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Conserved domains on  [gi|42563076|ref|NP_177107|]
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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

Graphical summary

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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 ...
413-749 2.33e-113

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: 346.88  E-value: 2.33e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   413 IIPLYSLFGFIILHMLMYSANIYFWKRYRVNYTFIFGFKQGTELGDREVFLVSTGLAVLAFVCFLLNLQLDMDwrmkhhk 492
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLLFWV------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   493 TLPEVIPLCLATIVLFILFCPFNIIYRSSRFFFIRSLFHCICAPLYEVTLPDFFLGDHLTSQIQAIRSFELFICYYGLGe 572
Cdd:pfam03124  74 DPLEYIPLLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYASG- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   573 YLQRQNKCHSHGVYnaFYFVVAVIPYWLRFLQCIRRLCEEKE-SVHGYNALKYMLTIIAVIVRTAYELKKG--RTWMILA 649
Cdd:pfam03124 153 WSGGDNQCGSSSRG--LVPLLAALPYLIRFLQCLRRYRDTGDwFPHLLNALKYSTAIPVIILSALYRIYKSdeNPLFVLW 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   650 LVSSGVATGMNTFWDIVIDWGLLRK-HSKNPYLRDKLLVPHKSVYFAAMVVNVILRVAWMQLVLEFNLKSLHKIAVTSII 728
Cdd:pfam03124 231 ILFAVINSLYSFYWDVKMDWGLLQLfKNKNWFLRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHLHSFQHSELGIFLL 310
                         330       340
                  ....*....|....*....|.
gi 42563076   729 SCLEIIRRGIWSFFRLENEHL 749
Cdd:pfam03124 311 ALLEVFRRFIWNFFRVENEHL 331
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-324 1.58e-59

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: 205.10  E-value: 1.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076     1 MKFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSYKHSK---------------------LTRAASRVSQQAEALHRSFS 59
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRELESTppssspsssdsgsaaspsdstTSLPLRDPLSRSSSLDRAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076    60 GLSFHPRHSERAGDIEDQvikvDTVQEEGSRKLYETKFLKKSEEGGEFEESFF------------KKLDENLNKVNKFYR 127
Cdd:pfam03105  81 GLVPSPPSSSSSSSSDSS----SSSNSSSSSSSSSPSLLRRLPSESDDSSESYettpldsedeffERLDSELNKVNKFYK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   128 DKVKEVIEEAALLDKQMDALIALRVKMQKPDVDNLNLEKHPSDkvvvDTSDNTMRTQGTANTDMVHGIERTNIPEEEASh 207
Cdd:pfam03105 157 EKEEEFLERLEALNKQLEALRDFRIKLIRESKSDLYRWREPFG----LYSSDSSVFFSTSELDSGNSSESSVDDEVEEE- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   208 imadivpvSHTNGDEEEASIGDKQDLR-EILERVKmndvleSPITTLKGVFGDSNE----PISKKGLKKGEEQLRLVFSE 282
Cdd:pfam03105 232 --------LERNGWISPIKSKDKKKRPsEALDKVK------TPDRTLKGFLDASRRdylnRINKVNLRKAKKKLKKAFIE 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 42563076   283 FYQKLRRLKEYSFMNLLAFSKIMKKYEKIASRNASRNYMKIV 324
Cdd:pfam03105 298 LYRGLELLKSYSELNRTAFRKILKKFDKVTSLNASKDYMKEV 339
 
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 ...
413-749 2.33e-113

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: 346.88  E-value: 2.33e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   413 IIPLYSLFGFIILHMLMYSANIYFWKRYRVNYTFIFGFKQGTELGDREVFLVSTGLAVLAFVCFLLNLQLDMDwrmkhhk 492
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLLFWV------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   493 TLPEVIPLCLATIVLFILFCPFNIIYRSSRFFFIRSLFHCICAPLYEVTLPDFFLGDHLTSQIQAIRSFELFICYYGLGe 572
Cdd:pfam03124  74 DPLEYIPLLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYASG- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   573 YLQRQNKCHSHGVYnaFYFVVAVIPYWLRFLQCIRRLCEEKE-SVHGYNALKYMLTIIAVIVRTAYELKKG--RTWMILA 649
Cdd:pfam03124 153 WSGGDNQCGSSSRG--LVPLLAALPYLIRFLQCLRRYRDTGDwFPHLLNALKYSTAIPVIILSALYRIYKSdeNPLFVLW 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   650 LVSSGVATGMNTFWDIVIDWGLLRK-HSKNPYLRDKLLVPHKSVYFAAMVVNVILRVAWMQLVLEFNLKSLHKIAVTSII 728
Cdd:pfam03124 231 ILFAVINSLYSFYWDVKMDWGLLQLfKNKNWFLRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHLHSFQHSELGIFLL 310
                         330       340
                  ....*....|....*....|.
gi 42563076   729 SCLEIIRRGIWSFFRLENEHL 749
Cdd:pfam03124 311 ALLEVFRRFIWNFFRVENEHL 331
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-324 1.58e-59

