Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
28-344
5.07e-129
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.
The actual alignment was detected with superfamily member cd17399:
Pssm-ID: 475125 Cd Length: 419 Bit Score: 380.07 E-value: 5.07e-129
Major facilitator superfamily domain-containing protein 7; Major facilitator superfamily ...
28-344
5.07e-129
Major facilitator superfamily domain-containing protein 7; Major facilitator superfamily domain-containing protein 7 (MFSD7) is also called myosin light polypeptide 5 regulatory protein (MYL5). It's function is unknown. It is encoded by the a SLC49A3 gene and is a member of the Solute carrier 49 (SLC49) family, which also includes feline leukemia virus subgroup C receptor 1 (FLVCR1, SLC49A1), FLVCR2 (SLC49A2), as well as disrupted in renal carcinoma protein 2 (DIRC2, SLC49A4). FLVCR1 and FLVCR2 are heme transporters. DIRC2 is an electrogenic lysosomal metabolite transporter that is regulated by limited proteolytic processing by cathepsin L. MFSD7 belongs to 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: 340957 Cd Length: 419 Bit Score: 380.07 E-value: 5.07e-129
Major facilitator superfamily domain-containing protein 7; Major facilitator superfamily ...
28-344
5.07e-129
Major facilitator superfamily domain-containing protein 7; Major facilitator superfamily domain-containing protein 7 (MFSD7) is also called myosin light polypeptide 5 regulatory protein (MYL5). It's function is unknown. It is encoded by the a SLC49A3 gene and is a member of the Solute carrier 49 (SLC49) family, which also includes feline leukemia virus subgroup C receptor 1 (FLVCR1, SLC49A1), FLVCR2 (SLC49A2), as well as disrupted in renal carcinoma protein 2 (DIRC2, SLC49A4). FLVCR1 and FLVCR2 are heme transporters. DIRC2 is an electrogenic lysosomal metabolite transporter that is regulated by limited proteolytic processing by cathepsin L. MFSD7 belongs to 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: 340957 Cd Length: 419 Bit Score: 380.07 E-value: 5.07e-129
Solute carrier 49 (SLC49) family of the Major Facilitator Superfamily of transporters; The ...
28-344
3.62e-95
Solute carrier 49 (SLC49) family of the Major Facilitator Superfamily of transporters; The Solute carrier 49 (SLC49) family is composed of four members: feline leukemia virus subgroup C receptor 1 (FLVCR1, SLC49A1); FLVCR2 (SLC49A2); major facilitator superfamily domain-containing protein 7 (MFSD7, SLC49A3); and disrupted in renal carcinoma protein 2 (DIRC2, SLC49A4). FLVCR1 and FLVCR2 are heme transporters. In addition, FLVCR2 also functions as a transporter for a calcium-chelator complex that is important for growth and calcium metabolism. The function of MFSD7 is unknown. DIRC2 is an electrogenic lysosomal metabolite transporter that is regulated by limited proteolytic processing by cathepsin L. The SLC49 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: 340892 [Multi-domain] Cd Length: 407 Bit Score: 292.77 E-value: 3.62e-95
Feline leukemia virus subgroup C receptor subfamily of the Major Facilitator Superfamily of ...
28-301
9.04e-27
Feline leukemia virus subgroup C receptor subfamily of the Major Facilitator Superfamily of transporters; The Feline leukemia virus subgroup C receptor (FLVCR) subfamily is conserved in metazoans and is composed of two vertebrate members, FLVCR1 and FLVCR2. FLVCR1 is a heme transporter and it has two isoforms: 1 (or FLVCR1a), which exports cytoplasmic heme as well as coproporphyrin and protoporphyrin IX; and 2 (FLVCR1b), which promotes heme efflux from the mitochondrion to the cytoplasm. FLVCR2 functions as a heme importer as well as a transporter for a calcium-chelator complex that is important for growth and calcium metabolism. The FLVCR subfamily belongs to the Solute carrier 49 (SLC49) 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: 340956 [Multi-domain] Cd Length: 406 Bit Score: 111.56 E-value: 9.04e-27
Disrupted in renal carcinoma protein 2 of the Major Facilitator Superfamily of transporters; ...
