Major Facilitator Superfamily with SPX (SYG1/Pho81/XPR1) domain-containing protein [Arabidopsis thaliana]
SPX domain-containing membrane protein( domain architecture ID 12997668)
SPX domain-containing membrane protein with a major facilitator superfamily (MFS) transporter domain may function in phosphate homeostasis and in the transport across cytoplasmic or internal membranes various substrates including sugar phosphates
List of domain hits
Name | Accession | Description | Interval | E-value | |||||||
SPX-MFS_plant | cd14479 | SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ... |
2-141 | 1.03e-84 | |||||||
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The SPX domain is found at the amino terminus of a variety of proteins. This family, mostly found in plants, contains a C-terminal MFS domain (major facilitator superfamily), suggesting a function as a secondary transporter. The function of this N-terminal region is unclear, although it might be involved in regulating transport. : Pssm-ID: 269900 [Multi-domain] Cd Length: 140 Bit Score: 262.99 E-value: 1.03e-84
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MFS super family | cl28910 | Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ... |
249-657 | 7.05e-23 | |||||||
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 cd17326: Pssm-ID: 475125 [Multi-domain] Cd Length: 374 Bit Score: 101.13 E-value: 7.05e-23
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Name | Accession | Description | Interval | E-value | |||||||
SPX-MFS_plant | cd14479 | SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ... |
2-141 | 1.03e-84 | |||||||
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The SPX domain is found at the amino terminus of a variety of proteins. This family, mostly found in plants, contains a C-terminal MFS domain (major facilitator superfamily), suggesting a function as a secondary transporter. The function of this N-terminal region is unclear, although it might be involved in regulating transport. Pssm-ID: 269900 [Multi-domain] Cd Length: 140 Bit Score: 262.99 E-value: 1.03e-84
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MFS_MFSD8 | cd17326 | Major facilitator superfamily domain-containing protein 8; Major facilitator superfamily (MFS) ... |
249-657 | 7.05e-23 | |||||||
Major facilitator superfamily domain-containing protein 8; Major facilitator superfamily (MFS) domain-containing protein 8 (MFSD8) is also called ceroid-lipofuscinosis neuronal protein 7 (CLN7). It is a polytopic lysosomal membrane protein that may transport small solutes by using chemiosmotic ion gradients. Mutations in MFSD8/CLN7 cause a variant of late-infantile neuronal ceroid lipofuscinoses (vLINCL), a neurodegenerative lysosomal storage disorder. Some variants are associated with nonsyndromic autosomal recessive macular dystrophy. MFSD8/CLN7 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance -like (SLC46/TetA-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: 340884 [Multi-domain] Cd Length: 374 Bit Score: 101.13 E-value: 7.05e-23
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AraJ | COG2814 | Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; |
249-646 | 1.38e-13 | |||||||
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; Pssm-ID: 442063 [Multi-domain] Cd Length: 348 Bit Score: 72.70 E-value: 1.38e-13
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MFS_1 | pfam07690 | Major Facilitator Superfamily; |
257-642 | 6.55e-10 | |||||||
Major Facilitator Superfamily; Pssm-ID: 429598 [Multi-domain] Cd Length: 344 Bit Score: 61.28 E-value: 6.55e-10
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SPX | pfam03105 | SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ... |
108-147 | 1.70e-08 | |||||||
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 residue long domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all the members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors PHO81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2 NUC-2 contains several ankyrin repeats pfam00023. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with murine xenotropic and polytropic leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signalling and result in cell toxicity and death. The similarity between SYG1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organizms. In addition, given the similarities between XPR1 and SYG1 and phosphate regulatory proteins, it has been proposed that XPR1 might be involved in G-protein associated signal transduction and may itself function as a phosphate sensor. Pssm-ID: 460807 [Multi-domain] Cd Length: 339 Bit Score: 56.80 E-value: 1.70e-08
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COG5408 | COG5408 | SPX domain-containing protein [Signal transduction mechanisms]; |