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: 205.10  E-value: 1.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076     1 MKFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSYKHSK---------------------LTRAASRVSQQAEALHRSFS 59
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRELESTppssspsssdsgsaaspsdstTSLPLRDPLSRSSSLDRAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076    60 GLSFHPRHSERAGDIEDQvikvDTVQEEGSRKLYETKFLKKSEEGGEFEESFF------------KKLDENLNKVNKFYR 127
Cdd:pfam03105  81 GLVPSPPSSSSSSSSDSS----SSSNSSSSSSSSSPSLLRRLPSESDDSSESYettpldsedeffERLDSELNKVNKFYK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   128 DKVKEVIEEAALLDKQMDALIALRVKMQKPDVDNLNLEKHPSDkvvvDTSDNTMRTQGTANTDMVHGIERTNIPEEEASh 207
Cdd:pfam03105 157 EKEEEFLERLEALNKQLEALRDFRIKLIRESKSDLYRWREPFG----LYSSDSSVFFSTSELDSGNSSESSVDDEVEEE- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   208 imadivpvSHTNGDEEEASIGDKQDLR-EILERVKmndvleSPITTLKGVFGDSNE----PISKKGLKKGEEQLRLVFSE 282
Cdd:pfam03105 232 --------LERNGWISPIKSKDKKKRPsEALDKVK------TPDRTLKGFLDASRRdylnRINKVNLRKAKKKLKKAFIE 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 42563076   283 FYQKLRRLKEYSFMNLLAFSKIMKKYEKIASRNASRNYMKIV 324
Cdd:pfam03105 298 LYRGLELLKSYSELNRTAFRKILKKFDKVTSLNASKDYMKEV 339
COG5409 COG5409
EXS domain-containing protein [Signal transduction mechanisms];
414-762 1.90e-40

EXS domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227696  Cd Length: 384  Bit Score: 153.03  E-value: 1.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 414 IPLYSLFGFIILHMLMYSANI--YFWKRYRVNYTFIFGFKQGTELG-----DREVFLVSTGLAVLAFVCFLLNLQLDMDW 486
Cdd:COG5409  35 ILLALWGGWILVFFLAFLFDVscYILTRTPINYRFIFLFEQLSSTArnfnlDFHRIIIPFHFFTTSLFIFLNAVEGLKFI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 487 RMKHHktlpeVIPLCLATIVLFILFCPFNIIYRSSRFFFIRSLFHCICAPLYEVTLPDFFLGDHLTSQIQAIRSFELFIC 566
Cdd:COG5409 115 LLFVY-----FLPLLQVGTVFWFLLKPFQIIYYWSRRYLIESLIRVFLFGYSLVRFTDFFFGDILISLTYALGDIYIFFC 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 567 YYGLgeyLQRQNKCHSHGVYnaFYFVVAVIPYWLRFLQCIRR-LCEEKESVHGYNALKYMLTIIAVIVRTAYELKKGRTW 645
Cdd:COG5409 190 VYSL---LFREPLCKSSHSD--LSGLAALLPVIVRFLQCLRRyRDSLHEFPHLLNALKYSLNIPVLFCLWLYRVYEGEER 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 646 M-ILALVSSGVATGMNTFWDIVIDWGLLR-KHSKNPYLRDKLLVPhksvYFAAMVVNVILRVAWMQLVLEFNLKSLHKIA 723
Cdd:COG5409 265 LfHLQIWFALLNSIYTSFWDVFMDWSLDSlTSLRSWSKRAVTLLK----YHIAMIINFLLRFSWIVYYLPPNHIQHSADI 340
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 42563076 724 VTSIISCLEIIRRGIWSFFRLENEHLNNVGKYRAFKSVP 762
Cdd:COG5409 341 FIFIMQLLEILRRFVWVFFRVEAEHSINFASFRAAGELK 379
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
2-318 2.07e-39

