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 ...
30-441
7.74e-149
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).
The actual alignment was detected with superfamily member pfam03092:
Pssm-ID: 308617 Cd Length: 432 Bit Score: 430.23 E-value: 7.74e-149
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative ...
30-441
7.74e-149
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: 430.23 E-value: 7.74e-149
Folate-biopterin transporter of the Major Facilitator Superfamily of transporters; The ...
21-424
1.02e-76
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: 244.44 E-value: 1.02e-76
folate/biopterin transporter; The Folate-Biopterin Transporter (FBT) Family (TC 2.A.71)The ...
27-437
6.28e-53
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: 184.22 E-value: 6.28e-53
BT1 family; Members of this family are transmembrane proteins. Several are Leishmania putative ...
30-441
7.74e-149
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: 430.23 E-value: 7.74e-149
Folate-biopterin transporter of the Major Facilitator Superfamily of transporters; The ...
21-424
1.02e-76
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: 244.44 E-value: 1.02e-76
folate/biopterin transporter; The Folate-Biopterin Transporter (FBT) Family (TC 2.A.71)The ...
27-437
6.28e-53
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: 184.22 E-value: 6.28e-53
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
23-425
3.68e-05
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: 45.88 E-value: 3.68e-05
Salmonella enterica Na+/melibiose symporter MelB and similar transporters of the Major ...
70-343
7.32e-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: 41.82 E-value: 7.32e-04
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
86-399
2.12e-03
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: 40.29 E-value: 2.12e-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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