108-299
3.37e-17
Disrupted in renal carcinoma protein 2 of the Major Facilitator Superfamily of transporters; Disrupted in renal carcinoma protein 2 or disrupted in renal cancer protein 2 (DIRC2), encoded by the SLC49A4 gene, was initially identified as a breakpoint-spanning gene in a chromosomal translocation associated with the development of renal cancer. It is an electrogenic lysosomal metabolite transporter that is regulated by limited proteolytic processing by cathepsin L. DIRC2 belongs to the Solute carrier 49 (SLC49) 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: 340955 [Multi-domain] Cd Length: 381 Bit Score: 83.12 E-value: 3.37e-17
Feline leukemia virus subgroup C receptor-related protein 1 of the Major Facilitator ...
28-302
3.14e-14
Feline leukemia virus subgroup C receptor-related protein 1 of the Major Facilitator Superfamily of transporters; Feline leukemia virus subgroup C receptor-related protein 1 (FLVCR1) is also called feline leukemia virus subgroup C receptor (FLVCR). FLVCR1 is a heme transporter and it has two isoforms: 1 (or FLVCR1a), which exports cytoplasmic heme as well as coproporphyrin and protoporphyrin IX; and 2 (FLVCR1b), which promotes heme efflux from the mitochondrion to the cytoplasm. Mutations in the FLVCR1 gene have been linked to vision impairment, posterior column ataxia, and sensory neurodegeneration with loss of pain perception. FLVCR1 belongs to the Solute carrier 49 (SLC49) 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: 341013 Cd Length: 407 Bit Score: 74.10 E-value: 3.14e-14
Feline leukemia virus subgroup C receptor-related protein 2 of the Major Facilitator ...
28-297
1.60e-10
Feline leukemia virus subgroup C receptor-related protein 2 of the Major Facilitator Superfamily of transporters; Feline leukemia virus subgroup C receptor-related protein 2 (FLVCR2) is also called calcium-chelate transporter (CCT). It functions as a heme importer as well as a transporter for a calcium-chelator complex that is important for growth and calcium metabolism. Mutations in the FLVCR2 gene cause Proliferative vasculopathy and hydranencephaly-hydrocephaly syndrome (PVHH), also known as Fowler syndrome, a rare autosomal recessive disorder characterized by glomerular vasculopathy in the central nervous system, severe hydrocephaly, hypokinesia and arthrogryphosis. FLVCR2 belongs to the Solute carrier 49 (SLC49) 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: 341014 Cd Length: 406 Bit Score: 62.88 E-value: 1.60e-10
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
30-304
3.18e-08
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: 55.51 E-value: 3.18e-08
MFS-type transporter YcxA and similar proteins of the Major Facilitator Superfamily of ...
88-288
5.44e-03
MFS-type transporter YcxA and similar proteins of the Major Facilitator Superfamily of transporters; This group is composed of uncharacterized bacterial MFS-type transporters including Bacillus subtilis YcxA and YbfB. YcxA has been shown to facilitate the export of surfactin in B. subtilis. The YcxA-like group belongs to the Monocarboxylate transporter -like (MCT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340913 [Multi-domain] Cd Length: 386 Bit Score: 38.79 E-value: 5.44e-03
Rft1-like subfamily of the multidrug and toxic compound extrusion family (MATE); This ...
223-348
6.89e-03
Rft1-like subfamily of the multidrug and toxic compound extrusion family (MATE); This eukaryotic family may function as a transporter, shuttling phospholipids, lipopolysaccharides or oligosaccharides from cytoplasmic to the lumenal side of the endoplasmic reticulum. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. MATE has also been identified as a large multigene family in plants, where the proteins are linked to disease resistance.
Pssm-ID: 240535 Cd Length: 441 Bit Score: 38.86 E-value: 6.89e-03
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator ...
50-282
7.00e-03
Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily; This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. 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 NepI-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: 340882 [Multi-domain] Cd Length: 370 Bit Score: 38.68 E-value: 7.00e-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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