V-type proton ATPase subunit H is subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase); it activates the ATPase activity of V-ATPase and couples ATPase activity to proton flow
VATPase_H, regulatory vacuolar ATP synthase subunit H (Vma13p); activation component of the ...
2-304
1.31e-164
VATPase_H, regulatory vacuolar ATP synthase subunit H (Vma13p); activation component of the peripheral V1 complex of V-ATPase, a heteromultimeric enzyme which uses ATP to actively transport protons into organelles and extracellular compartments. The topology is that of a superhelical spiral, in part the geometry is similar to superhelices composed of armadillo repeat motifs, as found in importins for example.
The actual alignment was detected with superfamily member cd00256:
Pssm-ID: 473943 [Multi-domain] Cd Length: 429 Bit Score: 465.34 E-value: 1.31e-164
VATPase_H, regulatory vacuolar ATP synthase subunit H (Vma13p); activation component of the ...
2-304
1.31e-164
VATPase_H, regulatory vacuolar ATP synthase subunit H (Vma13p); activation component of the peripheral V1 complex of V-ATPase, a heteromultimeric enzyme which uses ATP to actively transport protons into organelles and extracellular compartments. The topology is that of a superhelical spiral, in part the geometry is similar to superhelices composed of armadillo repeat motifs, as found in importins for example.
Pssm-ID: 238159 [Multi-domain] Cd Length: 429 Bit Score: 465.34 E-value: 1.31e-164
V-ATPase subunit H; The yeast Saccharomyces cerevisiae vacuolar H+-ATPase (V-ATPase) is a ...
188-303
6.56e-68
V-ATPase subunit H; The yeast Saccharomyces cerevisiae vacuolar H+-ATPase (V-ATPase) is a multisubunit complex responsible for acidifying organelles. It functions as an ATP dependent proton pump that transports protons across a lipid bilayer. This domain corresponds to the C terminal domain of the H subunit of V-ATPase. The N-terminal domain is required for the activation of the complex whereas the C-terminal domain is required for coupling ATP hydrolysis to proton translocation.
Pssm-ID: 432010 [Multi-domain] Cd Length: 117 Bit Score: 207.74 E-value: 6.56e-68
VATPase_H, regulatory vacuolar ATP synthase subunit H (Vma13p); activation component of the ...
2-304
1.31e-164
VATPase_H, regulatory vacuolar ATP synthase subunit H (Vma13p); activation component of the peripheral V1 complex of V-ATPase, a heteromultimeric enzyme which uses ATP to actively transport protons into organelles and extracellular compartments. The topology is that of a superhelical spiral, in part the geometry is similar to superhelices composed of armadillo repeat motifs, as found in importins for example.
Pssm-ID: 238159 [Multi-domain] Cd Length: 429 Bit Score: 465.34 E-value: 1.31e-164
V-ATPase subunit H; The yeast Saccharomyces cerevisiae vacuolar H+-ATPase (V-ATPase) is a ...
188-303
6.56e-68
V-ATPase subunit H; The yeast Saccharomyces cerevisiae vacuolar H+-ATPase (V-ATPase) is a multisubunit complex responsible for acidifying organelles. It functions as an ATP dependent proton pump that transports protons across a lipid bilayer. This domain corresponds to the C terminal domain of the H subunit of V-ATPase. The N-terminal domain is required for the activation of the complex whereas the C-terminal domain is required for coupling ATP hydrolysis to proton translocation.
Pssm-ID: 432010 [Multi-domain] Cd Length: 117 Bit Score: 207.74 E-value: 6.56e-68
V-ATPase subunit H; The yeast Saccharomyces cerevisiae vacuolar H+-ATPase (V-ATPase) is a ...
1-181
5.87e-51
V-ATPase subunit H; The yeast Saccharomyces cerevisiae vacuolar H+-ATPase (V-ATPase) is a multisubunit complex responsible for acidifying organelles. It functions as an ATP dependent proton pump that transports protons across a lipid bilayer. This domain corresponds to the N terminal domain of the H subunit of V-ATPase. The N-terminal domain is required for the activation of the complex whereas the C-terminal domain is required for coupling ATP hydrolysis to proton translocation.
Pssm-ID: 460852 Cd Length: 314 Bit Score: 170.93 E-value: 5.87e-51
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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