MULTISPECIES: hypothetical protein [Halobacteriales]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| S_2TMBeta super family | cl40286 | SMODS-associating 2TM, beta-strand rich effector domain; Predicted sensor/effector coupled ... |
18-221 | 1.97e-35 | ||||
SMODS-associating 2TM, beta-strand rich effector domain; Predicted sensor/effector coupled domain which occurs in conserved genome contexts with the SMODS nucleotide synthetase. In addition to the predicted pore-forming 2TM region, the domain contains seven predicted beta-strands, suggestive of a lipocalin-like beta-barrel structure which could act as the sensor which activates the pore-forming effector response. The actual alignment was detected with superfamily member pfam18153: Pssm-ID: 407984 Cd Length: 180 Bit Score: 123.61 E-value: 1.97e-35
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| Name | Accession | Description | Interval | E-value | ||||
| S_2TMBeta | pfam18153 | SMODS-associating 2TM, beta-strand rich effector domain; Predicted sensor/effector coupled ... |
18-221 | 1.97e-35 | ||||
SMODS-associating 2TM, beta-strand rich effector domain; Predicted sensor/effector coupled domain which occurs in conserved genome contexts with the SMODS nucleotide synthetase. In addition to the predicted pore-forming 2TM region, the domain contains seven predicted beta-strands, suggestive of a lipocalin-like beta-barrel structure which could act as the sensor which activates the pore-forming effector response. Pssm-ID: 407984 Cd Length: 180 Bit Score: 123.61 E-value: 1.97e-35
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| Voltage_gated_ClC | cd00400 | CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ... |
3-94 | 6.06e-03 | ||||
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function. Pssm-ID: 238233 [Multi-domain] Cd Length: 383 Bit Score: 37.16 E-value: 6.06e-03
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| Name | Accession | Description | Interval | E-value | ||||
| S_2TMBeta | pfam18153 | SMODS-associating 2TM, beta-strand rich effector domain; Predicted sensor/effector coupled ... |
18-221 | 1.97e-35 | ||||
SMODS-associating 2TM, beta-strand rich effector domain; Predicted sensor/effector coupled domain which occurs in conserved genome contexts with the SMODS nucleotide synthetase. In addition to the predicted pore-forming 2TM region, the domain contains seven predicted beta-strands, suggestive of a lipocalin-like beta-barrel structure which could act as the sensor which activates the pore-forming effector response. Pssm-ID: 407984 Cd Length: 180 Bit Score: 123.61 E-value: 1.97e-35
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| Voltage_gated_ClC | cd00400 | CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ... |
3-94 | 6.06e-03 | ||||
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function. Pssm-ID: 238233 [Multi-domain] Cd Length: 383 Bit Score: 37.16 E-value: 6.06e-03
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| Blast search parameters | ||||
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