cation diffusion facilitator (CDF) family transporter facilitates the active efflux of one or more from a variety of metal cations including Zn, Cd, Ni, Co, Mn, and Cu
cation diffusion facilitator family transporter; This model describes a broadly distributed ...
22-285
2.53e-63
cation diffusion facilitator family transporter; This model describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273544 [Multi-domain] Cd Length: 268 Bit Score: 200.52 E-value: 2.53e-63
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
23-205
2.98e-41
Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.
Pssm-ID: 426316 [Multi-domain] Cd Length: 189 Bit Score: 141.25 E-value: 2.98e-41
alkaline shock response membrane anchor protein AmaP; The founding member of this family, AmaP ...
220-284
7.34e-03
alkaline shock response membrane anchor protein AmaP; The founding member of this family, AmaP (Asp23 membrane anchoring protein), is related to Asp23 through part of its length, but includes a highly hydrophobic N-terminal region that should make it an integral membrane protein. Asp23 (alkaline shock protein of 23 kDa), described in PMID:7864904, is a cytosolic protein in Staphylococcus aureus, strongly induced by a pH shift from 7 to 10, and also recruited to the membrane. AmaP appears to be the partner protein with an integral membrane segment and the ability to anchor Asp23 to the membrane. This model was built to identify full-length homologs of AmaP, while excluding Asp23. Some but not all members of this family score above the cutoffs of Pfam model version PF03780.11, but full-length homologs of Asp23 score considerably higher. Asp23 family members previously were known as DUF322.
Pssm-ID: 468002 Cd Length: 166 Bit Score: 36.41 E-value: 7.34e-03
cation diffusion facilitator family transporter; This model describes a broadly distributed ...
22-285
2.53e-63
cation diffusion facilitator family transporter; This model describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273544 [Multi-domain] Cd Length: 268 Bit Score: 200.52 E-value: 2.53e-63
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
23-205
2.98e-41
Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.
Pssm-ID: 426316 [Multi-domain] Cd Length: 189 Bit Score: 141.25 E-value: 2.98e-41
dimerization domain of Zinc Transporter; ZT_dimer is the dimerization region of the whole ...
214-285
2.01e-17
dimerization domain of Zinc Transporter; ZT_dimer is the dimerization region of the whole molecule of zinc transporters since the full-length members form a homodimer during activity. The domain lies within the cytoplasm and exhibits an overall structural similarity with the copper metallochaperone Hah1 UniProtKB:O00244, exhibiting an open alpha-beta domain with two alpha helices (H1 and H2) aligned on one side and a three-stranded mixed beta-sheet (S1 to S3) on the other side. The N-terminal part of the members is the Cation_efflux family, pfam01545.
Pssm-ID: 465312 [Multi-domain] Cd Length: 74 Bit Score: 74.80 E-value: 2.01e-17
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
13-106
1.47e-03
Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.
Pssm-ID: 426316 [Multi-domain] Cd Length: 189 Bit Score: 38.79 E-value: 1.47e-03
alkaline shock response membrane anchor protein AmaP; The founding member of this family, AmaP ...
220-284
7.34e-03
alkaline shock response membrane anchor protein AmaP; The founding member of this family, AmaP (Asp23 membrane anchoring protein), is related to Asp23 through part of its length, but includes a highly hydrophobic N-terminal region that should make it an integral membrane protein. Asp23 (alkaline shock protein of 23 kDa), described in PMID:7864904, is a cytosolic protein in Staphylococcus aureus, strongly induced by a pH shift from 7 to 10, and also recruited to the membrane. AmaP appears to be the partner protein with an integral membrane segment and the ability to anchor Asp23 to the membrane. This model was built to identify full-length homologs of AmaP, while excluding Asp23. Some but not all members of this family score above the cutoffs of Pfam model version PF03780.11, but full-length homologs of Asp23 score considerably higher. Asp23 family members previously were known as DUF322.
Pssm-ID: 468002 Cd Length: 166 Bit Score: 36.41 E-value: 7.34e-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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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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,
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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
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the domain superfamily to which the specific and non-specific hits belong
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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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