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Conserved domains on  [gi|2133473693|ref|XP_044962787|]
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ATP synthase subunit 9, mitochondrial [Hordeum vulgare subsp. vulgare]

Protein Classification

ATP synthase subunit C family protein( domain architecture ID 13031262)

ATP synthase subunit C family protein similar to bacterial ATP synthase subunit c and eukaryotic mitochondrial ATP synthase subunit 9, which are components of non-enzymatic membrane component (F0) of F-type ATPases that produce ATP from ADP in the presence of a proton or sodium gradient

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATP-synt_Fo_c_ATP5G3 cd18182
ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP ...
 55-103 8.91e-21

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: 78.71  E-value: 8.91e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLI 103
Cdd:cd18182    17 IGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI 65
 
Name Accession Description Interval E-value
ATP-synt_Fo_c_ATP5G3 cd18182
ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP ...
 55-103 8.91e-21

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: 78.71  E-value: 8.91e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLI 103
Cdd:cd18182    17 IGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI 65
ATP9 MTH00222
ATP synthase F0 subunit 9; Provisional
 33-105 1.75e-16

ATP synthase F0 subunit 9; Provisional


Pssm-ID: 164765 [Multi-domain]  Cd Length: 77  Bit Score: 67.95  E-value: 1.75e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2133473693  33 EMLEGAKSIGAGAATIALAGAAVGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLISF 105
Cdd:MTH00222    3 EILTAAKFVGAGAATIGAAGSGAGIGTVFGNLIIGYARNPSLKQQLFTYAILGFAISEAMGLFCLMMAFLILF 75
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 55-106 2.68e-10

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: 52.05  E-value: 2.68e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLISFV 106
Cdd:COG0636    23 IGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFA 74
ATP-synt_C pfam00137
ATP synthase subunit C;
54-103 1.20e-06

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 42.31  E-value: 1.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2133473693  54 AVGIGNVLSSLIHSVARNPSLakqsFGYAILGFALTEAIALFAPMMAFLI 103
Cdd:pfam00137  15 GIGQGIAGAAAIEAIARQPKL----FGKMLIGAALAEALAIYGLVVALLL 60
 
Name Accession Description Interval E-value
ATP-synt_Fo_c_ATP5G3 cd18182
ATP synthase F(0) complex subunit C3 (ATP5G3) and similar proteins; ATP5G3 (also called ATP ...
 55-103 8.91e-21

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: 78.71  E-value: 8.91e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLI 103
Cdd:cd18182    17 IGIGNVFGSLINGVARNPSAKQQLFTYAILGFALTEAIGLFALMVAFLI 65
ATP9 MTH00222
ATP synthase F0 subunit 9; Provisional
 33-105 1.75e-16

ATP synthase F0 subunit 9; Provisional


Pssm-ID: 164765 [Multi-domain]  Cd Length: 77  Bit Score: 67.95  E-value: 1.75e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2133473693  33 EMLEGAKSIGAGAATIALAGAAVGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLISF 105
Cdd:MTH00222    3 EILTAAKFVGAGAATIGAAGSGAGIGTVFGNLIIGYARNPSLKQQLFTYAILGFAISEAMGLFCLMMAFLILF 75
PRK07558 PRK07558
F0F1 ATP synthase subunit C; Validated
 34-106 9.18e-12

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 181027  Cd Length: 74  Bit Score: 55.75  E-value: 9.18e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2133473693  34 MLEGAKSIGAGAATIALAGAAVGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLISFV 106
Cdd:PRK07558    2 DAEALKFIGAGLACIGMAGAALGVGNIFGNYLSGALRNPSAADSQFGYLLIGAALAEALGIFSFLIALLLLFA 74
AtpE COG0636
FoF1-type ATP synthase, membrane subunit c/Archaeal/vacuolar-type H+-ATPase, subunit K [Energy ...
 55-106 2.68e-10

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: 52.05  E-value: 2.68e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLISFV 106
Cdd:COG0636    23 IGIGLAGGKALEAIARQPEAAGKLQTTMFIGAALIEALAIYALVIALILLFA 74
ATP-synt_Fo_c cd18121
membrane-bound Fo complex of F-ATP synthase, subunit c; Subunit c (also called subunit 9, or ...
 55-103 2.14e-09

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: 49.69  E-value: 2.14e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLI 103
Cdd:cd18121    17 IGIGLAAAKALEGIARQPEAAGKIRTTMIIGLALIESLAIYALVIALIL 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 ...
 55-103 8.58e-09

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: 48.15  E-value: 8.58e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLI 103
Cdd:cd00313    17 IGIGLAGAAALEAIARQPEAAGKIFTTMLIGLALIESLAIYGLVIAFLL 65
ATP-synt_C pfam00137
ATP synthase subunit C;
54-103 1.20e-06

ATP synthase subunit C;


Pssm-ID: 459687  Cd Length: 60  Bit Score: 42.31  E-value: 1.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2133473693  54 AVGIGNVLSSLIHSVARNPSLakqsFGYAILGFALTEAIALFAPMMAFLI 103
Cdd:pfam00137  15 GIGQGIAGAAAIEAIARQPKL----FGKMLIGAALAEALAIYGLVVALLL 60
ATP-synt_Fo_c_ATPE cd18185
F-type proton-translocating ATPase subunit c (ATPE) and similar proteins; This family includes ...
 55-107 1.12e-04

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: 37.46  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIalfaPMMAFLISFVF 107
Cdd:cd18185    17 IGDGLVGSKFIEGIARQPELRGKLRTNMFIGVGLVEAV----PIIAVVIALLL 65
PRK07874 PRK07874
ATP synthase F0 subunit C;
55-102 3.08e-04

ATP synthase F0 subunit C;


Pssm-ID: 169138  Cd Length: 80  Bit Score: 36.70  E-value: 3.08e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFL 102
Cdd:PRK07874   32 IGVGIVVGKALEGMARQPEMAGQLRTTMFLGIAFVEALALIGLVAGFL 79
PRK07159 PRK07159
F0F1 ATP synthase subunit C; Validated
 55-106 6.39e-04

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 235949  Cd Length: 100  Bit Score: 36.41  E-value: 6.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLISFV 106
Cdd:PRK07159   48 LGQGYAFGKAVEAIARNPEAQKQVFKLLFIGSAISETSSIYALLVAFILIFV 99
PRK06876 PRK06876
F0F1 ATP synthase subunit C; Validated
 55-106 8.19e-03

F0F1 ATP synthase subunit C; Validated


Pssm-ID: 180739  Cd Length: 78  Bit Score: 32.60  E-value: 8.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2133473693  55 VGIGNVLSSLIHSVARNPSLAKQSFGYAILGFALTEAIALFAPMMAFLISFV 106
Cdd:PRK06876   25 IGIGLLGGKFLEGAARQPELIPMLQTKMFIGAGLVDAIPIIGVGIALLFLFA 76
 
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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