EXS (ERD1/XPR1/SYG1) family protein [Arabidopsis thaliana]
Protein Classification
SPX and EXS domain-containing protein( domain architecture ID 12041798)
SPX (Syg1, Pho81 and XPR1) and EXS (ERD1, XPR1, and SYG1) domain-containing protein similar to plant PHO1 family phosphate transporters
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| EXS | pfam03124 | EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family ... |
439-781 | 1.39e-107 | ||||||
EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family includes C-terminus portions from the SYG1 G-protein associated signal transduction protein from Saccharomyces cerevisiae, and sequences that are thought to be murine leukaemia virus (MLV) receptors (XPR1). N-terminus portions from these proteins are aligned in the SPX pfam03105 family. The previously noted similarity between SYG1 and MLV receptors over their whole sequences is thus borne out in pfam03105 and this family. While the N-termini aligned in pfam03105 are thought to be involved in signal transduction, the role of the C-terminus sequences aligned in this family is not known. This region of similarity contains several predicted transmembrane helices. This family also includes the ERD1 (ERD: ER retention defective) yeast proteins. ERD1 proteins are involved in the localization of endogenous endoplasmic reticulum (ER) proteins. erd1 null mutants secrete such proteins even though they possess the C-terminal HDEL ER lumen localization label sequence. In addition, null mutants also exhibit defects in the Golgi-dependent processing of several glycoproteins, which led to the suggestion that the sorting of luminal ER proteins actually occurs in the Golgi, with subsequent return of these proteins to the ER via `salvage' vesicles. : Pssm-ID: 460816 [Multi-domain] Cd Length: 331 Bit Score: 332.62 E-value: 1.39e-107
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| SPX | pfam03105 | SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ... |
1-350 | 4.04e-82 | ||||||
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: 266.35 E-value: 4.04e-82
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| Name | Accession | Description | Interval | E-value | ||||||
| EXS | pfam03124 | EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family ... |
439-781 | 1.39e-107 | ||||||
EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family includes C-terminus portions from the SYG1 G-protein associated signal transduction protein from Saccharomyces cerevisiae, and sequences that are thought to be murine leukaemia virus (MLV) receptors (XPR1). N-terminus portions from these proteins are aligned in the SPX pfam03105 family. The previously noted similarity between SYG1 and MLV receptors over their whole sequences is thus borne out in pfam03105 and this family. While the N-termini aligned in pfam03105 are thought to be involved in signal transduction, the role of the C-terminus sequences aligned in this family is not known. This region of similarity contains several predicted transmembrane helices. This family also includes the ERD1 (ERD: ER retention defective) yeast proteins. ERD1 proteins are involved in the localization of endogenous endoplasmic reticulum (ER) proteins. erd1 null mutants secrete such proteins even though they possess the C-terminal HDEL ER lumen localization label sequence. In addition, null mutants also exhibit defects in the Golgi-dependent processing of several glycoproteins, which led to the suggestion that the sorting of luminal ER proteins actually occurs in the Golgi, with subsequent return of these proteins to the ER via `salvage' vesicles. Pssm-ID: 460816 [Multi-domain] Cd Length: 331 Bit Score: 332.62 E-value: 1.39e-107
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| SPX | pfam03105 | SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ... |
1-350 | 4.04e-82 | ||||||
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: 266.35 E-value: 4.04e-82
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| SPX_PHO1_like | cd14476 | SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ... |
2-344 | 1.19e-52 | ||||||
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: 179.38 E-value: 1.19e-52
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| COG5409 | COG5409 | EXS domain-containing protein [Signal transduction mechanisms]; |
458-795 | 1.79e-31 | ||||||
EXS domain-containing protein [Signal transduction mechanisms]; Pssm-ID: 227696 Cd Length: 384 Bit Score: 127.22 E-value: 1.79e-31
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| COG5408 | COG5408 | SPX domain-containing protein [Signal transduction mechanisms]; |
1-354 | 4.18e-14 | ||||||
SPX domain-containing protein [Signal transduction mechanisms]; Pssm-ID: 227695 [Multi-domain] Cd Length: 296 Bit Score: 73.71 E-value: 4.18e-14
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| Name | Accession | Description | Interval | E-value | ||||||
| EXS | pfam03124 | EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family ... |
439-781 | 1.39e-107 | ||||||
EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family includes C-terminus portions from the SYG1 G-protein associated signal transduction protein from Saccharomyces cerevisiae, and sequences that are thought to be murine leukaemia virus (MLV) receptors (XPR1). N-terminus portions from these proteins are aligned in the SPX pfam03105 family. The previously noted similarity between SYG1 and MLV receptors over their whole sequences is thus borne out in pfam03105 and this family. While the N-termini aligned in pfam03105 are thought to be involved in signal transduction, the role of the C-terminus sequences aligned in this family is not known. This region of similarity contains several predicted transmembrane helices. This family also includes the ERD1 (ERD: ER retention defective) yeast proteins. ERD1 proteins are involved in the localization of endogenous endoplasmic reticulum (ER) proteins. erd1 null mutants secrete such proteins even though they possess the C-terminal HDEL ER lumen localization label sequence. In addition, null mutants also exhibit defects in the Golgi-dependent processing of several glycoproteins, which led to the suggestion that the sorting of luminal ER proteins actually occurs in the Golgi, with subsequent return of these proteins to the ER via `salvage' vesicles. Pssm-ID: 460816 [Multi-domain] Cd Length: 331 Bit Score: 332.62 E-value: 1.39e-107
|
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| SPX | pfam03105 | SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ... |
1-350 | 4.04e-82 | ||||||
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: 266.35 E-value: 4.04e-82
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| SPX_PHO1_like | cd14476 | SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ... |
2-344 | 1.19e-52 | ||||||
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: 179.38 E-value: 1.19e-52
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| COG5409 | COG5409 | EXS domain-containing protein [Signal transduction mechanisms]; |
458-795 | 1.79e-31 | ||||||
EXS domain-containing protein [Signal transduction mechanisms]; Pssm-ID: 227696 Cd Length: 384 Bit Score: 127.22 E-value: 1.79e-31
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| COG5408 | COG5408 | SPX domain-containing protein [Signal transduction mechanisms]; |
1-354 | 4.18e-14 | ||||||
SPX domain-containing protein [Signal transduction mechanisms]; Pssm-ID: 227695 [Multi-domain] Cd Length: 296 Bit Score: 73.71 E-value: 4.18e-14
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| SPX_SYG1_like | cd14475 | SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ... |
301-336 | 9.11e-10 | ||||||
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: 57.57 E-value: 9.11e-10
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| SPX | cd14447 | Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ... |
2-167 | 1.69e-07 | ||||||
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: 51.03 E-value: 1.69e-07
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| SPX_XPR1_like | cd14477 | SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ... |
301-336 | 5.30e-07 | ||||||
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: 49.98 E-value: 5.30e-07
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| SPX | cd14447 | Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ... |
292-336 | 9.98e-07 | ||||||
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: 49.10 E-value: 9.98e-07
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| SPX_VTC2_like | cd14480 | SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ... |
2-31 | 2.10e-04 | ||||||
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: 42.14 E-value: 2.10e-04
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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, ... |
2-38 | 2.80e-04 | ||||||
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: 41.75 E-value: 2.80e-04
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| SPX_PHO87_PHO90_like | cd14478 | SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ... |
306-336 | 3.18e-04 | ||||||
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: 41.75 E-value: 3.18e-04
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| SPX_SYG1_like | cd14475 | SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ... |
2-30 | 3.27e-04 | ||||||
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: 41.40 E-value: 3.27e-04
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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 ... |
307-336 | 8.65e-04 | ||||||
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: 40.33 E-value: 8.65e-04
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| SPX_XPR1_like | cd14477 | SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ... |
2-31 | 1.09e-03 | ||||||
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: 40.35 E-value: 1.09e-03
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| SPX_BAH1-like | cd14482 | SPX domain of the E3 ubiquitin-protein ligase BAH1/NLA and similar proteins; This region has ... |
311-339 | 6.81e-03 | ||||||
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: 38.10 E-value: 6.81e-03
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