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: 142.01  E-value: 2.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   2 KFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSYKHSkltraasrvsqqaealhrsfsglsfhprhseragdiedqvikv 81
Cdd:cd14476   1 KFGKEFESQMVPEWQEAYVDYKQLKKDLKRIQKFRDE------------------------------------------- 37
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076  82 dtvqeegsrklYETKFLKKSEEGGEFEESFFKKLDENLNKVNKFYRDKVKEVIEEAALLDKQMDALIALRVKMQKPDvdn 161
Cdd:cd14476  38 -----------YETTFLEAAEEGGEYELVFFRRLDDELNKVNKFYRSKVEEVLKEAAALNKQMDALIAFRVKVENPQ--- 103
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 162 lnlekhpsdkvvvdtsdntmrtqgtantdmvhgiertnipeeeashimadivpvshtngdeeeasigdkqdlreilervk 241
Cdd:cd14476     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563076 242 mndvlespittlkgvfgdsnepiskkglkkgeeqlrlvfseFYQKLRRLKEYSFMNLLAFSKIMKKYEKIASRNASR 318
Cdd:cd14476 104 -----------------------------------------FYRKLRLLKSYSFLNMLAFSKILKKYDKVTSRNASK 139
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-326 4.29e-10

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 61.77  E-value: 4.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   1 MKFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSyKHSKLTRAASRVSQQAEALHRSFSG--LSFHPRHSERAGDIEDQV 78
Cdd:COG5408   1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQK-DQLSSYHGVSDNDETRDEAGEPSNWrdRFNHALKKELSPLQANYV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076  79 ------------IKVDTVQEEGSRKLYETKFLKKSEEGGEFEES------FFKKLDENLNKVNKFYRDkvkevieeaall 140
Cdd:COG5408  80 akffenyiseeaIKLDEFYSQGQYIAYKKREFRKISSKFFYSERkalvqkEENTASSNYDTFLNLQTD------------ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 141 dkQMDALIALRVKMQKPDVdnlnlekHPSDKVVVDTSDNTMRTQGTANTDMVHGIERTNipeeeashimaDIVPVSHTNG 220
Cdd:COG5408 148 --EGAYVADARKRAEAKSY-------DPFDSLRIDTSKEGLTKRNLNLPDYEKIVSGTD-----------EEVPSNDQDD 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 221 -DEEEASIGDKQDlREILERvkmndvLESPITTLKGVFgdsnepiSKKGLKKgeeqlRLVfsEFYQKLRRLKEYSFMNLL 299
Cdd:COG5408 208 eDQDFDYLAKKND-NTALLD------LSQFNFKIVKYQ-------KRSLLKK-----RII--ELYIQLHQLKSFIELNYT 266
                       330       340
                ....*....|....*....|....*..
gi 42563076 300 AFSKIMKKYEKIASRNASRNYMKIVDN 326
Cdd:COG5408 267 GFSKITKKYDKTLHQNLRHEYMSRSVN 293
 
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 ...
413-749 2.33e-113

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: 346.88  E-value: 2.33e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   413 IIPLYSLFGFIILHMLMYSANIYFWKRYRVNYTFIFGFKQGTELGDREVFLVSTGLAVLAFVCFLLNLQLDMDwrmkhhk 492
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLLFWV------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   493 TLPEVIPLCLATIVLFILFCPFNIIYRSSRFFFIRSLFHCICAPLYEVTLPDFFLGDHLTSQIQAIRSFELFICYYGLGe 572
Cdd:pfam03124  74 DPLEYIPLLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYASG- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   573 YLQRQNKCHSHGVYnaFYFVVAVIPYWLRFLQCIRRLCEEKE-SVHGYNALKYMLTIIAVIVRTAYELKKG--RTWMILA 649
Cdd:pfam03124 153 WSGGDNQCGSSSRG--LVPLLAALPYLIRFLQCLRRYRDTGDwFPHLLNALKYSTAIPVIILSALYRIYKSdeNPLFVLW 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   650 LVSSGVATGMNTFWDIVIDWGLLRK-HSKNPYLRDKLLVPHKSVYFAAMVVNVILRVAWMQLVLEFNLKSLHKIAVTSII 728
Cdd:pfam03124 231 ILFAVINSLYSFYWDVKMDWGLLQLfKNKNWFLRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHLHSFQHSELGIFLL 310
                         330       340
                  ....*....|....*....|.
gi 42563076   729 SCLEIIRRGIWSFFRLENEHL 749
Cdd:pfam03124 311 ALLEVFRRFIWNFFRVENEHL 331
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-324 1.58e-59

