SLC13 (solute carrier 13) family permease is a sodium-coupled symporter that facilitates the transport across biological membranes of various ions including sulfate or Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate; may function as a regulator
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
442-870
1.26e-116
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.
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Pssm-ID: 238535 [Multi-domain] Cd Length: 382 Bit Score: 360.36 E-value: 1.26e-116
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
442-870
1.26e-116
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: 360.36 E-value: 1.26e-116
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
2-276
1.15e-41
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The SPX domain of the Saccharomyces cerevisiae membrane-localized low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. Pho91 is involved in the export of inorganic phosphate from the vacuole to the cytosol. While both, Pho87 and Pho90, transport phosphate into the cell, only Pho87 appears to also function as a sensor for high extracellular phosphate concentrations.
Pssm-ID: 269899 [Multi-domain] Cd Length: 148 Bit Score: 149.22 E-value: 1.15e-41
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-289
4.55e-41
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 residue long domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all the members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors PHO81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2 NUC-2 contains several ankyrin repeats pfam00023. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with murine xenotropic and polytropic leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signalling and result in cell toxicity and death. The similarity between SYG1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organizms. In addition, given the similarities between XPR1 and SYG1 and phosphate regulatory proteins, it has been proposed that XPR1 might be involved in G-protein associated signal transduction and may itself function as a phosphate sensor.
Pssm-ID: 460807 [Multi-domain] Cd Length: 339 Bit Score: 154.26 E-value: 4.55e-41
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally ...
439-820
4.55e-36
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: 142.10 E-value: 4.55e-36
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
442-870
1.26e-116
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: 360.36 E-value: 1.26e-116
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
451-865
4.80e-63
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: 217.89 E-value: 4.80e-63
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
2-276
1.15e-41
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The SPX domain of the Saccharomyces cerevisiae membrane-localized low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. Pho91 is involved in the export of inorganic phosphate from the vacuole to the cytosol. While both, Pho87 and Pho90, transport phosphate into the cell, only Pho87 appears to also function as a sensor for high extracellular phosphate concentrations.
Pssm-ID: 269899 [Multi-domain] Cd Length: 148 Bit Score: 149.22 E-value: 1.15e-41
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-289
4.55e-41
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 residue long domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all the members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors PHO81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2 NUC-2 contains several ankyrin repeats pfam00023. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with murine xenotropic and polytropic leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signalling and result in cell toxicity and death. The similarity between SYG1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organizms. In addition, given the similarities between XPR1 and SYG1 and phosphate regulatory proteins, it has been proposed that XPR1 might be involved in G-protein associated signal transduction and may itself function as a phosphate sensor.
Pssm-ID: 460807 [Multi-domain] Cd Length: 339 Bit Score: 154.26 E-value: 4.55e-41
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally ...
439-820
4.55e-36
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: 142.10 E-value: 4.55e-36
Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible ...
501-860
3.01e-14
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: 75.75 E-value: 3.01e-14
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
384-642
4.43e-12
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: 68.82 E-value: 4.43e-12
Sodium:sulfate symporter transmembrane region; There are also some members in this family that ...
419-866
5.50e-12
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: 68.94 E-value: 5.50e-12
Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to ...
501-747
2.68e-11
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: 66.53 E-value: 2.68e-11
Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in ...
498-763
8.24e-09
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: 58.82 E-value: 8.24e-09
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
2-35
1.24e-05
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). This domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. NUC-2 contains several ankyrin repeats. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with xenotropic and polytropic murine leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signaling and result in cell toxicity and death. The similarity between Syg1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, S. cerevisiae, and many other diverse organisms.
Pssm-ID: 269894 [Multi-domain] Cd Length: 143 Bit Score: 46.02 E-value: 1.24e-05
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally ...
671-877
1.18e-04
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: 45.41 E-value: 1.18e-04
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
2-44
3.98e-04
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-terminus of the human XPR1 protein (xenotropic and polytropic retrovirus receptor 1) binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all members of this family are involved in G-protein associated signal transduction. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with xenotropic and polytropic murine leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signaling and result in cell toxicity and death. Similarity between Syg1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organisms.
Pssm-ID: 269898 [Multi-domain] Cd Length: 161 Bit Score: 41.89 E-value: 3.98e-04
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
1-36
4.62e-04
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The SPX domain is found at the amino terminus of a variety of proteins. This family, mostly found in plants, contains a C-terminal MFS domain (major facilitator superfamily), suggesting a function as a secondary transporter. The function of this N-terminal region is unclear, although it might be involved in regulating transport.
Pssm-ID: 269900 [Multi-domain] Cd Length: 140 Bit Score: 41.12 E-value: 4.62e-04
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
252-276
1.23e-03
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. NUC-2 plays an important role in the phosphate-regulated signal transduction pathway in N. crassa. It shows high similarity to a cyclin-dependent kinase inhibitory protein Pho81, which is part of the phosphate regulatory cascade in S. cerevisiae. Both, NUC-2 and Pho81, have multi-domain architecture, including the SPX N-terminal domain following by several ankyrin repeats and a putative C-terminal glycerophosphodiester phosphodiesterase domain (GDPD) with unknown function.
Pssm-ID: 269904 [Multi-domain] Cd Length: 162 Bit Score: 40.31 E-value: 1.23e-03
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ...
256-276
2.88e-03
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The yeast protein Gde1/Ypl110c is similar to both, NUC-2 and Pho81, in sharing their multi-domain architecture, which includes the SPX N-terminal domain followed by several ankyrin repeats and a C-terminal glycerophosphodiester phosphodiesterase domain (GDPD). Gde1 hydrolyzes intracellular glycerophosphocholine into glycerolphosphate and choline, and plays a role in the utilization of glycerophosphocholine as a source for phosphate.
Pssm-ID: 269905 [Multi-domain] Cd Length: 134 Bit Score: 38.67 E-value: 2.88e-03
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
256-276
3.36e-03
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus binds directly to the G-protein beta subunit and inhibits transduction of the mating pheromone signal, and it co-occurs with a C-terminal domain from the EXS family.
Pssm-ID: 269896 [Multi-domain] Cd Length: 139 Bit Score: 38.70 E-value: 3.36e-03
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
2-46
4.87e-03
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. Vtc2 is part of the Saccharomyces cerevisiae membrane-integral VTC complex, together with Vtc1, Vtc3, and Vtc4. It contains an N-terminal SPX domain next to a central polyphosphate polymerase domain and a C-terminal domain of unknown function.
Pssm-ID: 269901 [Multi-domain] Cd Length: 135 Bit Score: 38.29 E-value: 4.87e-03
Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to ...
502-642
7.98e-03
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: 39.57 E-value: 7.98e-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.
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