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Conserved domains on  [gi|1897364186|ref|WP_187150594|]
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ATP synthase F0 subunit C [Candidatus Mycoplasma haematobovis]

Protein Classification

ATP synthase F0 subunit C; ATP synthase subunit C( domain architecture ID 13031275)

ATP synthase Fo subunit c is part of the mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V), which produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain| ATP synthase subunit C is a component of membrane-bound Vo/Ao complexes of V/A-type ATP synthases that produce ATP from ADP in the presence of a proton gradient across the membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_c_NaATPase cd18184
F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type ...
 30-94 4.06e-22

F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type Na(+)-coupled ATP synthase and similar proteins.


:

Pssm-ID: 349424 [Multi-domain]  Cd Length: 65  Bit Score: 81.47  E-value: 4.06e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1897364186 30 SNIGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLC 94
Cdd:cd18184    1 AAIGAGLAMIAGIGPGIGQGYAAGKAVEAVGRNPEAEGKIRSTMILGAAVAETTAIYGLIIALLL 65
 
Name Accession Description Interval E-value
ATP-synt_Fo_c_NaATPase cd18184
F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type ...
 30-94 4.06e-22

F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type Na(+)-coupled ATP synthase and similar proteins.


Pssm-ID: 349424 [Multi-domain]  Cd Length: 65  Bit Score: 81.47  E-value: 4.06e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1897364186 30 SNIGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLC 94
Cdd:cd18184    1 AAIGAGLAMIAGIGPGIGQGYAAGKAVEAVGRNPEAEGKIRSTMILGAAVAETTAIYGLIIALLL 65
PRK07159 PRK07159
F0F1 ATP synthase subunit C; Validated
 18-96 3.59e-21

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 235949  Cd Length: 100  Bit Score: 80.32  E-value: 3.59e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897364186  18 QQQAQAQKDELGSNIGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:PRK07159   20 QKVAADSSGLKAAYIGAGLAMIGVIGVGLGQGYAFGKAVEAIARNPEAQKQVFKLLFIGSAISETSSIYALLVAFILIF 98
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 26-96 2.17e-16

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: 67.07  E-value: 2.17e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1897364186 26 DELGSNIGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:COG0636    2 EAAASAIGAGLAIgLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLF 73
ATP-synt_C pfam00137
ATP synthase subunit C;
32-93 1.98e-11

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 54.25  E-value: 1.98e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEvealIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:pfam00137  1 LGAGLAVgLAALGSGIGQGIAGAAAIEAIARQPK----LFGKMLIGAALAEALAIYGLVVALL 59
ATP_synt_c TIGR01260
ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a ...
 40-96 2.03e-09

ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a membrane associated multisubunit complex found in bacteria and organelles of higher eukaryotes, namely, mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. The functional role of subunit c, which is the part of F0 cluster, has been delineated in-vitro reconstitution experiments. Overall experimental proof exists that demonstrate the electrochemical gradient is converted into a rotational torque that leads to ATP synthesis. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130327  Cd Length: 58  Bit Score: 48.94  E-value: 2.03e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1897364186 40 AGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:TIGR01260  1 AAIGAAIGIGILGGKFLESAARQPELKPLLRTTMFIGMGLVDAIPMIAVVIALILLF 57
 
Name Accession Description Interval E-value
ATP-synt_Fo_c_NaATPase cd18184
F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type ...
 30-94 4.06e-22

F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type Na(+)-coupled ATP synthase and similar proteins.


