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Conserved domains on  [gi|1371545289|ref|NP_001348462|]
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V-type proton ATPase 16 kDa proteolipid subunit c isoform c [Mus musculus]

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
 1-91 2.11e-37

F0F1 ATP synthase subunit C; Provisional


The actual alignment was detected with superfamily member TIGR01100:

Pssm-ID: 469780  Cd Length: 108  Bit Score: 122.88  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDG--ITLYRSFLQLGAGLSVGLSGLA 78
Cdd:TIGR01100  16 LGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSLKPKsnYSLYKGFIHLGAGLAVGLSGLA 95

                          90
                  ....*....|...
gi 1371545289  79 AGFAIGIVGDAGV 91
Cdd:TIGR01100  96 AGFAIGIVGDAGV 108
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 59-126 5.68e-29

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: 99.89  E-value: 5.68e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371545289  59 LYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILS 126
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 ...
 1-91 2.11e-37

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: 122.88  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDG--ITLYRSFLQLGAGLSVGLSGLA 78
Cdd:TIGR01100  16 LGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSLKPKsnYSLYKGFIHLGAGLAVGLSGLA 95

                          90
                  ....*....|...
gi 1371545289  79 AGFAIGIVGDAGV 91
Cdd:TIGR01100  96 AGFAIGIVGDAGV 108
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 59-126 5.68e-29

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: 99.89  E-value: 5.68e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371545289  59 LYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILS 126
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 ...
 1-53 2.61e-21

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: 80.66  E-value: 2.61e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSL 53
Cdd:cd18175    16 LGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISNNI 68
ATP-synt_C pfam00137
ATP synthase subunit C;
66-125 6.51e-10

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 51.17  E-value: 6.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:pfam00137   1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
PRK06558 PRK06558
V-type ATP synthase subunit K; Validated
 1-125 1.36e-08

V-type ATP synthase subunit K; Validated


Pssm-ID: 235830 [Multi-domain]  Cd Length: 159  Bit Score: 49.99  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDGITLYRSFLQLGAGLSVGLSGLAAG 80
Cdd:PRK06558   30 IGSAKGVGKAGEAAAGLLTEEPEKFGKALILQLLPGTQGLYGFVIGFLIWQKITPELSLAQGLAYFAACLPIAIVGLFSA 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1371545289  81 FAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:PRK06558  110 ISQGKVAAAGIQILAKRPEEFTKGIILAAMVETYAILAFVVSFLL 154
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 66-125 5.50e-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: 5.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQP----RLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:COG0636     8 IGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPeaagKLQTTMFIGAALIEALAIYALVIALIL 71
ATP-synt_C pfam00137
ATP synthase subunit C;
1-49 1.39e-04

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 37.30  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLI 49
Cdd:pfam00137  12 LGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
PRK06251 PRK06251
V-type ATP synthase subunit K; Validated
 64-125 7.51e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 235752  Cd Length: 102  Bit Score: 33.56  E-value: 7.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371545289  64 LQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:PRK06251   36 INIGAGLAVGLAAIGAGIAVGMAAAAGIGVLTERRDMFGTVLIFVAIGEGIAVYGILFAVLM 97
 
Name Accession Description Interval E-value
V_ATP_synt_C TIGR01100
vacuolar ATP synthase 16 kDa proteolipid subunit; This model describes the vacuolar ATP ...
 1-91 2.11e-37

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: 122.88  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDG--ITLYRSFLQLGAGLSVGLSGLA 78
Cdd:TIGR01100  16 LGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIAGSLKPKsnYSLYKGFIHLGAGLAVGLSGLA 95

                          90
                  ....*....|...
gi 1371545289  79 AGFAIGIVGDAGV 91
Cdd:TIGR01100  96 AGFAIGIVGDAGV 108
ATP-synt_Vo_c_ATP6C_rpt2 cd18176
V-type proton ATPase 16 kDa proteolipid subunit (ATP6C/ATP6V0C/ATP6L/ATPL) and similar ...
 59-126 5.68e-29