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: 205.10  E-value: 1.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076     1 MKFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSYKHSK---------------------LTRAASRVSQQAEALHRSFS 59
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRELESTppssspsssdsgsaaspsdstTSLPLRDPLSRSSSLDRAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076    60 GLSFHPRHSERAGDIEDQvikvDTVQEEGSRKLYETKFLKKSEEGGEFEESFF------------KKLDENLNKVNKFYR 127
Cdd:pfam03105  81 GLVPSPPSSSSSSSSDSS----SSSNSSSSSSSSSPSLLRRLPSESDDSSESYettpldsedeffERLDSELNKVNKFYK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   128 DKVKEVIEEAALLDKQMDALIALRVKMQKPDVDNLNLEKHPSDkvvvDTSDNTMRTQGTANTDMVHGIERTNIPEEEASh 207
Cdd:pfam03105 157 EKEEEFLERLEALNKQLEALRDFRIKLIRESKSDLYRWREPFG----LYSSDSSVFFSTSELDSGNSSESSVDDEVEEE- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   208 imadivpvSHTNGDEEEASIGDKQDLR-EILERVKmndvleSPITTLKGVFGDSNE----PISKKGLKKGEEQLRLVFSE 282
Cdd:pfam03105 232 --------LERNGWISPIKSKDKKKRPsEALDKVK------TPDRTLKGFLDASRRdylnRINKVNLRKAKKKLKKAFIE 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 42563076   283 FYQKLRRLKEYSFMNLLAFSKIMKKYEKIASRNASRNYMKIV 324
Cdd:pfam03105 298 LYRGLELLKSYSELNRTAFRKILKKFDKVTSLNASKDYMKEV 339
COG5409 COG5409
EXS domain-containing protein [Signal transduction mechanisms];
414-762 1.90e-40

EXS domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227696  Cd Length: 384  Bit Score: 153.03  E-value: 1.90e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 414 IPLYSLFGFIILHMLMYSANI--YFWKRYRVNYTFIFGFKQGTELG-----DREVFLVSTGLAVLAFVCFLLNLQLDMDW 486
Cdd:COG5409  35 ILLALWGGWILVFFLAFLFDVscYILTRTPINYRFIFLFEQLSSTArnfnlDFHRIIIPFHFFTTSLFIFLNAVEGLKFI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 487 RMKHHktlpeVIPLCLATIVLFILFCPFNIIYRSSRFFFIRSLFHCICAPLYEVTLPDFFLGDHLTSQIQAIRSFELFIC 566
Cdd:COG5409 115 LLFVY-----FLPLLQVGTVFWFLLKPFQIIYYWSRRYLIESLIRVFLFGYSLVRFTDFFFGDILISLTYALGDIYIFFC 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 567 YYGLgeyLQRQNKCHSHGVYnaFYFVVAVIPYWLRFLQCIRR-LCEEKESVHGYNALKYMLTIIAVIVRTAYELKKGRTW 645
Cdd:COG5409 190 VYSL---LFREPLCKSSHSD--LSGLAALLPVIVRFLQCLRRyRDSLHEFPHLLNALKYSLNIPVLFCLWLYRVYEGEER 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 646 M-ILALVSSGVATGMNTFWDIVIDWGLLR-KHSKNPYLRDKLLVPhksvYFAAMVVNVILRVAWMQLVLEFNLKSLHKIA 723
Cdd:COG5409 265 LfHLQIWFALLNSIYTSFWDVFMDWSLDSlTSLRSWSKRAVTLLK----YHIAMIINFLLRFSWIVYYLPPNHIQHSADI 340
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 42563076 724 VTSIISCLEIIRRGIWSFFRLENEHLNNVGKYRAFKSVP 762
Cdd:COG5409 341 FIFIMQLLEILRRFVWVFFRVEAEHSINFASFRAAGELK 379
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
2-318 2.07e-39

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: 142.01  E-value: 2.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   2 KFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSYKHSkltraasrvsqqaealhrsfsglsfhprhseragdiedqvikv 81
Cdd:cd14476   1 KFGKEFESQMVPEWQEAYVDYKQLKKDLKRIQKFRDE------------------------------------------- 37
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076  82 dtvqeegsrklYETKFLKKSEEGGEFEESFFKKLDENLNKVNKFYRDKVKEVIEEAALLDKQMDALIALRVKMQKPDvdn 161
Cdd:cd14476  38 -----------YETTFLEAAEEGGEYELVFFRRLDDELNKVNKFYRSKVEEVLKEAAALNKQMDALIAFRVKVENPQ--- 103
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 162 lnlekhpsdkvvvdtsdntmrtqgtantdmvhgiertnipeeeashimadivpvshtngdeeeasigdkqdlreilervk 241
Cdd:cd14476     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563076 242 mndvlespittlkgvfgdsnepiskkglkkgeeqlrlvfseFYQKLRRLKEYSFMNLLAFSKIMKKYEKIASRNASR 318
Cdd:cd14476 104 -----------------------------------------FYRKLRLLKSYSFLNMLAFSKILKKYDKVTSRNASK 139
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
2-135 2.53e-10