Pssm-ID: 349424 [Multi-domain]  Cd Length: 65  Bit Score: 81.47  E-value: 4.06e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1897364186 30 SNIGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLC 94
Cdd:cd18184    1 AAIGAGLAMIAGIGPGIGQGYAAGKAVEAVGRNPEAEGKIRSTMILGAAVAETTAIYGLIIALLL 65
PRK07159 PRK07159
F0F1 ATP synthase subunit C; Validated
 18-96 3.59e-21

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 235949  Cd Length: 100  Bit Score: 80.32  E-value: 3.59e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1897364186  18 QQQAQAQKDELGSNIGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:PRK07159   20 QKVAADSSGLKAAYIGAGLAMIGVIGVGLGQGYAFGKAVEAIARNPEAQKQVFKLLFIGSAISETSSIYALLVAFILIF 98
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 32-93 1.01e-16

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: 67.80  E-value: 1.01e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:cd18121    2 LGAGLAIgLGAIGPGIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIALI 64
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 26-96 2.17e-16

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: 67.07  E-value: 2.17e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1897364186 26 DELGSNIGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:COG0636    2 EAAASAIGAGLAIgLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLF 73
PRK13469 PRK13469
F0F1 ATP synthase subunit C; Provisional
 30-96 3.59e-16

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184068  Cd Length: 79  Bit Score: 66.61  E-value: 3.59e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897364186 30 SNIGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:PRK13469  11 SAIGAGIAALAGIGAGIGIGIATGKAVEAVGRQPEASGKIMSTMLLGAALAEATAIYGLVIAIILLF 77
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 ...
 32-93 2.52e-15

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: 64.33  E-value: 2.52e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:cd00313    2 LGAGLAIgLAAIGAGIGIGLAGAAALEAIARQPEAAGKIFTTMLIGLALIESLAIYGLVIAFL 64
ATP-synt_C pfam00137
ATP synthase subunit C;
32-93 1.98e-11

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 54.25  E-value: 1.98e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEvealIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:pfam00137  1 LGAGLAVgLAALGSGIGQGIAGAAAIEAIARQPK----LFGKMLIGAALAEALAIYGLVVALL 59
ATP-synt_Fo_c_ATP5G3 cd18182
ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP ...
 32-93 6.49e-11

ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP synthase lipid-binding protein, ATP synthase proteolipid P3, ATP synthase proton-transporting mitochondrial F(o) complex subunit C3, ATPase protein 9, or ATPase subunit c) transports protons across the inner mitochondrial membrane to the F1-ATPase protruding on the matrix side, resulting in the generation of ATP.


Pssm-ID: 349422  Cd Length: 65  Bit Score: 52.90  E-value: 6.49e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1897364186 32 IGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:cd18182    3 IGAGLATIGLAGAGIGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFL 64
ATP_synt_c TIGR01260
ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a ...
 40-96 2.03e-09

ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a membrane associated multisubunit complex found in bacteria and organelles of higher eukaryotes, namely, mitochondria and chloroplast. This enzyme is principally involved in the synthesis of ATP from ADP and inorganic phosphate by coupling the energy derived from the proton electrochemical gradient across the biological membrane. A brief description of this multisubunit enzyme complex: F1 and F0 represent two major clusters of subunits. The functional role of subunit c, which is the part of F0 cluster, has been delineated in-vitro reconstitution experiments. Overall experimental proof exists that demonstrate the electrochemical gradient is converted into a rotational torque that leads to ATP synthesis. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 130327  Cd Length: 58  Bit Score: 48.94  E-value: 2.03e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1897364186 40 AGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:TIGR01260  1 AAIGAAIGIGILGGKFLESAARQPELKPLLRTTMFIGMGLVDAIPMIAVVIALILLF 57
atpH CHL00061
ATP synthase CF0 C subunit
 30-98 3.19e-09

ATP synthase CF0 C subunit


Pssm-ID: 177001  Cd Length: 81  Bit Score: 48.94  E-value: 3.19e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897364186 30 SNIGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKFGS 98
Cdd:CHL00061   9 SVIAAGLAVgLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFAN 78
PRK13468 PRK13468
F0F1 ATP synthase subunit C; Provisional
 27-96 4.23e-09

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184067  Cd Length: 82  Bit Score: 48.93  E-value: 4.23e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1897364186 27 ELGSNIGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:PRK13468   6 AVVSIIAAGLAVsIGAIGPALAEGRAVAAALDAIAQQPDAAGTISRTLFVGLAMIESMAIYCFVVAMILLF 76
PRK13471 PRK13471
F0F1 ATP synthase subunit C; Provisional
 28-96 6.27e-09