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: 99.89  E-value: 5.68e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371545289  59 LYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILS 126
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 ...
 1-53 2.61e-21

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: 80.66  E-value: 2.61e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSL 53
Cdd:cd18175    16 LGAAYGTAKSGVGIAAMGVMRPELIMKSIIPVVMAGILGIYGLVVAVLISNNI 68
ATP-synt_C pfam00137
ATP synthase subunit C;
66-125 6.51e-10

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 51.17  E-value: 6.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
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 ...
 66-125 6.78e-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: 48.68  E-value: 6.78e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:cd18120     3 LGAALAVGLSCLGAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI 62
PRK06558 PRK06558
V-type ATP synthase subunit K; Validated
 1-125 1.36e-08

V-type ATP synthase subunit K; Validated


Pssm-ID: 235830 [Multi-domain]  Cd Length: 159  Bit Score: 49.99  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDGITLYRSFLQLGAGLSVGLSGLAAG 80
Cdd:PRK06558   30 IGSAKGVGKAGEAAAGLLTEEPEKFGKALILQLLPGTQGLYGFVIGFLIWQKITPELSLAQGLAYFAACLPIAIVGLFSA 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1371545289  81 FAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:PRK06558  110 ISQGKVAAAGIQILAKRPEEFTKGIILAAMVETYAILAFVVSFLL 154
ATP-synt_Vo_c_ATP6F_rpt2 cd18178
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 62-125 4.79e-08

V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.


Pssm-ID: 349418  Cd Length: 65  Bit Score: 46.35  E-value: 4.79e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371545289  62 SFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:cd18178     2 GYALFGAGLTVGFSNLACGISVGIIGSGAALADAKNPSLFVKILIVEIFASAIGLFGLIVGILM 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 ...
 66-125 1.44e-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: 42.76  E-value: 1.44e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQP----RLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:cd00313     2 LGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPeaagKIFTTMLIGLALIESLAIYGLVIAFLL 65
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 66-125 3.36e-06

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: 41.60  E-value: 3.36e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQP----RLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:cd18121     2 LGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPeaagKIRTTMIIGLALIESLAIYALVIALIL 65
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 66-125 5.50e-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: 5.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQP----RLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:COG0636     8 IGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPeaagKLQTTMFIGAALIEALAIYALVIALIL 71
ATP-synt_C pfam00137
ATP synthase subunit C;
1-49 1.39e-04

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 37.30  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1371545289   1 MGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLI 49
Cdd:pfam00137  12 LGSGIGQGIAGAAAIEAIARQPKLFGKMLIGAALAEALAIYGLVVALLL 60
ATP-synt_Vo_Ao_c cd18120
Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase ...
 2-49 3.76e-04

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: 36.35  E-value: 3.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1371545289   2 GAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLI 49
Cdd:cd18120    15 GAGIAVGMVGAAAIGAIAEKPELFGKALIFVGLAEGLAIYGLIVAILI 62
ATP-synt_Vo_c_ATP6F_rpt1 cd18177
V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F ...
 66-125 1.13e-03

V-type proton ATPase 21 kDa proteolipid subunit (ATP6F/ATP6V0B) and similar proteins; ATP6F (also called V-ATPase 21 kDa proteolipid subunit, or vacuolar proton pump 21 kDa proteolipid subunit) is a proton-conducting pore forming subunit of the membrane integral Vo complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.


Pssm-ID: 349417  Cd Length: 63  Bit Score: 34.93  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371545289  66 LGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:cd18177     4 LGIGLSIGLSVVGAAWGIFITGSSIVGAGVKAPRIRTKNLISIIFCEAVAIYGIIMAIVL 63
PRK06251 PRK06251
V-type ATP synthase subunit K; Validated
 64-125 7.51e-03

V-type ATP synthase subunit K; Validated


Pssm-ID: 235752  Cd Length: 102  Bit Score: 33.56  E-value: 7.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1371545289  64 LQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIL 125
Cdd:PRK06251   36 INIGAGLAVGLAAIGAGIAVGMAAAAGIGVLTERRDMFGTVLIFVAIGEGIAVYGILFAVLM 97
 
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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