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 transporter; The ZIP family consists of zinc transport proteins and many putative ...
258-684
6.11e-74
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.
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Pssm-ID: 396884 [Multi-domain] Cd Length: 325 Bit Score: 241.90 E-value: 6.11e-74
ZIP Zinc transporter; The ZIP family consists of zinc transport proteins and many putative ...
258-684
6.11e-74
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: 241.90 E-value: 6.11e-74
UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily ...
593-650
7.60e-03
UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.
Pssm-ID: 259832 Cd Length: 162 Bit Score: 37.66 E-value: 7.60e-03
ZIP Zinc transporter; The ZIP family consists of zinc transport proteins and many putative ...
258-684
6.11e-74
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: 241.90 E-value: 6.11e-74
UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily ...
593-650
7.60e-03
UreI/Amis family, proton-gated urea channel and putative amide transporters; This subfamily includes UreI proton-gated urea channels as well as putative amide transporters (AmiS of the amidase gene cluster). Helicobacter pylori UreI (HpUreI), a proton-gated inner membrane urea channel opens in acidic pH to allow urea influx to the cytoplasm. There urea is metabolized, producing NH3 and Co2, leading to buffering of the periplasm. This action is essential for the survival of H. pylori in the stomach, and has been identified as a mechanism that could be clinically targeted to prevent various illnesses associated with infection by H. pylori. UreI and the related amide channels (AmiS) appear to function as hexamers, and have 6 predicted transmembrane segments. UreI has also been shown have a lipid "plug" in the center of the hexamer. Urea enters at the periplasmic opening of UreI and must pass 2 constriction sites, one on each side of a conserved Glu (Glu 177, H. pylori numbering), to reach the cytoplasm. Urea/thiourea selectivity is diminished by mutation of a conserved Trp to Ala or Phe in constriction site 2 (cytoplasmic). Channel functionality is greatly diminished by mutation of a conserved Trp in constriction site 1 (periplasmic) and a conserved Tyr in constriction site 2, and to a lesser extent a conserved Phe in site 1. In the cytoplasm, urease hydrolyzes urea to form ammonia and carbamate, which decomposes to carbonic acid. UreI is fully open at pH 5.0 to facilitate urea influx, but closes at neutral pH, preventing over-alkalization. Glu 177 (H. pylori numbering) is present in urea channel proteins, but absent in the related amide channels, suggesting that it plays a role in urea specificity.
Pssm-ID: 259832 Cd Length: 162 Bit Score: 37.66 E-value: 7.60e-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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(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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