109-152 | 1.13e-03 | |||||||
SPX domain-containing protein [Signal transduction mechanisms]; Pssm-ID: 227695 [Multi-domain] Cd Length: 296 Bit Score: 41.74 E-value: 1.13e-03
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Name | Accession | Description | Interval | E-value | |||||||
SPX-MFS_plant | cd14479 | SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ... |
2-141 | 1.03e-84 | |||||||
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The SPX domain is found at the amino terminus of a variety of proteins. This family, mostly found in plants, contains a C-terminal MFS domain (major facilitator superfamily), suggesting a function as a secondary transporter. The function of this N-terminal region is unclear, although it might be involved in regulating transport. Pssm-ID: 269900 [Multi-domain] Cd Length: 140 Bit Score: 262.99 E-value: 1.03e-84
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SPX | cd14447 | Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ... |
4-133 | 2.36e-27 | |||||||
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). This domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. NUC-2 contains several ankyrin repeats. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with xenotropic and polytropic murine leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signaling and result in cell toxicity and death. The similarity between Syg1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, S. cerevisiae, and many other diverse organisms. Pssm-ID: 269894 [Multi-domain] Cd Length: 143 Bit Score: 108.04 E-value: 2.36e-27
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MFS_MFSD8 | cd17326 | Major facilitator superfamily domain-containing protein 8; Major facilitator superfamily (MFS) ... |
249-657 | 7.05e-23 | |||||||
Major facilitator superfamily domain-containing protein 8; Major facilitator superfamily (MFS) domain-containing protein 8 (MFSD8) is also called ceroid-lipofuscinosis neuronal protein 7 (CLN7). It is a polytopic lysosomal membrane protein that may transport small solutes by using chemiosmotic ion gradients. Mutations in MFSD8/CLN7 cause a variant of late-infantile neuronal ceroid lipofuscinoses (vLINCL), a neurodegenerative lysosomal storage disorder. Some variants are associated with nonsyndromic autosomal recessive macular dystrophy. MFSD8/CLN7 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance -like (SLC46/TetA-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: 340884 [Multi-domain] Cd Length: 374 Bit Score: 101.13 E-value: 7.05e-23
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SPX_PHO81_NUC-2_like | cd14483 | SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ... |
4-134 | 4.34e-21 | |||||||
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. NUC-2 plays an important role in the phosphate-regulated signal transduction pathway in N. crassa. It shows high similarity to a cyclin-dependent kinase inhibitory protein Pho81, which is part of the phosphate regulatory cascade in S. cerevisiae. Both, NUC-2 and Pho81, have multi-domain architecture, including the SPX N-terminal domain following by several ankyrin repeats and a putative C-terminal glycerophosphodiester phosphodiesterase domain (GDPD) with unknown function. Pssm-ID: 269904 [Multi-domain] Cd Length: 162 Bit Score: 90.39 E-value: 4.34e-21
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SPX_GDE1_like | cd14484 | SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ... |
4-136 | 3.75e-20 | |||||||
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The yeast protein Gde1/Ypl110c is similar to both, NUC-2 and Pho81, in sharing their multi-domain architecture, which includes the SPX N-terminal domain followed by several ankyrin repeats and a C-terminal glycerophosphodiester phosphodiesterase domain (GDPD). Gde1 hydrolyzes intracellular glycerophosphocholine into glycerolphosphate and choline, and plays a role in the utilization of glycerophosphocholine as a source for phosphate. Pssm-ID: 269905 [Multi-domain] Cd Length: 134 Bit Score: 86.82 E-value: 3.75e-20
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SPX_SYG1_like | cd14475 | SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ... |
4-133 | 8.41e-15 | |||||||
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus binds directly to the G-protein beta subunit and inhibits transduction of the mating pheromone signal, and it co-occurs with a C-terminal domain from the EXS family. Pssm-ID: 269896 [Multi-domain] Cd Length: 139 Bit Score: 71.83 E-value: 8.41e-15
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AraJ | COG2814 | Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; |
