folate/biopterin family major facilitator superfamily (MFS) transporter facilitates folate monoglutamate transport involved in tetrahydrofolate biosynthesis, as well as the transport of antifolates such as methotrexate and aminopterin
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative ...
61-473
1.74e-167
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative proteins that are thought to be pteridine transporters. One such protein Swiss:Q25272, previously termed (and is still annotated as) ORFG, was shown to encode a biopterin transport protein using null mutants, thus being subsequently renamed BT1. The significant similarity of ORFG/BT1 to Trypanosoma brucei ESAG10 (a putative transmembrane protein and another member of this family) was previously noted. This family also contains five putative Arabidopsis thaliana proteins of unknown function. In addition, it also contains two predicted prokaryotic proteins (from the cyanobacteria Synechocystis and Synechococcus).
:
Pssm-ID: 308617 Cd Length: 432 Bit Score: 479.92 E-value: 1.74e-167
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative ...
61-473
1.74e-167
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative proteins that are thought to be pteridine transporters. One such protein Swiss:Q25272, previously termed (and is still annotated as) ORFG, was shown to encode a biopterin transport protein using null mutants, thus being subsequently renamed BT1. The significant similarity of ORFG/BT1 to Trypanosoma brucei ESAG10 (a putative transmembrane protein and another member of this family) was previously noted. This family also contains five putative Arabidopsis thaliana proteins of unknown function. In addition, it also contains two predicted prokaryotic proteins (from the cyanobacteria Synechocystis and Synechococcus).
Pssm-ID: 308617 Cd Length: 432 Bit Score: 479.92 E-value: 1.74e-167
Folate-biopterin transporter of the Major Facilitator Superfamily of transporters; The ...
52-457
6.47e-159
Folate-biopterin transporter of the Major Facilitator Superfamily of transporters; The Folate-biopterin transporter (FBT) family includes folate carriers related to those of trypanosomatids in higher plant plastids and cyanobacteria. FBT mediates folate monoglutamate transport involved in tetrahydrofolate biosynthesis. It also mediates transport of antifolates, such as methotrexate and aminopterin. The FBT 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: 341037 [Multi-domain] Cd Length: 399 Bit Score: 456.69 E-value: 6.47e-159
folate/biopterin transporter; The Folate-Biopterin Transporter (FBT) Family (TC 2.A.71)The ...
66-460
8.42e-63
folate/biopterin transporter; The Folate-Biopterin Transporter (FBT) Family (TC 2.A.71)The only functionally characterized members of the family are from protozoa and include FT1, the major folate transporter in Leishmania, and BT1, the Leishmania biopterin/folate transporter. A related protein in Trypanosoma brucei, ESAGIO, shows weak folate/biopterin transport activity. [Cell envelope, Other]
Pssm-ID: 273268 Cd Length: 468 Bit Score: 211.95 E-value: 8.42e-63
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative ...
61-473
1.74e-167
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative proteins that are thought to be pteridine transporters. One such protein Swiss:Q25272, previously termed (and is still annotated as) ORFG, was shown to encode a biopterin transport protein using null mutants, thus being subsequently renamed BT1. The significant similarity of ORFG/BT1 to Trypanosoma brucei ESAG10 (a putative transmembrane protein and another member of this family) was previously noted. This family also contains five putative Arabidopsis thaliana proteins of unknown function. In addition, it also contains two predicted prokaryotic proteins (from the cyanobacteria Synechocystis and Synechococcus).
Pssm-ID: 308617 Cd Length: 432 Bit Score: 479.92 E-value: 1.74e-167
Folate-biopterin transporter of the Major Facilitator Superfamily of transporters; The ...
52-457
6.47e-159
Folate-biopterin transporter of the Major Facilitator Superfamily of transporters; The Folate-biopterin transporter (FBT) family includes folate carriers related to those of trypanosomatids in higher plant plastids and cyanobacteria. FBT mediates folate monoglutamate transport involved in tetrahydrofolate biosynthesis. It also mediates transport of antifolates, such as methotrexate and aminopterin. The FBT 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: 341037 [Multi-domain] Cd Length: 399 Bit Score: 456.69 E-value: 6.47e-159
folate/biopterin transporter; The Folate-Biopterin Transporter (FBT) Family (TC 2.A.71)The ...
