sodium-dependent phosphate transport protein 2 may be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane
Na+/Pi-cotransporter; This is a family of mainly mammalian type II renal Na+/Pi-cotransporters ...
113-204
2.45e-17
Na+/Pi-cotransporter; This is a family of mainly mammalian type II renal Na+/Pi-cotransporters with other related sequences from lower eukaryotes and bacteria some of which are also Na+/Pi-cotransporters. In the kidney the type II renal Na+/Pi-cotransporters protein allows re-absorption of filtered Pi in the proximal tubule.
Pssm-ID: 460653 [Multi-domain] Cd Length: 137 Bit Score: 78.21 E-value: 2.45e-17
Na+/Pi-cotransporter; This is a family of mainly mammalian type II renal Na+/Pi-cotransporters ...
113-204
2.45e-17
Na+/Pi-cotransporter; This is a family of mainly mammalian type II renal Na+/Pi-cotransporters with other related sequences from lower eukaryotes and bacteria some of which are also Na+/Pi-cotransporters. In the kidney the type II renal Na+/Pi-cotransporters protein allows re-absorption of filtered Pi in the proximal tubule.
Pssm-ID: 460653 [Multi-domain] Cd Length: 137 Bit Score: 78.21 E-value: 2.45e-17
Na/Pi-cotransporter; This model describes essentially the full length of an uncharacterized ...
146-204
7.63e-03
Na/Pi-cotransporter; This model describes essentially the full length of an uncharacterized protein from Bacillus subtilis and correponding lengths of longer proteins from E. coli and Treponema pallidum. PSI-BLAST analysis converges to demonstrate homology to one other group of proteins, type II sodium/phosphate (Na/Pi) cotransporters. A well-conserved repeated domain in this family, approximately 60 residues in length, is also repeated in the Na/Pi cotransporters, although with greater spacing between the repeats. The two families share additional homology in the region after the first repeat, share the properly of having extensive hydrophobic regions, and may be similar in function. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273225 [Multi-domain] Cd Length: 308 Bit Score: 38.36 E-value: 7.63e-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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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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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.
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(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.
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(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
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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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