249-646 | 1.38e-13 | |||||||
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; Pssm-ID: 442063 [Multi-domain] Cd Length: 348 Bit Score: 72.70 E-value: 1.38e-13
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MFS_MdtG_SLC18_like | cd17325 | bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ... |
257-461 | 3.93e-13 | |||||||
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: 71.45 E-value: 3.93e-13
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MFS_SLC46_TetA_like | cd17330 | Eukaryotic Solute carrier 46 (SLC46) family, Bacterial Tetracycline resistance proteins, and ... |
258-663 | 4.43e-12 | |||||||
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: 67.99 E-value: 4.43e-12
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SPX_VTC2_like | cd14480 | SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ... |
4-133 | 3.33e-11 | |||||||
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. Vtc2 is part of the Saccharomyces cerevisiae membrane-integral VTC complex, together with Vtc1, Vtc3, and Vtc4. It contains an N-terminal SPX domain next to a central polyphosphate polymerase domain and a C-terminal domain of unknown function. Pssm-ID: 269901 [Multi-domain] Cd Length: 135 Bit Score: 61.40 E-value: 3.33e-11
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SPX_AtSPX1_like | cd14481 | SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ... |
4-134 | 3.83e-11 | |||||||
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. This family of plant proteins contains a single SPX domain. Arabidopsis thaliana SPX1 and SPX3 have been reported to play roles in the adaptation to low-phosphate conditions, SPX3 may be involved in the regulation of SPX1 activity. Oryza sativa SPX1 suppresses the regulation of expression of OsPT2, a low-affinity phosphate transporter, by the MYB-like OsPHR2. Pssm-ID: 269902 [Multi-domain] Cd Length: 149 Bit Score: 61.52 E-value: 3.83e-11
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MFS_1 | pfam07690 | Major Facilitator Superfamily; |
257-642 | 6.55e-10 | |||||||
Major Facilitator Superfamily; Pssm-ID: 429598 [Multi-domain] Cd Length: 344 Bit Score: 61.28 E-value: 6.55e-10
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SPX_YDR089W | cd14474 | SPX domain of the yeast protein YDR089W and related proteins; This region has been named the ... |
4-133 | 1.03e-09 | |||||||
SPX domain of the yeast protein YDR089W and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The uncharacterized yeast protein YDR089W has not been shown to be involved in phosphate homeostasis, in contrast to most of the other SPX-domain containing proteins. Pssm-ID: 269895 [Multi-domain] Cd Length: 144 Bit Score: 57.24 E-value: 1.03e-09
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SPX_PHO87_PHO90_like | cd14478 | SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ... |
15-133 | 1.93e-09 | |||||||
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The SPX domain of the Saccharomyces cerevisiae membrane-localized low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. Pho91 is involved in the export of inorganic phosphate from the vacuole to the cytosol. While both, Pho87 and Pho90, transport phosphate into the cell, only Pho87 appears to also function as a sensor for high extracellular phosphate concentrations. Pssm-ID: 269899 [Multi-domain] Cd Length: 148 Bit Score: 56.78 E-value: 1.93e-09
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SPX | pfam03105 | SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ... |
108-147 | 1.70e-08 | |||||||
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 residue long domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all the members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors PHO81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2 NUC-2 contains several ankyrin repeats pfam00023. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with murine xenotropic and polytropic leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signalling and result in cell toxicity and death. The similarity between SYG1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organizms. In addition, given the similarities between XPR1 and SYG1 and phosphate regulatory proteins, it has been proposed that XPR1 might be involved in G-protein associated signal transduction and may itself function as a phosphate sensor. Pssm-ID: 460807 [Multi-domain] Cd Length: 339 Bit Score: 56.80 E-value: 1.70e-08
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MFS_YfcJ_like | cd17489 | Escherichia coli YfcJ, YhhS, and similar transporters of the Major Facilitator Superfamily; ... |
252-396 | 2.15e-08 | |||||||
