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ATP synthase beta subunit, partial (chloroplast) [Senna occidentalis]
List of domain hits
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Name | Accession | Description | Interval | E-value | |||||
atpB super family | cl33325 | ATP synthase CF1 beta subunit |
2-250 | 0e+00 | |||||
ATP synthase CF1 beta subunit The actual alignment was detected with superfamily member CHL00060: Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 532.69 E-value: 0e+00
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Name | Accession | Description | Interval | E-value | |||||
atpB | CHL00060 | ATP synthase CF1 beta subunit |
2-250 | 0e+00 | |||||
ATP synthase CF1 beta subunit Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 532.69 E-value: 0e+00
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AtpD | COG0055 | FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
12-250 | 4.65e-143 | |||||
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: 408.71 E-value: 4.65e-143
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atpD | TIGR01039 | ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
15-250 | 2.59e-125 | |||||
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: 363.27 E-value: 2.59e-125
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F1-ATPase_beta_CD | cd01133 | F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-250 | 9.82e-98 | |||||
F1 ATP synthase beta subunit, central domain; The F-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 mitochondrial 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. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain. Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 286.81 E-value: 9.82e-98
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ATP-synt_ab | pfam00006 | ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
148-250 | 1.68e-21 | |||||
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho. Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 88.95 E-value: 1.68e-21
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Name | Accession | Description | Interval | E-value | |||||
atpB | CHL00060 | ATP synthase CF1 beta subunit |
2-250 | 0e+00 | |||||
ATP synthase CF1 beta subunit Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 532.69 E-value: 0e+00
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AtpD | COG0055 | FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
12-250 | 4.65e-143 | |||||
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: 408.71 E-value: 4.65e-143
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atpD | TIGR01039 | ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
15-250 | 2.59e-125 | |||||
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: 363.27 E-value: 2.59e-125
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F1-ATPase_beta_CD | cd01133 | F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
95-250 | 9.82e-98 | |||||
F1 ATP synthase beta subunit, central domain; The F-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 mitochondrial 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. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain. Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 286.81 E-value: 9.82e-98
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alt_F1F0_F1_bet | TIGR03305 | alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
17-250 | 1.12e-75 | |||||
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase. Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 236.26 E-value: 1.12e-75
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RecA-like_ion-translocating_ATPases | cd19476 | RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
95-250 | 3.27e-62 | |||||
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion. Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 196.14 E-value: 3.27e-62
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ATP-synt_F1_beta_N | cd18115 | F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
15-94 | 1.20e-39 | |||||
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-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: 349739 [Multi-domain] Cd Length: 76 Bit Score: 131.87 E-value: 1.20e-39
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FliI | COG1157 | Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
17-177 | 3.79e-25 | |||||
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 102.42 E-value: 3.79e-25
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ATP-synt_ab | pfam00006 | ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
148-250 | 1.68e-21 | |||||
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho. Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 88.95 E-value: 1.68e-21
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PRK13343 | PRK13343 | F0F1 ATP synthase subunit alpha; Provisional |
65-184 | 3.37e-20 | |||||
F0F1 ATP synthase subunit alpha; Provisional Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 88.82 E-value: 3.37e-20
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atpA | TIGR00962 | proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
65-184 | 1.08e-19 | |||||
proton translocating ATP synthase, F1 alpha 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. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion] Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 87.44 E-value: 1.08e-19
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ATP-synt_ab_N | pfam02874 | ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
19-91 | 1.82e-19 | |||||
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella. Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 79.51 E-value: 1.82e-19
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ATPase_flagellum-secretory_path_III | cd01136 | Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
95-249 | 1.25e-18 | |||||
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway. Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 82.22 E-value: 1.25e-18
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AtpA | COG0056 | FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
65-161 | 4.33e-18 | |||||
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 82.78 E-value: 4.33e-18
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PRK09281 | PRK09281 | F0F1 ATP synthase subunit alpha; Validated |
70-161 | 5.48e-18 | |||||
F0F1 ATP synthase subunit alpha; Validated Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 82.42 E-value: 5.48e-18
