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Conserved domains on  [gi|1743172575|ref|XP_012352032|]
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V-type proton ATPase 16 kDa proteolipid subunit-like [Nomascus leucogenys]

Protein Classification

V-type proton ATPase proteolipid subunit( domain architecture ID 13052832)

V-type proton ATPase 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13469 super family cl00466
F0F1 ATP synthase subunit C; Provisional
 17-122 1.61e-42

F0F1 ATP synthase subunit C; Provisional


The actual alignment was detected with superfamily member TIGR01100:

Pssm-ID: 469780  Cd Length: 108  Bit Score: 137.52  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  17 FFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANS--PNDGISLYRSC 94
Cdd:TIGR01100   1 FFGVMGAAAALVFSALGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSlkPKSNYSLYKGF 80

                          90       100
                  ....*....|....*....|....*...
gi 1743172575  95 LQLGAGRSVGLSGLAAGFAIDIAGDAGV 122
Cdd:TIGR01100  81 IHLGAGLAVGLSGLAAGFAIGIVGDAGV 108
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 90-157 4.50e-28

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: 99.12  E-value: 4.50e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743172575  90 LYRSCLQLGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALILS 157
Cdd:cd18176     1 LFKGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALILS 68
 
Name Accession Description Interval E-value
V_ATP_synt_C TIGR01100
vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP ...
 17-122 1.61e-42

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: 137.52  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  17 FFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANS--PNDGISLYRSC 94
Cdd:TIGR01100   1 FFGVMGAAAALVFSALGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSlkPKSNYSLYKGF 80

                          90       100
                  ....*....|....*....|....*...
gi 1743172575  95 LQLGAGRSVGLSGLAAGFAIDIAGDAGV 122
Cdd:TIGR01100  81 IHLGAGLAVGLSGLAAGFAIGIVGDAGV 108
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 90-157 4.50e-28

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: 99.12  E-value: 4.50e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743172575  90 LYRSCLQLGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALILS 157
Cdd:cd18176     1 LFKGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALILS 68
ATP-synt_Vo_c_ATP6C_rpt1 cd18175
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 17-83 1.31e-26

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: 95.68  E-value: 1.31e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743172575  17 FFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANS 83
Cdd:cd18175     1 FFGYMGAAAALVFSNLGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISNN 67
ATP-synt_C pfam00137
ATP synthase subunit C;
97-156 2.81e-11

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 55.79  E-value: 2.81e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
PRK06558 PRK06558
V-type ATP synthase subunit K; Validated
 17-156 1.73e-07

V-type ATP synthase subunit K; Validated


Pssm-ID: 235830 [Multi-domain]  Cd Length: 159  Bit Score: 48.06  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  17 FFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANSPNDGISLYRSCLQ 96
Cdd:PRK06558   15 FFAALGAALAVGLSGIGSAKGVGKAGEAAAGLLTEEPEKFGKALILQLLPGTQGLYGFVIGFLIWQKITPELSLAQGLAY 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:PRK06558   95 FAACLPIAIVGLFSAISQGKVAAAGIQILAKRPEEFTKGIILAAMVETYAILAFVVSFLL 154
ATP-synt_C pfam00137
ATP synthase subunit C;
21-80 4.94e-07

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 44.62  E-value: 4.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  21 MGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLI 80
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 97-156 9.57e-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: 38.95  E-value: 9.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQP----RLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:COG0636     8 IGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPeaagKLQTTMFIGAALIEALAIYALVIALIL 71
 
Name Accession Description Interval E-value
V_ATP_synt_C TIGR01100
vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP ...
 17-122 1.61e-42

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: 137.52  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  17 FFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANS--PNDGISLYRSC 94
Cdd:TIGR01100   1 FFGVMGAAAALVFSALGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSlkPKSNYSLYKGF 80

                          90       100
                  ....*....|....*....|....*...
gi 1743172575  95 LQLGAGRSVGLSGLAAGFAIDIAGDAGV 122
Cdd:TIGR01100  81 IHLGAGLAVGLSGLAAGFAIGIVGDAGV 108
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 90-157 4.50e-28

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: 99.12  E-value: 4.50e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1743172575  90 LYRSCLQLGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALILS 157
Cdd:cd18176     1 LFKGFAHLGAGLSVGLSGLAAGFAIGIVGDAGVRATAQQPKLFVGMILILIFAEALGLYGLIVALILS 68
ATP-synt_Vo_c_ATP6C_rpt1 cd18175
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 17-83 1.31e-26

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: 95.68  E-value: 1.31e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1743172575  17 FFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANS 83
Cdd:cd18175     1 FFGYMGAAAALVFSNLGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISNN 67
ATP-synt_C pfam00137
ATP synthase subunit C;
97-156 2.81e-11

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 55.79  E-value: 2.81e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
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 ...
 97-156 2.95e-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: 50.60  E-value: 2.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:cd18120     3 LGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI 62
PRK06558 PRK06558
V-type ATP synthase subunit K; Validated
 17-156 1.73e-07