Escherichia coli YfcJ, YhhS, and similar transporters of the Major Facilitator Superfamily; This subfamily is composed of Escherichia coli membrane proteins, YfcJ and YhhS, Bacillus subtilis uncharacterized MFS-type transporter YwoG, and similar proteins. YfcJ and YhhS are putative arabinose efflux transporters. YhhS has been implicated glyphosate resistance. YfcJ-like arabinose efflux transporters belong to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) 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: 341042 [Multi-domain] Cd Length: 367 Bit Score: 56.83 E-value: 2.15e-08
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MFS_MdtG_SLC18_like | cd17325 | bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ... |
249-395 | 5.28e-08 | |||||||
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: 55.66 E-value: 5.28e-08
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MFS_MdtH_MDR_like | cd17329 | Multidrug resistance protein MdtH and similar multidrug resistance (MDR) transporters of the ... |
246-433 | 1.27e-07 | |||||||
Multidrug resistance protein MdtH and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of Escherichia coli MdtH and similar multidrug resistance (MDR) transporters from bacteria and archaea, many of which remain uncharacterized. 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. MdtH confers resistance to norfloxacin and enoxacin. MdtH-like MDR transporters belong 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: 340887 [Multi-domain] Cd Length: 376 Bit Score: 54.54 E-value: 1.27e-07
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MFS_MFSD9 | cd17390 | Major facilitator superfamily domain-containing protein 9; Major facilitator superfamily ... |
266-431 | 3.57e-07 | |||||||
Major facilitator superfamily domain-containing protein 9; Major facilitator superfamily domain-containing protein 9 (MFSD9) is expressed in the central nervous system (CNS) and in most peripheral tissues but at very low expression levels. The function of MFSD9 is unknown. MFSD9 belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-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: 340948 [Multi-domain] Cd Length: 350 Bit Score: 53.00 E-value: 3.57e-07
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ProP | COG0477 | MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and ... |
257-395 | 1.72e-06 | |||||||
MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and metabolism, Amino acid transport and metabolism, Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 440245 [Multi-domain] Cd Length: 295 Bit Score: 50.19 E-value: 1.72e-06
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MFS_NepI_like | cd17324 | Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator ... |
257-395 | 2.11e-06 | |||||||
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: 50.63 E-value: 2.11e-06
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MFS_YajR_like | cd17472 | Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux ... |
258-402 | 2.85e-06 | |||||||
Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux transporters of the Major Facilitator Superfamily; This family is composed of Escherichia coli inner membrane transport protein YajR and some uncharacterized multidrug-efflux transporters. YajR is a putative proton-driven major facilitator superfamily (MFS) transporter found in many gram-negative bacteria. Unlike most MFS transporters, YajR contains a C-terminal, cytosolic YAM domain, which may play an essential role for the proper functioning of the transporter. YajR-like transporters belong 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: 341025 [Multi-domain] Cd Length: 371 Bit Score: 49.91 E-value: 2.85e-06
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MFS_TetA | cd17388 | Tetracycline resistance protein TetA and related proteins of the Major Facilitator Superfamily ... |
267-594 | 3.73e-06 | |||||||
Tetracycline resistance protein TetA and related proteins of the Major Facilitator Superfamily of transporters; This subfamily is composed of tetracycline resistance proteins similar to Escherichia coli TetA(A), TetA(B), and TetA(E), which are metal-tetracycline/H(+) antiporters that confer resistance to tetracycline by an active tetracycline efflux, which is an energy-dependent process that decreases the accumulation of the antibiotic in cells. TetA-like tetracycline resistance proteins belongs to the Eukaryotic Solute carrier 46 (SLC46)/Bacterial Tetracycline resistance (TetA) -like (SLC46/TetA-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: 340946 [Multi-domain] Cd Length: 385 Bit Score: 49.94 E-value: 3.73e-06
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SPX_PHO1_like | cd14476 | SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ... |
