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Conserved domains on  [gi|2535553117|ref|WP_292361370|]
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MULTISPECIES: F0F1 ATP synthase subunit C [unclassified Methylophaga]

Protein Classification

FoF1 ATP synthase subunit c( domain architecture ID 10012848)

FoF1 ATP synthase subunit c is part of the membrane proton channel of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane

Gene Ontology:  GO:0045263|GO:0046933|GO:0008289
PubMed:  26621635

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06876 PRK06876
F0F1 ATP synthase subunit C; Validated
1-76 3.41e-23

F0F1 ATP synthase subunit C; Validated


:

Pssm-ID: 180739  Cd Length: 78  Bit Score: 83.45  E-value: 3.41e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2535553117  1 MDMGLVYIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFAVA 76
Cdd:PRK06876   3 LIMGLTAIAAAIAIGLAALGAAIGIGLLGGKFLEGAARQPELIPMLQTKMFIGAGLVDAIPIIGVGIALLFLFANP 78
 
Name Accession Description Interval E-value
PRK06876 PRK06876
F0F1 ATP synthase subunit C; Validated
1-76 3.41e-23

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180739  Cd Length: 78  Bit Score: 83.45  E-value: 3.41e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2535553117  1 MDMGLVYIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFAVA 76
Cdd:PRK06876   3 LIMGLTAIAAAIAIGLAALGAAIGIGLLGGKFLEGAARQPELIPMLQTKMFIGAGLVDAIPIIGVGIALLFLFANP 78
ATP-synt_Fo_c_ATPE cd18185
F-type proton-translocating ATPase subunit c (ATPE) and similar proteins; This family includes ...
7-70 1.40e-16

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: 66.35  E-value: 1.40e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535553117  7 YIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMY 70
Cdd:cd18185    1 LIAAGLAIGLAAIGAAIGDGLVGSKFIEGIARQPELRGKLRTNMFIGVGLVEAVPIIAVVIALL 64
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
1-75 1.11e-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: 1.11e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2535553117  1 MDMGLVYIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFAV 75
Cdd:COG0636    1 MEAAASAIGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFAN 75
ATP_synt_c TIGR01260
ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a ...
18-74 2.56e-14

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: 60.50  E-value: 2.56e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2535553117 18 ALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFA 74
Cdd:TIGR01260  2 AIGAAIGIGILGGKFLESAARQPELKPLLRTTMFIGMGLVDAIPMIAVVIALILLFA 58
ATP-synt_C pfam00137
ATP synthase subunit C;
8-70 8.80e-03

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 31.14  E-value: 8.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2535553117  8 IAGALMIGLGALGAAVGVGLLGGRFLEAAARQPElvpmLRTQFFLVAGLVDAVPMIAVGLAMY 70
Cdd:pfam00137  1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPK----LFGKMLIGAALAEALAIYGLVVALL 59
 
Name Accession Description Interval E-value
PRK06876 PRK06876
F0F1 ATP synthase subunit C; Validated
1-76 3.41e-23

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180739  Cd Length: 78  Bit Score: 83.45  E-value: 3.41e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2535553117  1 MDMGLVYIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFAVA 76
Cdd:PRK06876   3 LIMGLTAIAAAIAIGLAALGAAIGIGLLGGKFLEGAARQPELIPMLQTKMFIGAGLVDAIPIIGVGIALLFLFANP 78
ATP-synt_Fo_c_ATPE cd18185
F-type proton-translocating ATPase subunit c (ATPE) and similar proteins; This family includes ...
7-70 1.40e-16

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: 66.35  E-value: 1.40e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535553117  7 YIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMY 70
Cdd:cd18185    1 LIAAGLAIGLAAIGAAIGDGLVGSKFIEGIARQPELRGKLRTNMFIGVGLVEAVPIIAVVIALL 64
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
1-75 1.11e-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: 1.11e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2535553117  1 MDMGLVYIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFAV 75
Cdd:COG0636    1 MEAAASAIGAGLAIGLAAIGAGIGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFAN 75
ATP_synt_c TIGR01260
ATP synthase, F0 subunit c; This model describes the subunit c in F1/F0-ATP synthase, a ...
18-74 2.56e-14

