sodium-potassium/proton antiporter ChaA functions mainly at alkaline pH; can also function as a potassium/proton and calcium/proton antiporter at alkaline pH; does not play a major role in calcium export
calcium/proton exchanger; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the ...
7-365
3.37e-117
calcium/proton exchanger; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the CaCA family are found ubiquitously, having been identified in animals, plants, yeast, archaea and widely divergent bacteria.All of the characterized animal proteins catalyze Ca2+:Na+ exchange although some also transport K+. The NCX1 plasma membrane protein exchanges 3 Na+ for 1 Ca2+. The E. coli ChaA protein catalyzes Ca2+:H+ antiport but may also catalyze Na+:H+ antiport. All remaining well-characterized members of the family catalyze Ca2+:H+ exchange.This model is generated from the calcium ion/proton exchangers of the CacA family. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273297 [Multi-domain] Cd Length: 363 Bit Score: 344.05 E-value: 3.37e-117
Sodium/calcium exchanger protein; This is a family of sodium/calcium exchanger integral ...
40-191
1.36e-07
Sodium/calcium exchanger protein; This is a family of sodium/calcium exchanger integral membrane proteins. This family covers the integral membrane regions of the proteins. Sodium/calcium exchangers regulate intracellular Ca2+ concentrations in many cells; cardiac myocytes, epithelial cells, neurons retinal rod photoreceptors and smooth muscle cells. Ca2+ is moved into or out of the cytosol depending on Na+ concentration. In humans and rats there are 3 isoforms; NCX1 NCX2 and NCX3.
Pssm-ID: 426387 [Multi-domain] Cd Length: 149 Bit Score: 50.29 E-value: 1.36e-07
calcium/proton exchanger; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the ...
7-365
3.37e-117
calcium/proton exchanger; The Ca2+:Cation Antiporter (CaCA) Family (TC 2.A.19)Proteins of the CaCA family are found ubiquitously, having been identified in animals, plants, yeast, archaea and widely divergent bacteria.All of the characterized animal proteins catalyze Ca2+:Na+ exchange although some also transport K+. The NCX1 plasma membrane protein exchanges 3 Na+ for 1 Ca2+. The E. coli ChaA protein catalyzes Ca2+:H+ antiport but may also catalyze Na+:H+ antiport. All remaining well-characterized members of the family catalyze Ca2+:H+ exchange.This model is generated from the calcium ion/proton exchangers of the CacA family. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273297 [Multi-domain] Cd Length: 363 Bit Score: 344.05 E-value: 3.37e-117
Sodium/calcium exchanger protein; This is a family of sodium/calcium exchanger integral ...
40-191
1.36e-07
Sodium/calcium exchanger protein; This is a family of sodium/calcium exchanger integral membrane proteins. This family covers the integral membrane regions of the proteins. Sodium/calcium exchangers regulate intracellular Ca2+ concentrations in many cells; cardiac myocytes, epithelial cells, neurons retinal rod photoreceptors and smooth muscle cells. Ca2+ is moved into or out of the cytosol depending on Na+ concentration. In humans and rats there are 3 isoforms; NCX1 NCX2 and NCX3.
Pssm-ID: 426387 [Multi-domain] Cd Length: 149 Bit Score: 50.29 E-value: 1.36e-07
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.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
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
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
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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