V-type ATP synthase subunit K; Validated


Pssm-ID: 235830 [Multi-domain]  Cd Length: 159  Bit Score: 48.06  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  17 FFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANSPNDGISLYRSCLQ 96
Cdd:PRK06558   15 FFAALGAALAVGLSGIGSAKGVGKAGEAAAGLLTEEPEKFGKALILQLLPGTQGLYGFVIGFLIWQKITPELSLAQGLAY 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:PRK06558   95 FAACLPIAIVGLFSAISQGKVAAAGIQILAKRPEEFTKGIILAAMVETYAILAFVVSFLL 154
ATP-synt_C pfam00137
ATP synthase subunit C;
21-80 4.94e-07

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 44.62  E-value: 4.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  21 MGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLI 80
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
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 ...
 97-156 2.19e-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: 43.14  E-value: 2.19e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQP----RLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:cd00313     2 LGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPeaagKIFTTMLIGLALIESLAIYGLVIAFLL 65
ATP-synt_Vo_Ao_c cd18120
Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase ...
 19-80 3.29e-06

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: 42.51  E-value: 3.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1743172575  19 AVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLI 80
Cdd:cd18120     1 AYLGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI 62
ATP-synt_Vo_c_ATP6F_rpt2 cd18178
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 98-156 1.07e-05

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: 41.34  E-value: 1.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1743172575  98 GAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:cd18178     7 GAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM 65
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 97-156 1.37e-05

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: 40.83  E-value: 1.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQP----RLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:cd18121     2 LGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPeaagKIRTTMIIGLALIESLAIYALVIALIL 65
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 97-156 9.57e-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: 38.95  E-value: 9.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQP----RLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:COG0636     8 IGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPeaagKLQTTMFIGAALIEALAIYALVIALIL 71
ATP-synt_Vo_Ao_c_TtATPase_like cd18181
Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of ...
 97-156 1.08e-04

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: 38.30  E-value: 1.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:cd18181     3 IGAGLAIGLAAIGTGWAQSRIGAAAVGAIAEKPELFGTALILTAIPETLVILGFVIAFLL 62
PRK14893 PRK14893
V-type ATP synthase subunit K; Provisional
 16-156 1.32e-04

V-type ATP synthase subunit K; Provisional


Pssm-ID: 184887 [Multi-domain]  Cd Length: 161  Bit Score: 40.22  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  16 SFFAVMGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLI-----ANSPNDGISL 90
Cdd:PRK14893    8 TALAAIGAGVAVGFAGLGSGLGQGIAAAGSVGAVAEDSDMFARGIIFSALPETQAIYGFLIAILLlvfsgLLGGGEGLSV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1743172575  91 YRSCLQLGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:PRK14893   88 TAGLVAIGAGAAIGFAGLGSGMGQGIASASSVGAVVEDPDMFARGIIFSALPETQAIYGFLIAILL 153
PRK13469 PRK13469
F0F1 ATP synthase subunit C; Provisional
 86-156 9.10e-04

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184068  Cd Length: 79  Bit Score: 36.56  E-value: 9.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1743172575  86 DGISLYRSCLQLGAGRSVgLSGLAAGFAIDIAGDAGVRATAQQP----RLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:PRK13469    2 DGKAFVMGMSAIGAGIAA-LAGIGAGIGIGIATGKAVEAVGRQPeasgKIMSTMLLGAALAEATAIYGLVIAIIL 75
PRK06251 PRK06251
V-type ATP synthase subunit K; Validated
 51-156 1.22e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 235752  Cd Length: 102  Bit Score: 36.64  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  51 MRPELIIKSIIPAVMAGIIAIyglvvtvliANSPNDgISLYRSCLQLGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPR 130
Cdd:PRK06251    2 KRASLILSVLLPILISSVIAG---------AQAPSD-TAQGFAGINIGAGLAVGLAAIGAGIAVGMAAAAGIGVLTERRD 71

                          90       100
                  ....*....|....*....|....*.
gi 1743172575 131 LFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:PRK06251   72 MFGTVLIFVAIGEGIAVYGILFAVLM 97
ATP-synt_Vo_c_ATP6F_rpt1 cd18177
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 97-156 2.36e-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: 2.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:cd18177     4 LGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63
ATP-synt_Vo_Ao_c_NTPK_rpt1 cd18179
V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+) ...
 97-156 3.85e-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: 3.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  97 LGAGRSVGLSGLAAGFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:cd18179     4 IGAALAVGLAGIGSAIGVGIAGQAAAGVLAEKPEKFGKLLVLQALPGTQGIYGFVIAFLI 63
PRK06271 PRK06271
V-type ATP synthase subunit K; Validated
 21-156 7.33e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 180501 [Multi-domain]  Cd Length: 213  Bit Score: 35.55  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1743172575  21 MGASAAMVFSSPRAAYGTVESGAGIAAMSVMRPELIIKSIIPAVMAGIIAIYGLVVTVLIANSpndgISLYRSCLQLGAG 100
Cdd:PRK06271    3 IGAGLAVGIAGLGSGIGAGITGASGAGVVAEDPNKFGTAIVFQALPQTQGLYGFLVAILILFV----FKTAPEWAMLAAG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1743172575 101 RSVGLSGLAAgFAIDIAGDAGVRATAQQPRLFMAMILTLIFPEVLGLYGPVVALIL 156
Cdd:PRK06271   79 LAVGLAGLSA-IGQGIAASAGLGAVAEDDSIFGKAMVFSVLPETQAIYGLLVAILL 133
 
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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