P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the ...
255-692
0e+00
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the C-terminal of Sey1 from yeast and RHD3 from Arabidopsis, GTP-binding proteins involved in homotypic membrane fusion of the endoplasmic reticulum. This is a stalk-like domain composed of four 3HBs that interacts with its own GTPase domain and that of a neighbouring molecule, to undergo major conformational changes during the GTP cycle to drive membrane fusion.
:
Pssm-ID: 466577 Cd Length: 419 Bit Score: 553.21 E-value: 0e+00
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
4-214
1.35e-118
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.
The actual alignment was detected with superfamily member pfam05879:
Pssm-ID: 461768 Cd Length: 243 Bit Score: 355.99 E-value: 1.35e-118
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the ...
255-692
0e+00
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the C-terminal of Sey1 from yeast and RHD3 from Arabidopsis, GTP-binding proteins involved in homotypic membrane fusion of the endoplasmic reticulum. This is a stalk-like domain composed of four 3HBs that interacts with its own GTPase domain and that of a neighbouring molecule, to undergo major conformational changes during the GTP cycle to drive membrane fusion.
Pssm-ID: 466577 Cd Length: 419 Bit Score: 553.21 E-value: 0e+00
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
4-214
1.35e-118
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.
Pssm-ID: 461768 Cd Length: 243 Bit Score: 355.99 E-value: 1.35e-118
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
8-175
7.34e-38
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 140.54 E-value: 7.34e-38
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the ...
255-692
0e+00
Sey1 three-helix bundle domain; This is the three-helix bundle (3HB) domain found at the C-terminal of Sey1 from yeast and RHD3 from Arabidopsis, GTP-binding proteins involved in homotypic membrane fusion of the endoplasmic reticulum. This is a stalk-like domain composed of four 3HBs that interacts with its own GTPase domain and that of a neighbouring molecule, to undergo major conformational changes during the GTP cycle to drive membrane fusion.
Pssm-ID: 466577 Cd Length: 419 Bit Score: 553.21 E-value: 0e+00
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
4-214
1.35e-118
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.
Pssm-ID: 461768 Cd Length: 243 Bit Score: 355.99 E-value: 1.35e-118
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
8-175
7.34e-38
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 140.54 E-value: 7.34e-38
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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