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Conserved domains on  [gi|156530123|gb|ABU75158|]
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AtpB, partial (chloroplast) [Castela tortuosa]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
atpB super family cl33325
ATP synthase CF1 beta subunit
 1-111 3.55e-85

ATP synthase CF1 beta subunit


The actual alignment was detected with superfamily member CHL00060:

Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 255.74  E-value: 3.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:CHL00060 384 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELD 463

                         90       100       110
                 ....*....|....*....|....*....|.
gi 156530123  81 GLPEQAFYLVGNIDEVTAKATNLEMESNLKK 111
Cdd:CHL00060 464 GLPEQAFYLVGNIDEATAKAANLEVESKLKK 494
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-111 3.55e-85

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 255.74  E-value: 3.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:CHL00060 384 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELD 463

                         90       100       110
                 ....*....|....*....|....*....|.
gi 156530123  81 GLPEQAFYLVGNIDEVTAKATNLEMESNLKK 111
Cdd:CHL00060 464 GLPEQAFYLVGNIDEATAKAANLEVESKLKK 494
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-107 5.52e-72

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 221.12  E-value: 5.52e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:COG0055  362 AREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYD 441

                         90       100
                 ....*....|....*....|....*..
gi 156530123  81 GLPEQAFYLVGNIDEVTAKATNLEMES 107
Cdd:COG0055  442 DLPEQAFYMVGTIDEAVEKAKKLKAEA 468
ATP-synt_F1_beta_C cd18110
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ...
 1-99 2.32e-70

F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.


Pssm-ID: 349745 [Multi-domain]  Cd Length: 108  Bit Score: 205.40  E-value: 2.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:cd18110   10 ARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGFKEILDGEYD 89

                         90
                 ....*....|....*....
gi 156530123  81 GLPEQAFYLVGNIDEVTAK 99
Cdd:cd18110   90 DLPEQAFYMVGTIDEAVEK 108
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-103 1.00e-61

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 194.55  E-value: 1.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123    1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:TIGR01039 359 ARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYD 438

                          90       100
                  ....*....|....*....|...
gi 156530123   81 GLPEQAFYLVGNIDEVTAKATNL 103
Cdd:TIGR01039 439 HLPEQAFYMVGTIEEVVEKAKKL 461
 
Name Accession Description Interval E-value
atpB CHL00060
ATP synthase CF1 beta subunit
 1-111 3.55e-85

ATP synthase CF1 beta subunit


Pssm-ID: 214349 [Multi-domain]  Cd Length: 494  Bit Score: 255.74  E-value: 3.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:CHL00060 384 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELD 463

                         90       100       110
                 ....*....|....*....|....*....|.
gi 156530123  81 GLPEQAFYLVGNIDEVTAKATNLEMESNLKK 111
Cdd:CHL00060 464 GLPEQAFYLVGNIDEATAKAANLEVESKLKK 494
AtpD COG0055
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ...
 1-107 5.52e-72

FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 439825 [Multi-domain]  Cd Length: 468  Bit Score: 221.12  E-value: 5.52e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:COG0055  362 AREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYD 441

                         90       100
                 ....*....|....*....|....*..
gi 156530123  81 GLPEQAFYLVGNIDEVTAKATNLEMES 107
Cdd:COG0055  442 DLPEQAFYMVGTIDEAVEKAKKLKAEA 468
ATP-synt_F1_beta_C cd18110
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ...
 1-99 2.32e-70

F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.


Pssm-ID: 349745 [Multi-domain]  Cd Length: 108  Bit Score: 205.40  E-value: 2.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:cd18110   10 ARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGFKEILDGEYD 89

                         90
                 ....*....|....*....
gi 156530123  81 GLPEQAFYLVGNIDEVTAK 99
Cdd:cd18110   90 DLPEQAFYMVGTIDEAVEK 108
atpD TIGR01039
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ...
 1-103 1.00e-61

ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]


Pssm-ID: 211621 [Multi-domain]  Cd Length: 461  Bit Score: 194.55  E-value: 1.00e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123    1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFKLILSGELD 80
Cdd:TIGR01039 359 ARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRIQRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYD 438

                          90       100
                  ....*....|....*....|...
gi 156530123   81 GLPEQAFYLVGNIDEVTAKATNL 103
Cdd:TIGR01039 439 HLPEQAFYMVGTIEEVVEKAKKL 461
ATP-synt_F1_V1_A1_AB_FliI_C cd01429
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ...
 1-60 5.78e-16

ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, 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 Fo, Vo, or Ao 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 synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are 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. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.


Pssm-ID: 349744 [Multi-domain]  Cd Length: 70  Bit Score: 66.31  E-value: 5.78e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156530123   1 AQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGK 60
Cdd:cd01429    5 ARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEK 64
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
 2-46 5.35e-05

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 40.54  E-value: 5.35e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 156530123   2 QRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 46
Cdd:PRK04192 458 DEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVARLIrEDFLQQ 503
ATP-synt_V_A-type_alpha_C cd18111
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ...
 2-46 1.43e-04

V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. 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-ATPase) is found in archaea and functions 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, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.


Pssm-ID: 349746 [Multi-domain]  Cd Length: 105  Bit Score: 37.75  E-value: 1.43e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 156530123   2 QRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKI-ERFLSQ 46
Cdd:cd18111    6 TEAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQ 51
ATP-synt_V_A-type_beta_C cd18112
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 ...
 12-46 3.27e-04

V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. 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-ATPase) is found in archaea and functions 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, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.


Pssm-ID: 349747 [Multi-domain]  Cd Length: 95  Bit Score: 36.64  E-value: 3.27e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 156530123  12 KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 46
Cdd:cd18112   22 KDVRALAAIVGEEALSEEDRLYLEFADRFErEFINQ 57
 
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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