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: 60.50  E-value: 2.56e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2535553117 18 ALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFA 74
Cdd:TIGR01260  2 AIGAAIGIGILGGKFLESAARQPELKPLLRTTMFIGMGLVDAIPMIAVVIALILLFA 58
PRK13464 PRK13464
F0F1 ATP synthase subunit B;
4-74 3.96e-08

F0F1 ATP synthase subunit B;


Pssm-ID: 184065  Cd Length: 101  Bit Score: 46.11  E-value: 3.96e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2535553117   4 GLVYIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFA 74
Cdd:PRK13464   13 GLTAVAVALLISLPALGTAIGFGVLGGKYLEGVARQPELGGMLLGRMFIVAAFVDAFAAISIAIGFLVLYA 83
PRK05880 PRK05880
F0F1 ATP synthase subunit C; Validated
8-77 1.39e-06

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180303  Cd Length: 81  Bit Score: 41.73  E-value: 1.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535553117  8 IAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFAVAG 77
Cdd:PRK05880  11 IGGGLIMAGGAIGAGIGDGVAGNALISGVARQPEAQGRLFTPFFITVGLVEAAYFINLAFMALFVFATPV 80
PRK07874 PRK07874
ATP synthase F0 subunit C;
10-63 1.37e-05

ATP synthase F0 subunit C;


Pssm-ID: 169138  Cd Length: 80  Bit Score: 39.01  E-value: 1.37e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2535553117 10 GALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMI 63
Cdd:PRK07874  19 GAVGYGLAAIGPGIGVGIVVGKALEGMARQPEMAGQLRTTMFLGIAFVEALALI 72
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
7-69 1.77e-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: 38.14  E-value: 1.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2535553117  7 YIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAM 69
Cdd:cd18121    1 ALGAGLAIGLGAIGPGIGIGLAAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIAL 63
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 ...
7-60 8.26e-05

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: 36.60  E-value: 8.26e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2535553117  7 YIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAV 60
Cdd:cd00313    1 ALGAGLAIGLAAIGAGIGIGLAGAAALEAIARQPEAAGKIFTTMLIGLALIESL 54
PRK13466 PRK13466
F0F1 ATP synthase subunit C; Provisional
10-68 4.70e-04

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 172066  Cd Length: 66  Bit Score: 34.93  E-value: 4.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 2535553117 10 GALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLA 68
Cdd:PRK13466   4 GALALGLACLGVSIGEGLLVASYLSSTARQPEMQSKLMAGVFLGVAFIEGTFFVTLAMT 62
PRK13471 PRK13471
F0F1 ATP synthase subunit C; Provisional
7-75 1.16e-03

F0F1 ATP synthase subunit C; Provisional


Pssm-ID: 184069  Cd Length: 85  Bit Score: 34.07  E-value: 1.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535553117  7 YIAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFAV 75
Cdd:PRK13471  17 YIGAGLCMGIGAIGPGIGEGNIGAHAMDAMARQPEMVGTITTRMLLADAVAETTGIYSLLIAFLILLVL 85
atpH CHL00061
ATP synthase CF0 C subunit
8-74 3.52e-03

ATP synthase CF0 C subunit


Pssm-ID: 177001  Cd Length: 81  Bit Score: 32.76  E-value: 3.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2535553117  8 IAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFA 74
Cdd:CHL00061  11 IAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFA 77
PRK07354 PRK07354
F0F1 ATP synthase subunit C; Validated
8-74 4.65e-03

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180942  Cd Length: 81  Bit Score: 32.50  E-value: 4.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2535553117  8 IAGALMIGLGALGAAVGVGLLGGRFLEAAARQPELVPMLRTQFFLVAGLVDAVPMIAVGLAMYVLFA 74
Cdd:PRK07354  11 VAAALAVGLAAIGPGIGQGNAAGGAVEGIARQPEAEGKIRGTLLLSLAFMESLTIYGLVVALVLLFA 77
ATP-synt_C pfam00137
ATP synthase subunit C;
8-70 8.80e-03

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 31.14  E-value: 8.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2535553117  8 IAGALMIGLGALGAAVGVGLLGGRFLEAAARQPElvpmLRTQFFLVAGLVDAVPMIAVGLAMY 70
Cdd:pfam00137  1 LGAGLAVGLAALGSGIGQGIAGAAAIEAIARQPK----LFGKMLIGAALAEALAIYGLVVALL 59
 
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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