SLAC1 (Slow Anion Channel-Associated 1) family protein similar to SLAC1 that is essential for stomatal closure in response to carbon dioxide, abscisic acid, ozone, light/dark transitions, humidity change, calcium ions, hydrogen peroxide and nitric oxide
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion ...
257-507
5.30e-99
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion Channel-Associated 1); SLAC1 (Slow Anion Channel-Associated 1) is a plasma membrane protein, preferentially expressed in guard cells, which encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. It is essential for stomatal closure in response to carbon dioxide, abscisic acid, ozone, light/dark transitions, humidity change, calcium ions, hydrogen peroxide and nitric oxide. In the Arabidopsis genome, SLAC1 is part of a gene family with five members and encodes a membrane protein that has ten putative transmembrane domains flanked by large N- and C-terminal domains. Mutations in SLAC1 impair slow (S-type) anion channel currents that are activated by cytosolic calcium ions and abscisic acid, but do not affect rapid (R-type) anion channel currents or calcium ion channel function.
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Pssm-ID: 187763 Cd Length: 297 Bit Score: 300.23 E-value: 5.30e-99
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion ...
257-507
5.30e-99
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion Channel-Associated 1); SLAC1 (Slow Anion Channel-Associated 1) is a plasma membrane protein, preferentially expressed in guard cells, which encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. It is essential for stomatal closure in response to carbon dioxide, abscisic acid, ozone, light/dark transitions, humidity change, calcium ions, hydrogen peroxide and nitric oxide. In the Arabidopsis genome, SLAC1 is part of a gene family with five members and encodes a membrane protein that has ten putative transmembrane domains flanked by large N- and C-terminal domains. Mutations in SLAC1 impair slow (S-type) anion channel currents that are activated by cytosolic calcium ions and abscisic acid, but do not affect rapid (R-type) anion channel currents or calcium ion channel function.
Pssm-ID: 187763 Cd Length: 297 Bit Score: 300.23 E-value: 5.30e-99
Voltage-dependent anion channel; This family of transporters has ten alpha helical ...
257-493
8.55e-35
Voltage-dependent anion channel; This family of transporters has ten alpha helical transmembrane segments. The structure of a bacterial homolog of SLAC1 shows it to have a trimeric arrangement. The pore is composed of five helices with a conserved Phe residue involved in gating. One homolog, Mae1 from the yeast Schizosaccharomyces pombe, functions as a malate uptake transporter; another, Ssu1 from Saccharomyces cerevisiae and other fungi including Aspergillus fumigatus, is characterized as a sulfite efflux pump; and TehA from Escherichia coli is identified as a tellurite resistance protein by virtue of its association in the tehA/tehB operon. In plants, this family is found in the stomatal guard cells functioning as an anion-transporting pore. Many homologs are incorrectly annotated as tellurite resistance or dicarboxylate transporter (TDT) proteins.
Pssm-ID: 460983 Cd Length: 321 Bit Score: 132.75 E-value: 8.55e-35
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion ...
257-507
5.30e-99
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes SLAC1 (Slow Anion Channel-Associated 1); SLAC1 (Slow Anion Channel-Associated 1) is a plasma membrane protein, preferentially expressed in guard cells, which encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. It is essential for stomatal closure in response to carbon dioxide, abscisic acid, ozone, light/dark transitions, humidity change, calcium ions, hydrogen peroxide and nitric oxide. In the Arabidopsis genome, SLAC1 is part of a gene family with five members and encodes a membrane protein that has ten putative transmembrane domains flanked by large N- and C-terminal domains. Mutations in SLAC1 impair slow (S-type) anion channel currents that are activated by cytosolic calcium ions and abscisic acid, but do not affect rapid (R-type) anion channel currents or calcium ion channel function.
Pssm-ID: 187763 Cd Length: 297 Bit Score: 300.23 E-value: 5.30e-99
The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes TehA proteins; The ...
263-507
2.81e-66
The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes TehA proteins; The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane a-helical spanners (TMSs).