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: 59.12  E-value: 2.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   2 KFGKIFKKQMVPEWVEAYVDYNGLKRVLKeirsykhsKLTRAASRVSQQAEALHRSFSGLSFHPRHSERAgdIEDQVIKV 81
Cdd:cd14447   1 KFGKRLREEAVPEWRDKYVDYKALKKLIK--------NLVASADEASNSSEALELSESGGEEFESEFFEA--LDAELEKV 70
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 42563076  82 DTVQEEGSRKLyeTKFLKKSEEGGEFEESFFKKLDENLNKVNKFYRDKVKEVIE 135
Cdd:cd14447  71 NEFYQELLEEL--QELLKRLEALEPDLPALRGSLKEELEDLRKELVESYSELEE 122
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-326 4.29e-10

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 61.77  E-value: 4.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076   1 MKFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSyKHSKLTRAASRVSQQAEALHRSFSG--LSFHPRHSERAGDIEDQV 78
Cdd:COG5408   1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQK-DQLSSYHGVSDNDETRDEAGEPSNWrdRFNHALKKELSPLQANYV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076  79 ------------IKVDTVQEEGSRKLYETKFLKKSEEGGEFEES------FFKKLDENLNKVNKFYRDkvkevieeaall 140
Cdd:COG5408  80 akffenyiseeaIKLDEFYSQGQYIAYKKREFRKISSKFFYSERkalvqkEENTASSNYDTFLNLQTD------------ 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 141 dkQMDALIALRVKMQKPDVdnlnlekHPSDKVVVDTSDNTMRTQGTANTDMVHGIERTNipeeeashimaDIVPVSHTNG 220
Cdd:COG5408 148 --EGAYVADARKRAEAKSY-------DPFDSLRIDTSKEGLTKRNLNLPDYEKIVSGTD-----------EEVPSNDQDD 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563076 221 -DEEEASIGDKQDlREILERvkmndvLESPITTLKGVFgdsnepiSKKGLKKgeeqlRLVfsEFYQKLRRLKEYSFMNLL 299
Cdd:COG5408 208 eDQDFDYLAKKND-NTALLD------LSQFNFKIVKYQ-------KRSLLKK-----RII--ELYIQLHQLKSFIELNYT 266
                       330       340
                ....*....|....*....|....*..
gi 42563076 300 AFSKIMKKYEKIASRNASRNYMKIVDN 326
Cdd:COG5408 267 GFSKITKKYDKTLHQNLRHEYMSRSVN 293
SPX_GDE1_like cd14484
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ...
2-32 2.21e-05

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: 44.83  E-value: 2.21e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 42563076   2 KFGKIFKKQMVPEWVEAYVDYNGLKRVLKEI 32
Cdd:cd14484   1 KFGKNLPRNQVPEWSSSYINYKGLKKLIKAI 31
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
260-310 1.96e-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: 42.17  E-value: 1.96e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 42563076 260 SNEPISKKGLKKgeeQLRLVFSEFYQKLRRLKEYSFMNLLAFSKIMKKYEK 310
Cdd:cd14475  92 AHDPVSYRSARR---KLKKALQEYYRGLELLKSYRLLNRTAFRKINKKFDK 139
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
2-37 2.69e-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: 41.76  E-value: 2.69e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 42563076   2 KFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIRSYKH 37
Cdd:cd14480   1 KFGKTLKSSIYPPWKDYYIDYDKLKKLLKERETDRG 36
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
275-310 8.99e-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: 40.74  E-value: 8.99e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 42563076 275 QLRLVFSEFYQKLRRLKEYSFMNLLAFSKIMKKYEK 310
Cdd:cd14477 126 DLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDK 161
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
2-61 9.48e-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: 9.48e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563076   2 KFGKIFKKQMV---PEWVEAYVDYNGLKRVLKEIRSY----KHSKLTRAASRVSQQAEALHRSFSGL 61
Cdd:cd14481   1 KFGKSLKRQIEetlPEWRDKFLSYKELKKLLKLISPGnadkPNSKRDRRGGGAARAMTKEEADFVRL 67
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
1-33 8.12e-03

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: 37.27  E-value: 8.12e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 42563076   1 MKFGKIFKKQMVPEWVEAYVDYNGLKRVLKEIR 33
Cdd:cd14479   1 VNFGKKLKEDQIPEWEGYYINYKLLKKKVKQYV 33
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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