sodium/hydrogen exchanger is a solute carrier family 9 member involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A. ...
52-650
0e+00
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36)The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals.Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in(1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles.This model is specific for the eukaryotic members members of this family. [Transport and binding proteins, Cations and iron carrying compounds]
:
Pssm-ID: 273294 [Multi-domain] Cd Length: 559 Bit Score: 781.66 E-value: 0e+00
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A. ...
52-650
0e+00
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36)The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals.Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in(1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles.This model is specific for the eukaryotic members members of this family. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273294 [Multi-domain] Cd Length: 559 Bit Score: 781.66 E-value: 0e+00
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
108-465
8.92e-81
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.
Pssm-ID: 425982 [Multi-domain] Cd Length: 377 Bit Score: 264.50 E-value: 8.92e-81
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A. ...
52-650
0e+00
sodium/hydrogen exchanger 3; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36)The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals.Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in(1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles.This model is specific for the eukaryotic members members of this family. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273294 [Multi-domain] Cd Length: 559 Bit Score: 781.66 E-value: 0e+00
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
108-465
8.92e-81
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.
Pssm-ID: 425982 [Multi-domain] Cd Length: 377 Bit Score: 264.50 E-value: 8.92e-81
Na+/H+ antiporter, bacterial form; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC ...
113-482
7.83e-30
Na+/H+ antiporter, bacterial form; The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36) The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals. Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in (1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles. This model is specific for the bacterial members of this family. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 129911 [Multi-domain] Cd Length: 525 Bit Score: 125.00 E-value: 7.83e-30
NhaP-type Na+/H+ and K+/H+ antiporter with C-terminal TrkAC and CorC domains [Energy ...
138-477
1.31e-13
NhaP-type Na+/H+ and K+/H+ antiporter with C-terminal TrkAC and CorC domains [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 442494 [Multi-domain] Cd Length: 502 Bit Score: 74.38 E-value: 1.31e-13
Regulatory region of Na+/H+ exchanger NHE binds to calmodulin; NEXCaM_BD is a coiled-coil ...
608-680
4.87e-04
Regulatory region of Na+/H+ exchanger NHE binds to calmodulin; NEXCaM_BD is a coiled-coil domain found as part of the regulatory, C-terminal region of the 12-14 TM sodium/proton exchangers (NHEs)2 of the solute carrier 9 (SLC9) family in all animal kingdoms. The C- lobe of CaM binds the first alpha-helix of the NHE, or NEXCaM_BD region, and the N-lobe of CaM binds the second helix of NEXCaM_BD.
Pssm-ID: 465214 Cd Length: 109 Bit Score: 40.46 E-value: 4.87e-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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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