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184069  Cd Length: 85  Bit Score: 48.32  E-value: 6.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897364186 28 LGSNIGAGISLIAG-LGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:PRK13471  14 LGKYIGAGLCMGIGaIGPGIGEGNIGAHAMDAMARQPEMVGTITTRMLLADAVAETTGIYSLLIAFLILL 83
PRK07558 PRK07558
F0F1 ATP synthase subunit C; Validated
 32-97 2.02e-08

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 181027  Cd Length: 74  Bit Score: 46.89  E-value: 2.02e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1897364186 32 IGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKFG 97
Cdd:PRK07558   9 IGAGLACIGMAGAALGVGNIFGNYLSGALRNPSAADSQFGYLLIGAALAEALGIFSFLIALLLLFA 74
ATP-synt_Fo_c_ATPE cd18185
F-type proton-translocating ATPase subunit c (ATPE) and similar proteins; This family includes ...
 32-93 6.50e-08

F-type proton-translocating ATPase subunit c (ATPE) and similar proteins; This family includes subunit c of F-ATP synthase (also called ATP synthase F(o) sector subunit c, F-type ATPase subunit c, or F-ATPase subunit c) and similar proteins. It is a proton-translocating subunit of the ATP synthase encoded by gene atpE.


Pssm-ID: 349425  Cd Length: 65  Bit Score: 45.16  E-value: 6.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:cd18185    2 IAAGLAIgLAAIGAAIGDGLVGSKFIEGIARQPELRGKLRTNMFIGVGLVEAVPIIAVVIALL 64
PRK07354 PRK07354
F0F1 ATP synthase subunit C; Validated
 39-96 8.06e-08

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180942  Cd Length: 81  Bit Score: 45.60  E-value: 8.06e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 1897364186 39 IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKF 96
Cdd:PRK07354  19 LAAIGPGIGQGNAAGGAVEGIARQPEAEGKIRGTLLLSLAFMESLTIYGLVVALVLLF 76
ATP-synt_Fo_c_ATPH cd18183
F-type proton-translocating ATP synthase (ATPH) and similar proteins; This family includes ...
 30-98 8.73e-08

F-type proton-translocating ATP synthase (ATPH) and similar proteins; This family includes subunit c of chloroplast F-ATP synthase (F1Fo-ATP synthase), also known as ATP synthase F(o) sector subunit c (also called ATPase subunit III, F-type ATPase subunit c, or F-ATPase subunit c)and similar proteins. It is a proton-translocating subunit of the ATP synthase encoded by gene atpH.


Pssm-ID: 349423  Cd Length: 75  Bit Score: 45.22  E-value: 8.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1897364186 30 SNIGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKFGS 98
Cdd:cd18183    6 SVIAAGLAVgLAAIGPGIGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFAN 75
PRK06876 PRK06876
F0F1 ATP synthase subunit C; Validated
 32-97 2.56e-05

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180739  Cd Length: 78  Bit Score: 38.77  E-value: 2.56e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKFG 97
Cdd:PRK06876  10 IAAAIAIgLAALGAAIGIGLLGGKFLEGAARQPELIPMLQTKMFIGAGLVDAIPIIGVGIALLFLFA 76
PRK07874 PRK07874
ATP synthase F0 subunit C;
16-93 3.57e-05

ATP synthase F0 subunit C;


Pssm-ID: 169138  Cd Length: 80  Bit Score: 38.62  E-value: 3.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1897364186 16 VLQQQAQAQKDELGSNIGAGIsliAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:PRK07874   5 ILAQEATETTFTGLGAVGYGL---AAIGPGIGVGIVVGKALEGMARQPEMAGQLRTTMFLGIAFVEALALIGLVAGFL 79
ATP-synt_Vo_Ao_c cd18120
Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase ...
 31-93 5.64e-05