4-133 | 4.93e-06 | |||||||
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The PHO1 gene family conserved in plants is involved in a variety of processes, most notably the transport of inorganic phosphate from the root to the shoot of the plant and mediating the response to low levels of inorganic phosphate. More recently it has become evident that PHO1 gene families have diverged in various plants and may play roles in stress response as well as the stomatal response to abscisic acid. Pssm-ID: 269897 [Multi-domain] Cd Length: 139 Bit Score: 46.48 E-value: 4.93e-06
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SPX | pfam03105 | SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ... |
4-46 | 9.03e-06 | |||||||
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 residue long domain is found at the amino terminus of a variety of proteins. In the yeast protein SYG1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all the members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors PHO81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2 NUC-2 contains several ankyrin repeats pfam00023. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with murine xenotropic and polytropic leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signalling and result in cell toxicity and death. The similarity between SYG1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organizms. In addition, given the similarities between XPR1 and SYG1 and phosphate regulatory proteins, it has been proposed that XPR1 might be involved in G-protein associated signal transduction and may itself function as a phosphate sensor. Pssm-ID: 460807 [Multi-domain] Cd Length: 339 Bit Score: 48.33 E-value: 9.03e-06
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Sugar_tr | pfam00083 | Sugar (and other) transporter; |
260-351 | 7.17e-05 | |||||||
Sugar (and other) transporter; Pssm-ID: 395036 [Multi-domain] Cd Length: 452 Bit Score: 45.73 E-value: 7.17e-05
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UhpC | COG2271 | Sugar phosphate permease [Carbohydrate transport and metabolism]; |
250-431 | 8.22e-05 | |||||||
Sugar phosphate permease [Carbohydrate transport and metabolism]; Pssm-ID: 441872 [Multi-domain] Cd Length: 363 Bit Score: 45.25 E-value: 8.22e-05
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MFS | cd06174 | Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ... |
258-442 | 9.14e-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: 45.50 E-value: 9.14e-05
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MFS_NepI_like | cd17324 | Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator ... |
279-395 | 1.77e-04 | |||||||
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: 44.46 E-value: 1.77e-04
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MFS | cd06174 | Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ... |
254-425 | 2.77e-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: 43.95 E-value: 2.77e-04
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SPX_XPR1_like | cd14477 | SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ... |
4-133 | 2.90e-04 | |||||||
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-terminus of the human XPR1 protein (xenotropic and polytropic retrovirus receptor 1) binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that all members of this family are involved in G-protein associated signal transduction. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with xenotropic and polytropic murine leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signaling and result in cell toxicity and death. Similarity between Syg1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, and Saccharomyces cerevisiae, and many other diverse organisms. Pssm-ID: 269898 [Multi-domain] Cd Length: 161 Bit Score: 41.89 E-value: 2.90e-04
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SPX_BAH1-like | cd14482 | SPX domain of the E3 ubiquitin-protein ligase BAH1/NLA and similar proteins; This region has ... |
79-133 | 9.91e-04 | |||||||
SPX domain of the E3 ubiquitin-protein ligase BAH1/NLA and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. BAH1 (benzoic acid hypersensitive 1) appears to function as an E3 ubiquitin ligase; the protein contains an SPX and a RING finger domain. It has been suggested that BAH1/NLA is involved in the regulation of plant immune responses, probably via a pathway of salicylic acid biosynthesis that includes benzoic acid as an intermediate. Pssm-ID: 269903 Cd Length: 156 Bit Score: 40.41 E-value: 9.91e-04
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COG5408 | COG5408 | SPX domain-containing protein [Signal transduction mechanisms]; |
109-152 | 1.13e-03 | |||||||
