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Conserved domains on  [gi|1162405765|gb|OPX20477|]
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MAG: ATP synthase F0 subunit C [Desulfobacca sp. 4484_104]

Protein Classification

ATP synthase F0 subunit C( domain architecture ID 13031112)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 39-88 2.82e-15

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: 64.33  E-value: 2.82e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:cd18121    16 GIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIALIL 65
 
Name Accession Description Interval E-value
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 39-88 2.82e-15

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: 64.33  E-value: 2.82e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:cd18121    16 GIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIALIL 65
PRK07354 PRK07354
F0F1 ATP synthase subunit C; Validated
 21-95 1.87e-14

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180942  Cd Length: 81  Bit Score: 62.93  E-value: 1.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162405765  21 SATVIAAGIGIGIAAFGTGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYAYPMA 95
Cdd:PRK07354    7 AASVVAAALAVGLAAIGPGIGQGNAAGGAVEGIARQPEAEGKIRGTLLLSLAFMESLTIYGLVVALVLLFANPFA 81
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 38-91 2.77e-14

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: 62.06  E-value: 2.77e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:COG0636    21 AGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFA 74
ATP_synt_c TIGR01260
ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a ...
 38-91 3.83e-08

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: 45.86  E-value: 3.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:TIGR01260   5 AAIGIGILGGKFLESAARQPELKPLLRTTMFIGMGLVDAIPMIAVVIALILLFA 58
ATP-synt_C pfam00137
ATP synthase subunit C;
38-88 7.70e-06

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 40.00  E-value: 7.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPeasgKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:pfam00137  14 SGIGQGIAGAAAIEAIARQP----KLFGKMLIGAALAEALAIYGLVVALLL 60
 
Name Accession Description Interval E-value
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 39-88 2.82e-15

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: 64.33  E-value: 2.82e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:cd18121    16 GIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIALIL 65
PRK07354 PRK07354
F0F1 ATP synthase subunit C; Validated
 21-95 1.87e-14

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180942  Cd Length: 81  Bit Score: 62.93  E-value: 1.87e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1162405765  21 SATVIAAGIGIGIAAFGTGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYAYPMA 95
Cdd:PRK07354    7 AASVVAAALAVGLAAIGPGIGQGNAAGGAVEGIARQPEAEGKIRGTLLLSLAFMESLTIYGLVVALVLLFANPFA 81
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 38-91 2.77e-14

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: 62.06  E-value: 2.77e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:COG0636    21 AGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFA 74
atpH CHL00061
ATP synthase CF0 C subunit
 39-95 2.89e-14

ATP synthase CF0 C subunit


Pssm-ID: 177001  Cd Length: 81  Bit Score: 62.42  E-value: 2.89e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYAYPMA 95
Cdd:CHL00061   25 GVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV 81
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 ...
 39-88 2.64e-13

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: 59.32  E-value: 2.64e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:cd00313    16 GIGIGLAGAAALEAIARQPEAAGKIFTTMLIGLALIESLAIYGLVIAFLL 65
PRK13469 PRK13469
F0F1 ATP synthase subunit C; Provisional
 39-91 2.95e-12

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184068  Cd Length: 79  Bit Score: 56.98  E-value: 2.95e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:PRK13469   26 GIGIGIATGKAVEAVGRQPEASGKIMSTMLLGAALAEATAIYGLVIAIILLFV 78
ATP-synt_Fo_c_ATPH cd18183
F-type proton-translocating ATP synthase (ATPH) and similar proteins; This family includes ...
 21-91 3.68e-12

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: 56.77  E-value: 3.68e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162405765  21 SATVIAAGIGIGIAAFGTGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:cd18183     4 AASVIAAGLAVGLAAIGPGIGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFA 74
PRK13468 PRK13468
F0F1 ATP synthase subunit C; Provisional
 40-96 4.18e-12

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184067  Cd Length: 82  Bit Score: 56.63  E-value: 4.18e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1162405765  40 IGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYAYPMAK 96
Cdd:PRK13468   26 LAEGRAVAAALDAIAQQPDAAGTISRTLFVGLAMIESMAIYCFVVAMILLFANPFWN 82
ATP-synt_Fo_c_NaATPase cd18184
F-type sodium ion-translocating ATP synthase and similar proteins; This family includes F-type ...
 38-88 5.90e-12

