sodium:proton antiporter NhaD; Proteins of this family usually have 10-13 transmembrane ...
57-461
0e+00
sodium:proton antiporter NhaD; Proteins of this family usually have 10-13 transmembrane regions. They extrudes Na+ or Li+ in exchange for H+. They have been identified and characterized in a number of bacterial species.
The actual alignment was detected with superfamily member NF038006:
Pssm-ID: 439423 Cd Length: 405 Bit Score: 688.50 E-value: 0e+00
sodium:proton antiporter NhaD; Proteins of this family usually have 10-13 transmembrane ...
57-461
0e+00
sodium:proton antiporter NhaD; Proteins of this family usually have 10-13 transmembrane regions. They extrudes Na+ or Li+ in exchange for H+. They have been identified and characterized in a number of bacterial species.
Pssm-ID: 439423 Cd Length: 405 Bit Score: 688.50 E-value: 0e+00
Na+/H+ antiporter, NhaD family; These proteins are members of the NhaD Na+:H+ Antiporter (NhaD) ...
48-476
1.01e-129
Na+/H+ antiporter, NhaD family; These proteins are members of the NhaD Na+:H+ Antiporter (NhaD) Family (TC 2.A.62). A single member of the NhaD family has been characterized. This protein is the NhaD protein of Vibrio parahaemolyticus which has 12 GES predicted transmembrane regions. It has been shown to catalyze Na+/H+ antiport, but Li+ can also be a substrate. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 129857 Cd Length: 420 Bit Score: 382.32 E-value: 1.01e-129
Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible ...
42-470
1.26e-76
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: 245.62 E-value: 1.26e-76
sodium:proton antiporter NhaD; Proteins of this family usually have 10-13 transmembrane ...
57-461
0e+00
sodium:proton antiporter NhaD; Proteins of this family usually have 10-13 transmembrane regions. They extrudes Na+ or Li+ in exchange for H+. They have been identified and characterized in a number of bacterial species.
Pssm-ID: 439423 Cd Length: 405 Bit Score: 688.50 E-value: 0e+00
Na+/H+ antiporter, NhaD family; These proteins are members of the NhaD Na+:H+ Antiporter (NhaD) ...
48-476
1.01e-129
Na+/H+ antiporter, NhaD family; These proteins are members of the NhaD Na+:H+ Antiporter (NhaD) Family (TC 2.A.62). A single member of the NhaD family has been characterized. This protein is the NhaD protein of Vibrio parahaemolyticus which has 12 GES predicted transmembrane regions. It has been shown to catalyze Na+/H+ antiport, but Li+ can also be a substrate. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 129857 Cd Length: 420 Bit Score: 382.32 E-value: 1.01e-129
Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible ...
42-470
1.26e-76
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: 245.62 E-value: 1.26e-76
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
100-469
6.08e-33
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: 128.91 E-value: 6.08e-33
Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to ...
103-459
1.82e-06
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: 49.97 E-value: 1.82e-06
Anion permease ArsB. These permeases have been shown to export arsenate and antimonite in ...
104-444
4.82e-03
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: 39.17 E-value: 4.82e-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.
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