Membrane-bound Vo/Ao complexes of V/A-type ATP synthases, subunit c; Vo/Ao-ATP synthase subunit c. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPases) is exclusively found in archaea and functions like the F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. The V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. The V1 complex consists of three A and three B subunits, two G subunits plus the C, D, E, F, and H subunits. The Vo complex consists of five different subunits: a, c, c', c'', and d. The Ao/A1 complexes are composed of nine subunits in a stoichiometry of A(3):B(3):C:D:E:F:H(2):a:c(x). ATP is synthesized on the A3:B3 hexamer and the energy released during that process is transferred to the Ao complex, which consists of the C-terminal segment of subunit a and subunit c.


Pssm-ID: 349413  Cd Length: 62  Bit Score: 37.50  E-value: 5.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1897364186 31 NIGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEvealIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:cd18120    2 YLGAALAVgLSCLGAGIAVGMVGAAAIGAIAEKPE----LFGKALIFVGLAEGLAIYGLIVAIL 61
PRK08482 PRK08482
F0F1 ATP synthase subunit C; Validated
 30-93 7.31e-04

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 181444  Cd Length: 105  Bit Score: 35.92  E-value: 7.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1897364186  30 SNIGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:PRK08482   32 SVLAAGIGLgIAALGGAIGMGNTAAATIAGTARNPGLGGKLMTTMFIALAMIEAQVIYALVIALI 96
ATP-synt_Vo_Ao_c_NTPK_rpt2 cd18180
V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+) ...
 32-93 1.15e-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: 349420  Cd Length: 64  Bit Score: 34.35  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVealiFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:cd18180    5 LGAGLPVgIVGLFSAIYQGKVAAAGIGAVAKRPEE----FGKAIILAAMVETYAILGLLISIL 63
ATP9 MTH00222
ATP synthase F0 subunit 9; Provisional
 32-97 1.25e-03

ATP synthase F0 subunit 9; Provisional


Pssm-ID: 164765 [Multi-domain]  Cd Length: 77  Bit Score: 34.44  E-value: 1.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1897364186 32 IGAGISLIAGLGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESVAIYGLIVALLCKFG 97
Cdd:MTH00222  11 VGAGAATIGAAGSGAGIGTVFGNLIIGYARNPSLKQQLFTYAILGFAISEAMGLFCLMMAFLILFA 76
ATP-synt_Vo_Ao_c_NTPK_rpt1 cd18179
V-type sodium ATPase subunit K (NTPK) and similar proteins; NTPK (also called Na(+) ...
 32-93 4.45e-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: 32.86  E-value: 4.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1897364186 32 IGAGISLI-AGLGAAIGQGYIGGKAVEALARNPEVealiFRQYIVGAAVCESVAIYGLIVALL 93
Cdd:cd18179    4 IGAALAVGlAGIGSAIGVGIAGQAAAGVLAEKPEK----FGKLLVLQALPGTQGIYGFVIAFL 62
ATP-synt_Vo_Ao_c_TtATPase_like cd18181
Thermus thermophilus V/A-ATPase and similar proteins; This family includes a group of ...
 32-94 4.79e-03

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: 32.52  E-value: 4.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1897364186 32 IGAGISL-IAGLGAAIGQGYIGGKAVEALARNPEVealiFRQYIVGAAVCESVAIYGLIVALLC 94
Cdd:cd18181    3 IGAGLAIgLAAIGTGWAQSRIGAAAVGAIAEKPEL----FGTALILTAIPETLVILGFVIAFLL 62
PRK05880 PRK05880
F0F1 ATP synthase subunit C; Validated
 29-83 8.63e-03

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180303  Cd Length: 81  Bit Score: 32.48  E-value: 8.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1897364186 29 GSNIGAGISLIAG-LGAAIGQGYIGGKAVEALARNPEVEALIFRQYIVGAAVCESV 83
Cdd:PRK05880   8 GALIGGGLIMAGGaIGAGIGDGVAGNALISGVARQPEAQGRLFTPFFITVGLVEAA 63
 
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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