQTIILAAYAELMGIFGLVFAILGLS 154
 
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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