SPX domain-containing protein [Signal transduction mechanisms]; Pssm-ID: 227695 [Multi-domain] Cd Length: 296 Bit Score: 41.74 E-value: 1.13e-03
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AraJ | COG2814 | Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; |
254-386 | 1.19e-03 | |||||||
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism]; Pssm-ID: 442063 [Multi-domain] Cd Length: 348 Bit Score: 41.88 E-value: 1.19e-03
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MFS_arabinose_efflux_permease_like | cd17473 | Putative arabinose efflux permease family transporters of the Major Facilitator Superfamily; ... |
249-427 | 1.32e-03 | |||||||
Putative arabinose efflux permease family transporters of the Major Facilitator Superfamily; This family includes a group of putative arabinose efflux permease family transporters, such as alpha proteobacterium quinolone resistance protein NorA (characterized Staphylococcus aureus Quinolone resistance protein NorA belongs to a different group), Desulfovibrio dechloracetivorans bacillibactin exporter, Vibrio aerogenes antiseptic resistance protein. The biological function of those transporters remain unclear. They belong 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: 341026 [Multi-domain] Cd Length: 374 Bit Score: 41.79 E-value: 1.32e-03
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MFS_GLUT_like | cd17315 | Glucose transporters (GLUTs) and other similar sugar transporters of the Major Facilitator ... |
254-422 | 2.36e-03 | |||||||
Glucose transporters (GLUTs) and other similar sugar transporters of the Major Facilitator Superfamily; This family is composed of glucose transporters (GLUTs) and other sugar transporters including fungal hexose transporters (HXT), bacterial xylose transporter (XylE), plant sugar transport proteins (STP) and polyol transporters (PLT), H(+)-myo-inositol cotransporter (HMIT), and similar proteins. GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. The GLUT-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: 340873 [Multi-domain] Cd Length: 365 Bit Score: 40.64 E-value: 2.36e-03
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MFS_YfcJ_like | cd17489 | Escherichia coli YfcJ, YhhS, and similar transporters of the Major Facilitator Superfamily; ... |
274-395 | 4.73e-03 | |||||||
Escherichia coli YfcJ, YhhS, and similar transporters of the Major Facilitator Superfamily; This subfamily is composed of Escherichia coli membrane proteins, YfcJ and YhhS, Bacillus subtilis uncharacterized MFS-type transporter YwoG, and similar proteins. YfcJ and YhhS are putative arabinose efflux transporters. YhhS has been implicated glyphosate resistance. YfcJ-like arabinose efflux transporters belong to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) 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: 341042 [Multi-domain] Cd Length: 367 Bit Score: 39.88 E-value: 4.73e-03
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MFS_Set | cd17471 | Sugar efflux transporter (Set) family of the Major Facilitator Superfamily of transporters; ... |
278-432 | 4.80e-03 | |||||||
Sugar efflux transporter (Set) family of the Major Facilitator Superfamily of transporters; This family is composed of sugar transporters such as Escherichia coli Sugar efflux transporter SetA, SetB, SetC and other sugar transporters. SetA, SetB, and SetC are involved in the efflux of sugars such as lactose, glucose, IPTG, and substituted glucosides or galactosides. They may be involved in the detoxification of non-metabolizable sugar analogs. The Set 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: 341024 [Multi-domain] Cd Length: 371 Bit Score: 39.84 E-value: 4.80e-03
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UhpC | COG2271 | Sugar phosphate permease [Carbohydrate transport and metabolism]; |
247-395 | 7.62e-03 | |||||||
Sugar phosphate permease [Carbohydrate transport and metabolism]; Pssm-ID: 441872 [Multi-domain] Cd Length: 363 Bit Score: 39.08 E-value: 7.62e-03
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MelB | COG2211 | Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; |
250-425 | 8.08e-03 | |||||||
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; Pssm-ID: 441813 [Multi-domain] Cd Length: 447 Bit Score: 39.12 E-value: 8.08e-03
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CynX | COG2807 | Cyanate permease [Inorganic ion transport and metabolism]; |
254-427 | 1.00e-02 | |||||||
Cyanate permease [Inorganic ion transport and metabolism]; Pssm-ID: 442057 [Multi-domain] Cd Length: 399 Bit Score: 38.70 E-value: 1.00e-02
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Blast search parameters | ||||
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