V-type proton ATPase subunit B1-like protein, partial [Crocus mathewii]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| V-ATPase_V1_B super family | cl36802 | V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
1-29 | 2.12e-12 | ||
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] The actual alignment was detected with superfamily member TIGR01040: Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 57.81 E-value: 2.12e-12
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| Name | Accession | Description | Interval | E-value | ||
| V-ATPase_V1_B | TIGR01040 | V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
1-29 | 2.12e-12 | ||
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: 57.81 E-value: 2.12e-12
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| 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 ... |
1-23 | 5.61e-07 | ||
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: 40.88 E-value: 5.61e-07
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| Name | Accession | Description | Interval | E-value | ||
| V-ATPase_V1_B | TIGR01040 | V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
1-29 | 2.12e-12 | ||
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: 57.81 E-value: 2.12e-12
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| 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 ... |
1-23 | 5.61e-07 | ||
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: 40.88 E-value: 5.61e-07
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