Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in ...
1-427
5.05e-98
Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in eubacteria and archaea. A typical ArsB permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump (ArsAB). The ArsAB complex is similar in many ways to ATP-binding cassette transporters, which have two groups of six transmembrane-spanning helical segments and two nucleotide-binding domains. The ArsB proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life.
:
Pssm-ID: 238538 [Multi-domain] Cd Length: 416 Bit Score: 299.57 E-value: 5.05e-98
Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in ...
1-427
5.05e-98
Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in eubacteria and archaea. A typical ArsB permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump (ArsAB). The ArsAB complex is similar in many ways to ATP-binding cassette transporters, which have two groups of six transmembrane-spanning helical segments and two nucleotide-binding domains. The ArsB proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life.
Pssm-ID: 238538 [Multi-domain] Cd Length: 416 Bit Score: 299.57 E-value: 5.05e-98
arsenite/antimonite efflux pump membrane protein; Members of this protein family are ArsB, a ...
1-431
2.55e-62
arsenite/antimonite efflux pump membrane protein; Members of this protein family are ArsB, a highly hydrophobic integral membrane protein involved in transport processes used to protect cells from arsenite (or antimonite). Members of the seed alignment were selected by adjacency to the ATPase subunit ArsA that energizes the transport. [Cellular processes, Detoxification, Transport and binding proteins, Other]
Pssm-ID: 213571 Cd Length: 426 Bit Score: 207.70 E-value: 2.55e-62
Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in ...
1-427
5.05e-98
Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in eubacteria and archaea. A typical ArsB permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump (ArsAB). The ArsAB complex is similar in many ways to ATP-binding cassette transporters, which have two groups of six transmembrane-spanning helical segments and two nucleotide-binding domains. The ArsB proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life.
Pssm-ID: 238538 [Multi-domain] Cd Length: 416 Bit Score: 299.57 E-value: 5.05e-98
arsenite/antimonite efflux pump membrane protein; Members of this protein family are ArsB, a ...
1-431
2.55e-62
arsenite/antimonite efflux pump membrane protein; Members of this protein family are ArsB, a highly hydrophobic integral membrane protein involved in transport processes used to protect cells from arsenite (or antimonite). Members of the seed alignment were selected by adjacency to the ATPase subunit ArsA that energizes the transport. [Cellular processes, Detoxification, Transport and binding proteins, Other]
Pssm-ID: 213571 Cd Length: 426 Bit Score: 207.70 E-value: 2.55e-62
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
3-424
1.88e-42
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, antimonite, sulfate and organic anions across biological membranes in all three kingdoms of life. A typical anion permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump.
Pssm-ID: 238344 [Multi-domain] Cd Length: 396 Bit Score: 153.94 E-value: 1.88e-42
Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible ...
12-414
6.55e-16
Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible for classic phenotype of oculocutaneous albinism type 2 (OCA2). Although the precise function of the P protein is unknown, it was predicted to regulate the intraorganelle pH, together with the ATP-driven proton pump. It shows significant sequence similarity to the Na+/H+ antiporter NhaD from Vibrio parahaemolyticus. Both proteins belong to ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease contains 8-13 transmembrane domains.
Pssm-ID: 238536 [Multi-domain] Cd Length: 413 Bit Score: 79.22 E-value: 6.55e-16
Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to ...
1-429
4.86e-12
Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to function as anion translocating permeases in eubacteria, archaea and plants. They belong to ArsB/NhaD superfamily of permeases that have been shown to translocate sodium, sulfate, arsenite and organic anions. A typical ArsB/NhaD permease is composed of 8-13 transmembrane domains.
Pssm-ID: 238537 [Multi-domain] Cd Length: 384 Bit Score: 66.92 E-value: 4.86e-12
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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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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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.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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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,
or click on the triangles, if present, that represent functional sites (conserved features)
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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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(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
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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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