anion permease translocates charged substrates such as sodium, arsenate, antimonite, sulfate and organic anions across biological membranes; similar to Eschericha coli L-tartrate/succinate antiporter
Sodium:sulfate symporter transmembrane region; There are also some members in this family that ...
4-487
0e+00
Sodium:sulfate symporter transmembrane region; There are also some members in this family that do not match the Prosite motif, and belong to the subfamily SODIT1.
:
Pssm-ID: 279307 [Multi-domain] Cd Length: 472 Bit Score: 533.10 E-value: 0e+00
Sodium:sulfate symporter transmembrane region; There are also some members in this family that ...
4-487
0e+00
Sodium:sulfate symporter transmembrane region; There are also some members in this family that do not match the Prosite motif, and belong to the subfamily SODIT1.
Pssm-ID: 279307 [Multi-domain] Cd Length: 472 Bit Score: 533.10 E-value: 0e+00
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally ...
24-481
3.53e-159
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally characterized proteins of the DASS family transport (1) organic di- and tricarboxylates of the Krebs Cycle as well as dicarboxylate amino acid, (2) inorganic sulfate and (3) phosphate. The animal NaDC-1 cotransport 3 Na+ with each dicarboxylate. Protonated tricarboxylates are also cotransported with 3Na+. [Transport and binding proteins, Anions, Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273267 [Multi-domain] Cd Length: 444 Bit Score: 458.73 E-value: 3.53e-159
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
44-482
8.37e-18
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: 84.99 E-value: 8.37e-18
Sodium:sulfate symporter transmembrane region; There are also some members in this family that ...
4-487
0e+00
Sodium:sulfate symporter transmembrane region; There are also some members in this family that do not match the Prosite motif, and belong to the subfamily SODIT1.
Pssm-ID: 279307 [Multi-domain] Cd Length: 472 Bit Score: 533.10 E-value: 0e+00
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally ...
24-481
3.53e-159
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally characterized proteins of the DASS family transport (1) organic di- and tricarboxylates of the Krebs Cycle as well as dicarboxylate amino acid, (2) inorganic sulfate and (3) phosphate. The animal NaDC-1 cotransport 3 Na+ with each dicarboxylate. Protonated tricarboxylates are also cotransported with 3Na+. [Transport and binding proteins, Anions, Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273267 [Multi-domain] Cd Length: 444 Bit Score: 458.73 E-value: 3.53e-159
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
44-482
8.37e-18
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: 84.99 E-value: 8.37e-18
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
94-482
1.94e-17
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been shown to translocate Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate across plasma membranes rabbit, human, and rat kidney. It is related to renal and intestinal Na+/sulfate cotransporters and a few putative bacterial permeases. The SLC13-type proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium and various anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease is composed of 8-13 transmembrane helices.
Pssm-ID: 238535 [Multi-domain] Cd Length: 382 Bit Score: 83.79 E-value: 1.94e-17
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
297-483
1.10e-04
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: 44.55 E-value: 1.10e-04
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
290-482
1.52e-03
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been shown to translocate Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate across plasma membranes rabbit, human, and rat kidney. It is related to renal and intestinal Na+/sulfate cotransporters and a few putative bacterial permeases. The SLC13-type proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium and various anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease is composed of 8-13 transmembrane helices.
Pssm-ID: 238535 [Multi-domain] Cd Length: 382 Bit Score: 40.65 E-value: 1.52e-03
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
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
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
Others (non-specific hits) and
superfamily placeholders are drawn in pastel colors.
if a domain or superfamily has been annotated with functional sites (conserved features),
they are mapped to the query sequence and indicated through sets of triangles
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
