ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid ...
314-618
1.36e-24
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
The actual alignment was detected with superfamily member COG1173:
Pssm-ID: 440786 [Multi-domain] Cd Length: 275 Bit Score: 103.65 E-value: 1.36e-24
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid ...
39-267
2.01e-13
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
The actual alignment was detected with superfamily member COG0601:
Pssm-ID: 440366 [Multi-domain] Cd Length: 314 Bit Score: 71.64 E-value: 2.01e-13
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid ...
314-618
1.36e-24
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440786 [Multi-domain] Cd Length: 275 Bit Score: 103.65 E-value: 1.36e-24
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid ...
39-267
2.01e-13
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440366 [Multi-domain] Cd Length: 314 Bit Score: 71.64 E-value: 2.01e-13
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
79-279
7.97e-05
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others.
Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 43.81 E-value: 7.97e-05
Binding-protein-dependent transport system inner membrane component; The alignments cover the ...
101-284
1.79e-04
Binding-protein-dependent transport system inner membrane component; The alignments cover the most conserved region of the proteins, which is thought to be located in a cytoplasmic loop between two transmembrane domains. The members of this family have a variable number of transmembrane helices.
Pssm-ID: 334128 [Multi-domain] Cd Length: 183 Bit Score: 42.67 E-value: 1.79e-04
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
400-556
3.19e-03
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others.
Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 39.18 E-value: 3.19e-03
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid ...
314-618
1.36e-24
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440786 [Multi-domain] Cd Length: 275 Bit Score: 103.65 E-value: 1.36e-24
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid ...
39-267
2.01e-13
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440366 [Multi-domain] Cd Length: 314 Bit Score: 71.64 E-value: 2.01e-13
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
79-279
7.97e-05
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others.
Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 43.81 E-value: 7.97e-05
Binding-protein-dependent transport system inner membrane component; The alignments cover the ...
101-284
1.79e-04
Binding-protein-dependent transport system inner membrane component; The alignments cover the most conserved region of the proteins, which is thought to be located in a cytoplasmic loop between two transmembrane domains. The members of this family have a variable number of transmembrane helices.
Pssm-ID: 334128 [Multi-domain] Cd Length: 183 Bit Score: 42.67 E-value: 1.79e-04
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid ...
81-233
2.32e-03
ABC-type dipeptide/oligopeptide/nickel transport system, permease component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440786 [Multi-domain] Cd Length: 275 Bit Score: 40.10 E-value: 2.32e-03
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
400-556
3.19e-03
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others.
Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 39.18 E-value: 3.19e-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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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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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,
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
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advanced search options)
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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