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: 56.05  E-value: 5.90e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:cd18184    15 PGIGQGYAAGKAVEAVGRNPEAEGKIRSTMILGAAVAETTAIYGLIIALLL 65
PRK07159 PRK07159
F0F1 ATP synthase subunit C; Validated
 39-90 8.47e-10

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 235949  Cd Length: 100  Bit Score: 51.43  E-value: 8.47e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILY 90
Cdd:PRK07159   47 GLGQGYAFGKAVEAIARNPEAQKQVFKLLFIGSAISETSSIYALLVAFILIF 98
ATP_synt_c TIGR01260
ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a ...
 38-91 3.83e-08

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: 45.86  E-value: 3.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:TIGR01260   5 AAIGIGILGGKFLESAARQPELKPLLRTTMFIGMGLVDAIPMIAVVIALILLFA 58
PRK08482 PRK08482
F0F1 ATP synthase subunit C; Validated
 33-94 6.20e-08

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 181444  Cd Length: 105  Bit Score: 46.70  E-value: 6.20e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1162405765  33 IAAFGTGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYAYPM 94
Cdd:PRK08482   42 IAALGGAIGMGNTAAATIAGTARNPGLGGKLMTTMFIALAMIEAQVIYALVIALIALYANPF 103
ATP-synt_Fo_c_ATPE cd18185
F-type proton-translocating ATPase subunit c (ATPE) and similar proteins; This family includes ...
 38-88 1.12e-06

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: 42.46  E-value: 1.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:cd18185    15 AAIGDGLVGSKFIEGIARQPELRGKLRTNMFIGVGLVEAVPIIAVVIALLL 65
PRK07874 PRK07874
ATP synthase F0 subunit C;
39-87 2.95e-06

ATP synthase F0 subunit C;


Pssm-ID: 169138  Cd Length: 80  Bit Score: 41.71  E-value: 2.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALI 87
Cdd:PRK07874   31 GIGVGIVVGKALEGMARQPEMAGQLRTTMFLGIAFVEALALIGLVAGFL 79
ATP-synt_C pfam00137
ATP synthase subunit C;
38-88 7.70e-06

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 40.00  E-value: 7.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPeasgKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:pfam00137  14 SGIGQGIAGAAAIEAIARQP----KLFGKMLIGAALAEALAIYGLVVALLL 60
PRK07558 PRK07558
F0F1 ATP synthase subunit C; Validated
 38-91 2.30e-05

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 181027  Cd Length: 74  Bit Score: 39.18  E-value: 2.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:PRK07558   21 AALGVGNIFGNYLSGALRNPSAADSQFGYLLIGAALAEALGIFSFLIALLLLFA 74
PRK06876 PRK06876
F0F1 ATP synthase subunit C; Validated
 37-93 4.62e-05

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180739  Cd Length: 78  Bit Score: 38.38  E-value: 4.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1162405765  37 GTGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYAYP 93
Cdd:PRK06876   22 GAAIGIGLLGGKFLEGAARQPELIPMLQTKMFIGAGLVDAIPIIGVGIALLFLFANP 78
ATP-synt_Fo_c_ATP5G3 cd18182
ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP ...
 39-88 1.56e-04

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: 36.72  E-value: 1.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1162405765  39 GIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALII 88
Cdd:cd18182    16 GIGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI 65
PRK13471 PRK13471
F0F1 ATP synthase subunit C; Provisional
 38-91 6.36e-04

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184069  Cd Length: 85  Bit Score: 35.61  E-value: 6.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYA 91
Cdd:PRK13471   31 PGIGEGNIGAHAMDAMARQPEMVGTITTRMLLADAVAETTGIYSLLIAFLILLV 84
PRK05880 PRK05880
F0F1 ATP synthase subunit C; Validated
 38-95 3.16e-03

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180303  Cd Length: 81  Bit Score: 33.64  E-value: 3.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1162405765  38 TGIGQGIAIQRAVEGIARNPEASGKITVTMLIGLAMIESLCIYALVVALIILYAYPMA 95
Cdd:PRK05880   24 AGIGDGVAGNALISGVARQPEAQGRLFTPFFITVGLVEAAYFINLAFMALFVFATPVK 81
 
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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