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PRK09099 | PRK09099 | type III secretion system ATPase; Provisional |
79-178 | 1.96e-17 | |||||
type III secretion system ATPase; Provisional Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 80.97 E-value: 1.96e-17
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fliI | PRK08472 | flagellar protein export ATPase FliI; |
94-188 | 8.84e-15 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 73.18 E-value: 8.84e-15
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fliI | PRK08927 | flagellar protein export ATPase FliI; |
17-186 | 1.00e-14 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 72.70 E-value: 1.00e-14
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PRK06936 | PRK06936 | EscN/YscN/HrcN family type III secretion system ATPase; |
16-184 | 2.38e-13 | |||||
EscN/YscN/HrcN family type III secretion system ATPase; Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 69.01 E-value: 2.38e-13
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PRK08149 | PRK08149 | FliI/YscN family ATPase; |
63-232 | 7.39e-13 | |||||
FliI/YscN family ATPase; Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 67.33 E-value: 7.39e-13
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F1-ATPase_alpha_CD | cd01132 | F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-184 | 1.28e-12 | |||||
F1 ATP synthase alpha subunit, central domain; The F-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 mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain. Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 65.66 E-value: 1.28e-12
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PRK06820 | PRK06820 | EscN/YscN/HrcN family type III secretion system ATPase; |
6-249 | 3.43e-12 | |||||
EscN/YscN/HrcN family type III secretion system ATPase; Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 65.61 E-value: 3.43e-12
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atpA | CHL00059 | ATP synthase CF1 alpha subunit |
65-184 | 4.24e-11 | |||||
ATP synthase CF1 alpha subunit Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 62.29 E-value: 4.24e-11
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PRK05922 | PRK05922 | type III secretion system ATPase; Validated |
73-223 | 5.94e-11 | |||||
type III secretion system ATPase; Validated Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 61.84 E-value: 5.94e-11
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fliI | PRK06002 | flagellar protein export ATPase FliI; |
104-178 | 7.43e-11 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 61.55 E-value: 7.43e-11
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fliI | PRK08972 | flagellar protein export ATPase FliI; |
80-178 | 1.26e-10 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 60.87 E-value: 1.26e-10
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fliI | PRK05688 | flagellar protein export ATPase FliI; |
77-178 | 7.39e-10 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 58.59 E-value: 7.39e-10
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fliI | PRK07721 | flagellar protein export ATPase FliI; |
90-178 | 1.81e-09 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 57.42 E-value: 1.81e-09
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fliI | PRK06793 | flagellar protein export ATPase FliI; |
51-217 | 3.31e-09 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 56.52 E-value: 3.31e-09
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PRK04196 | PRK04196 | V-type ATP synthase subunit B; Provisional |
19-171 | 4.40e-09 | |||||
V-type ATP synthase subunit B; Provisional Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 55.99 E-value: 4.40e-09
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fliI | PRK07960 | flagellum-specific ATP synthase FliI; |
96-178 | 6.35e-09 | |||||
flagellum-specific ATP synthase FliI; Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 55.56 E-value: 6.35e-09
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V_A-ATPase_B | cd01135 | V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
93-171 | 1.32e-08 | |||||
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit. Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 54.15 E-value: 1.32e-08
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PRK07594 | PRK07594 | EscN/YscN/HrcN family type III secretion system ATPase; |
76-183 | 1.77e-07 | |||||
EscN/YscN/HrcN family type III secretion system ATPase; Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 51.49 E-value: 1.77e-07
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fliI | PRK07196 | flagellar protein export ATPase FliI; |
80-178 | 2.65e-07 | |||||
flagellar protein export ATPase FliI; Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 50.66 E-value: 2.65e-07
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V-ATPase_V1_B | TIGR01040 | V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
90-172 | 4.86e-06 | |||||
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 47.02 E-value: 4.86e-06
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PRK02118 | PRK02118 | V-type ATP synthase subunit B; Provisional |
78-171 | 7.36e-06 | |||||
V-type ATP synthase subunit B; Provisional Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 46.57 E-value: 7.36e-06
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PTZ00185 | PTZ00185 | ATPase alpha subunit; Provisional |
17-184 | 9.00e-05 | |||||
ATPase alpha subunit; Provisional Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 43.11 E-value: 9.00e-05
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ATP-synt_F1_V1_A1_AB_FliI_N | cd01426 | ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
16-92 | 1.40e-03 | |||||
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the 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, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which 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: 349738 [Multi-domain] Cd Length: 73 Bit Score: 36.52 E-value: 1.40e-03
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PRK04192 | PRK04192 | V-type ATP synthase subunit A; Provisional |
15-117 | 7.11e-03 | |||||
V-type ATP synthase subunit A; Provisional Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 37.45 E-value: 7.11e-03
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Blast search parameters | ||||
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