major facilitator superfamily (MFS) transporter facilitates the transport across cytoplasmic or internal membranes of one or more from a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
25-449
1.78e-111
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major Facilitator Superfamily; This family is composed of Salmonella enterica Na+/melibiose symporter MelB, Major Facilitator Superfamily domain-containing proteins, MFSD2 and MFSD12, and other sugar transporters. MelB catalyzes the electrogenic symport of galactosides with Na+, Li+ or H+. The MFSD2 subfamily is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. MelB-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
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Pssm-ID: 340890 [Multi-domain] Cd Length: 424 Bit Score: 335.34 E-value: 1.78e-111
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
25-449
1.78e-111
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major Facilitator Superfamily; This family is composed of Salmonella enterica Na+/melibiose symporter MelB, Major Facilitator Superfamily domain-containing proteins, MFSD2 and MFSD12, and other sugar transporters. MelB catalyzes the electrogenic symport of galactosides with Na+, Li+ or H+. The MFSD2 subfamily is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. MelB-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340890 [Multi-domain] Cd Length: 424 Bit Score: 335.34 E-value: 1.78e-111
sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH): ...
25-462
7.79e-87
sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH):Cation Symporter Family (TC 2.A.2) GPH:cation symporters catalyze uptake of sugars in symport with a monovalent cation (H+ or Na+). Members of this family includes transporters for melibiose, lactose, raffinose, glucuronides, pentosides and isoprimeverose. Mutants of two groups of these symporters (the melibiose permeases of enteric bacteria, and the lactose permease of Streptococcus thermophilus) have been isolated in which altered cation specificity is observed or in which sugar transport is uncoupled from cation symport (i.e., uniport is catalyzed). The various members of the family can use Na+, H+ or Li, Na+ or Li+, H+ or Li+, or only H+ as the symported cation. All of these proteins possess twelve putative transmembrane a-helical spanners. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273270 Cd Length: 437 Bit Score: 272.59 E-value: 7.79e-87
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
25-449
1.78e-111
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major Facilitator Superfamily; This family is composed of Salmonella enterica Na+/melibiose symporter MelB, Major Facilitator Superfamily domain-containing proteins, MFSD2 and MFSD12, and other sugar transporters. MelB catalyzes the electrogenic symport of galactosides with Na+, Li+ or H+. The MFSD2 subfamily is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. MelB-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340890 [Multi-domain] Cd Length: 424 Bit Score: 335.34 E-value: 1.78e-111
sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH): ...
25-462
7.79e-87
sugar (Glycoside-Pentoside-Hexuronide) transporter; The Glycoside-Pentoside-Hexuronide (GPH):Cation Symporter Family (TC 2.A.2) GPH:cation symporters catalyze uptake of sugars in symport with a monovalent cation (H+ or Na+). Members of this family includes transporters for melibiose, lactose, raffinose, glucuronides, pentosides and isoprimeverose. Mutants of two groups of these symporters (the melibiose permeases of enteric bacteria, and the lactose permease of Streptococcus thermophilus) have been isolated in which altered cation specificity is observed or in which sugar transport is uncoupled from cation symport (i.e., uniport is catalyzed). The various members of the family can use Na+, H+ or Li, Na+ or Li+, H+ or Li+, or only H+ as the symported cation. All of these proteins possess twelve putative transmembrane a-helical spanners. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273270 Cd Length: 437 Bit Score: 272.59 E-value: 7.79e-87
Major facilitator superfamily domain-containing protein 2 subfamily; The major facilitator ...
25-415
2.52e-14
Major facilitator superfamily domain-containing protein 2 subfamily; The major facilitator superfamily domain-containing protein 2 (MFSD2) subfamily is composed of two vertebrate members, MFSD2A amd MFSD2B. MFSD2A is more commonly called sodium-dependent lysophosphatidylcholine symporter 1 (NLS1). It is an LPC symporter that plays an essential role for blood-brain barrier formation and function. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. The MFSD2 subfamily belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340950 Cd Length: 446 Bit Score: 74.81 E-value: 2.52e-14
Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of ...
25-415
1.15e-12
Sodium-dependent lysophosphatidylcholine symporter 1 of the Major Facilitator Superfamily of transporters; Sodium-dependent lysophosphatidylcholine (LPC) symporter 1 (NLS1) is also called major facilitator superfamily domain-containing protein 2A (MFSD2A). NLS1/MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. It also transports the essential omega-3 fatty acid docosahexaenoic acid (DHA), which is essential for normal brain growth and cognitive function, in the form of LPC into the brain across the blood-brain barrier. Inactivating mutations in MFSD2A cause a lethal microcephaly syndrome. NLS1/MFSD2A belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 341009 Cd Length: 419 Bit Score: 69.46 E-value: 1.15e-12
Major facilitator superfamily domain-containing protein 2B; Major facilitator superfamily ...
25-418
2.53e-12
Major facilitator superfamily domain-containing protein 2B; Major facilitator superfamily domain-containing protein 2B (MFSD2B) is closely related to MFSD2A, and their conserved genomic structure suggests that they are derived from the duplication of an ancestral gene. Variations of chromosome 2 gene expressions among patients with lung cancer or non-cancer identified MFSD2B as a potential risk or protect factor in the prognosis of lung adenocarcinoma. MFSD2B belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 341010 Cd Length: 416 Bit Score: 68.31 E-value: 2.53e-12
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
50-404
4.17e-04
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.
Pssm-ID: 349949 [Multi-domain] Cd Length: 378 Bit Score: 42.41 E-value: 4.17e-04
Major facilitator superfamily domain-containing protein 12; Major facilitator superfamily ...
45-192
1.77e-03
Major facilitator superfamily domain-containing protein 12; Major facilitator superfamily domain-containing protein 12 (MFSD12) protein subfamily includes a group of uncharacterized proteins similar to human MFSD2. MFSD2 is composed of two vertebrate members, MFSD2A and MFSD2B. MFSD2A is an LPC symporter that plays an essential role for blood-brain barrier formation and function. MFSD2B is a potential risk or protect factor in the prognosis of lung adenocarcinoma. The MFSD12 subfamily belongs to the Salmonella enterica Na+/melibiose symporter like (MelB-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 341044 Cd Length: 438 Bit Score: 40.70 E-value: 1.77e-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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Domains are color coded according to superfamilies
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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
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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