66-460
8.42e-63
folate/biopterin transporter; The Folate-Biopterin Transporter (FBT) Family (TC 2.A.71)The only functionally characterized members of the family are from protozoa and include FT1, the major folate transporter in Leishmania, and BT1, the Leishmania biopterin/folate transporter. A related protein in Trypanosoma brucei, ESAGIO, shows weak folate/biopterin transport activity. [Cell envelope, Other]
Pssm-ID: 273268 Cd Length: 468 Bit Score: 211.95 E-value: 8.42e-63
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
96-448
1.35e-10
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: 62.83 E-value: 1.35e-10
AmpG and similar transporters of the Major Facilitator Superfamily; AmpG acts as an inner ...
54-321
1.17e-06
AmpG and similar transporters of the Major Facilitator Superfamily; AmpG acts as an inner membrane permease in the beta-lactamase induction system and in peptidoglycan recycling. It transports meuropeptide from the periplasm into the cytosol in gram-negative bacteria, which is essential for the induction of the ampC encoding beta-lactamase. The AmpG 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: 341039 [Multi-domain] Cd Length: 387 Bit Score: 50.68 E-value: 1.17e-06
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
116-428
3.78e-06
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters; This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-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: 340863 [Multi-domain] Cd Length: 383 Bit Score: 49.15 E-value: 3.78e-06
Major facilitator superfamily domain containing 3 protein; Major facilitator superfamily ...
91-428
7.50e-06
Major facilitator superfamily domain containing 3 protein; Major facilitator superfamily domain containing 3 protein (MFSD3) is a predicted acetyl-CoA transporter. As an atypical putative membrane-bound solute carrier (SLC), MFSD3 is most likely to be functionally active in the plasma membrane and not in any intracellular organelles. MFSD3 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: 341038 [Multi-domain] Cd Length: 386 Bit Score: 47.99 E-value: 7.50e-06
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ...
99-424
1.58e-04
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters; This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 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: 340883 [Multi-domain] Cd Length: 375 Bit Score: 44.10 E-value: 1.58e-04
Eukaryotic Solute carrier 46 (SLC46) family, Bacterial Tetracycline resistance proteins, and similar proteins of the Major Facilitator Superfamily of transporters; This family is composed of the eukaryotic proteins MFSD9, MFSD10, MFSD14, and SLC46 family proteins, as well as bacterial multidrug resistance (MDR) transporters such as tetracycline resistance protein TetA and multidrug resistance protein MdtG. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. TetA proteins confer resistance to tetracycline while MdtG confers resistance to fosfomycin and deoxycholate. The Solute carrier 46 (SLC46) family is composed of three vertebrate members (SLC46A1, SLC46A2, and SLC46A3), the best-studied of which is SLC46A1, which functions both as an intestinal proton-coupled high-affinity folate transporter involved in the absorption of folates and as an intestinal heme transporter which mediates heme uptake. MFSD10 facilitates the uptake of organic anions such as some non-steroidal anti-inflammatory drugs (NSAIDs) and confers resistance to such NSAIDs. The SLC46/TetA-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: 340888 [Multi-domain] Cd Length: 349 Bit Score: 42.57 E-value: 3.76e-04
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
99-370
6.69e-04
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: 42.21 E-value: 6.69e-04
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.
Click on the triangle to view details about the feature, including a multiple sequence alignment
of your query sequence and the protein sequences used to curate the domain model,
where hash marks (#) above the aligned sequences show the location of the conserved feature residues.
The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
Functional characterization of the conserved domain architecture found on the query.
Click here to see more details.
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
(labeled illustration) or all hits
(labeled illustration).
Domains are color coded according to superfamilies
to which they have been assigned. Hits with scores that pass a domain-specific threshold
(specific hits) are drawn in bright colors.
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
with the same color and shade of the domain or superfamily that provides the annotation. Mouse over the colored bars or triangles to see descriptions of the domains and features.
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)
mapped to the query sequence.
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
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
(CDART).
Modify your query to search against a different database and/or use advanced search options
