polyphosphate (polyP) polymerase domain-containing protein similar to yeast vacuolar transport chaperone (VTC) proteins VTC-2, -3 and- 4, which are components of the integral membrane VTC complex; the polyP polymerase domain generates polyP from ATP by a phosphotransfer reaction releasing ADP
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion ...
1-234
4.96e-50
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion transport and metabolism, Intracellular trafficking, secretion, and vesicular transport];
The actual alignment was detected with superfamily member COG5036:
Pssm-ID: 444047 Cd Length: 241 Bit Score: 163.62 E-value: 4.96e-50
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion ...
1-234
4.96e-50
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion transport and metabolism, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444047 Cd Length: 241 Bit Score: 163.62 E-value: 4.96e-50
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
8-225
4.76e-45
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins VTC-2, -3 and- 4, and similar proteins; Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2, -3, and -4 contain polyP polymerase domains. For S. cerevisiae VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.
Pssm-ID: 143622 Cd Length: 214 Bit Score: 150.16 E-value: 4.76e-45
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
7-225
1.30e-34
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins VTC2, VTC3 and VTC4. This domain is also found in a variety of bacterial proteins.
Pssm-ID: 401343 Cd Length: 235 Bit Score: 123.60 E-value: 1.30e-34
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion ...
1-234
4.96e-50
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion transport and metabolism, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 444047 Cd Length: 241 Bit Score: 163.62 E-value: 4.96e-50
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
8-225
4.76e-45
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins VTC-2, -3 and- 4, and similar proteins; Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2, -3, and -4 contain polyP polymerase domains. For S. cerevisiae VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.
Pssm-ID: 143622 Cd Length: 214 Bit Score: 150.16 E-value: 4.76e-45
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
7-225
1.30e-34
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins VTC2, VTC3 and VTC4. This domain is also found in a variety of bacterial proteins.
Pssm-ID: 401343 Cd Length: 235 Bit Score: 123.60 E-value: 1.30e-34
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein ...
41-225
1.91e-09
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein VTC4, and similar proteins; Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2,-3, and -4 contain polyP polymerase domains. S. cerevisiae VTC4 belongs to this subgroup. For VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.
Pssm-ID: 143623 Cd Length: 290 Bit Score: 56.60 E-value: 1.91e-09
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
37-171
3.55e-04
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins VTC-2, and -3 , and similar proteins; Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2, -3, and -4 contain polyP polymerase domains. S. cerevisiae VTC-2,and -3 belong to this subgroup. For VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.
Pssm-ID: 143630 Cd Length: 303 Bit Score: 40.81 E-value: 3.55e-04
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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