Pssm-ID: 187762 Cd Length: 289 Bit Score: 215.48 E-value: 2.81e-66
Voltage-dependent anion channel; This family of transporters has ten alpha helical ...
257-493
8.55e-35
Voltage-dependent anion channel; This family of transporters has ten alpha helical transmembrane segments. The structure of a bacterial homolog of SLAC1 shows it to have a trimeric arrangement. The pore is composed of five helices with a conserved Phe residue involved in gating. One homolog, Mae1 from the yeast Schizosaccharomyces pombe, functions as a malate uptake transporter; another, Ssu1 from Saccharomyces cerevisiae and other fungi including Aspergillus fumigatus, is characterized as a sulfite efflux pump; and TehA from Escherichia coli is identified as a tellurite resistance protein by virtue of its association in the tehA/tehB operon. In plants, this family is found in the stomatal guard cells functioning as an anion-transporting pore. Many homologs are incorrectly annotated as tellurite resistance or dicarboxylate transporter (TDT) proteins.
Pssm-ID: 460983 Cd Length: 321 Bit Score: 132.75 E-value: 8.55e-35
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes TehA protein; This ...
259-476
9.28e-21
Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes TehA protein; This subfamily includes Tellurite resistance protein TehA that belongs to the C4-dicarboxylate transporter/malic acid transport (TDT) protein family and is a homolog of plant Slow Anion Channel-Associated 1 (SLAC1). The tehA gene encodes an integral membrane protein that has been shown to have efflux activity of quaternary ammonium compounds. TehA protein of Escherichia coli functions as a tellurite-resistance uptake permease.
Pssm-ID: 187764 Cd Length: 301 Bit Score: 92.71 E-value: 9.28e-21
The Tellurite-resistance/Dicarboxylate Transporter (TDT) family; The Tellurite-resistance ...
296-470
1.80e-09
The Tellurite-resistance/Dicarboxylate Transporter (TDT) family; The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane a-helical spanners (TMSs).
Pssm-ID: 187761 Cd Length: 327 Bit Score: 59.24 E-value: 1.80e-09
C4-dicarboxylate transporters of the Tellurite-resistance/Dicarboxylate Transporter (TDT) ...
259-464
2.16e-03
C4-dicarboxylate transporters of the Tellurite-resistance/Dicarboxylate Transporter (TDT) family; This subfamily contains bacterial C4-dicarboxylate transporters, which is part of the Tellurite-resistance/Dicarboxylate Transporter (TDT) family. It includes Tellurite resistance protein tehA; the tehA gene encodes an integral membrane protein that has been shown to have efflux activity of quaternary ammonium compounds. TehA protein of Escherichia coli functions as a tellurite-resistance uptake permease.
Pssm-ID: 187765 Cd Length: 293 Bit Score: 40.22 E-value: 2.16e-03
The Tellurite-resistance/Dicarboxylate Transporter (TDT) family; The Tellurite-resistance ...
263-470
2.42e-03
The Tellurite-resistance/Dicarboxylate Transporter (TDT) family; The Tellurite-resistance/Dicarboxylate Transporter (TDT) family includes members from all three kingdoms, but only three members of the family have been functionally characterized: the TehA protein of E. coli functioning as a tellurite-resistance uptake permease, the Mae1 protein of S. pombe functioning in the uptake of malate and other dicarboxylates, and the sulfite efflux pump (SSU1) of Saccharomyces cerevisiae. In plants, the plasma membrane protein SLAC1 (Slow Anion Channel-Associated 1), which is preferentially expressed in guard cells, encodes a distant homolog of fungal and bacterial dicarboxylate/malic acid transport proteins. SLAC1 is essential in mediating stomatal responses to physiological and stress stimuli. Members of the TDT family exhibit 10 putative transmembrane alpha-helical spanners (TMSs).
Pssm-ID: 187756 Cd Length: 326 Bit Score: 40.00 E-value: 2.42e-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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