ZIP family transporter may function as a zinc transporter, mediating the uptake of zinc in bacteria or the transport of zinc from one cellular compartment to another in eukaryotes
ZIP zinc/iron transport family; The Zinc (Zn2+)-Iron (Fe2+) Permease (ZIP) Family (TC 2.A.5) ...
38-339
1.39e-167
ZIP zinc/iron transport family; The Zinc (Zn2+)-Iron (Fe2+) Permease (ZIP) Family (TC 2.A.5)Members of the ZIP family consist of proteins with eight putative transmembrane spanners. They are derived from animals, plants and yeast. Theycomprise a diverse family, with several paralogues in any one organism (e.g., at least five in Caenorabditis elegans, at least five in Arabidopsis thaliana and two inSaccharomyces cervisiae. The two S. cerevisiae proteins, Zrt1 and Zrt2, both probably transport Zn2+ with high specificity, but Zrt1 transports Zn2+ with ten-fold higher affinitythan Zrt2. Some members of the ZIP family have been shown to transport Zn2+ while others transport Fe2+, and at least one transports a range of metal ions. The energy source fortransport has not been characterized, but these systems probably function as secondary carriers. [Transport and binding proteins, Cations and iron carrying compounds]
:
Pssm-ID: 273287 Cd Length: 324 Bit Score: 469.18 E-value: 1.39e-167
ZIP zinc/iron transport family; The Zinc (Zn2+)-Iron (Fe2+) Permease (ZIP) Family (TC 2.A.5) ...
38-339
1.39e-167
ZIP zinc/iron transport family; The Zinc (Zn2+)-Iron (Fe2+) Permease (ZIP) Family (TC 2.A.5)Members of the ZIP family consist of proteins with eight putative transmembrane spanners. They are derived from animals, plants and yeast. Theycomprise a diverse family, with several paralogues in any one organism (e.g., at least five in Caenorabditis elegans, at least five in Arabidopsis thaliana and two inSaccharomyces cervisiae. The two S. cerevisiae proteins, Zrt1 and Zrt2, both probably transport Zn2+ with high specificity, but Zrt1 transports Zn2+ with ten-fold higher affinitythan Zrt2. Some members of the ZIP family have been shown to transport Zn2+ while others transport Fe2+, and at least one transports a range of metal ions. The energy source fortransport has not been characterized, but these systems probably function as secondary carriers. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273287 Cd Length: 324 Bit Score: 469.18 E-value: 1.39e-167
ZIP Zinc transporter; The ZIP family consists of zinc transport proteins and many putative ...
53-336
3.91e-81
ZIP Zinc transporter; The ZIP family consists of zinc transport proteins and many putative metal transporters. The main contribution to this family is from the Arabidopsis thaliana ZIP protein family these proteins are responsible for zinc uptake in the plant. Also found within this family are C. elegans proteins of unknown function which are annotated as being similar to human growth arrest inducible gene product, although this protein in not found within this family.
Pssm-ID: 396884 [Multi-domain] Cd Length: 325 Bit Score: 249.60 E-value: 3.91e-81
ZIP zinc/iron transport family; The Zinc (Zn2+)-Iron (Fe2+) Permease (ZIP) Family (TC 2.A.5) ...
38-339
1.39e-167
ZIP zinc/iron transport family; The Zinc (Zn2+)-Iron (Fe2+) Permease (ZIP) Family (TC 2.A.5)Members of the ZIP family consist of proteins with eight putative transmembrane spanners. They are derived from animals, plants and yeast. Theycomprise a diverse family, with several paralogues in any one organism (e.g., at least five in Caenorabditis elegans, at least five in Arabidopsis thaliana and two inSaccharomyces cervisiae. The two S. cerevisiae proteins, Zrt1 and Zrt2, both probably transport Zn2+ with high specificity, but Zrt1 transports Zn2+ with ten-fold higher affinitythan Zrt2. Some members of the ZIP family have been shown to transport Zn2+ while others transport Fe2+, and at least one transports a range of metal ions. The energy source fortransport has not been characterized, but these systems probably function as secondary carriers. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273287 Cd Length: 324 Bit Score: 469.18 E-value: 1.39e-167
ZIP Zinc transporter; The ZIP family consists of zinc transport proteins and many putative ...
53-336
3.91e-81
ZIP Zinc transporter; The ZIP family consists of zinc transport proteins and many putative metal transporters. The main contribution to this family is from the Arabidopsis thaliana ZIP protein family these proteins are responsible for zinc uptake in the plant. Also found within this family are C. elegans proteins of unknown function which are annotated as being similar to human growth arrest inducible gene product, although this protein in not found within this family.
Pssm-ID: 396884 [Multi-domain] Cd Length: 325 Bit Score: 249.60 E-value: 3.91e-81
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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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
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Domains are color coded according to superfamilies
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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
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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)
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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
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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
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