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Conserved domains on  [gi|208609982|ref|NP_001129141|]
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solute carrier family 53 member 1 isoform 2 [Homo sapiens]

Protein Classification

xenotropic and polytropic retrovirus receptor 1( domain architecture ID 10199615)

xenotropic and polytropic retrovirus receptor 1 (XPR1) plays a role in phosphate homeostasis

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 ...
 268-552 1.40e-102

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: 314.90  E-value: 1.40e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  268 LIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRSNLSHQHLFEIAGFLGILWCLSLLACFFApISVIPTYVY 347
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLL-FWVDPLEYI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  348 PLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSleLKWDESK 427
Cdd:pfam03124  80 PLLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYA--SGWSGGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  428 GLLPNNSEE---------------------------------------------------RGHSDTMVFFYLWIVFYIIS 456
Cdd:pfam03124 158 NQCGSSSRGlvpllaalpylirflqclrryrdtgdwfphllnalkystaipviilsalyrIYKSDENPLFVLWILFAVIN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  457 SCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITSTTLlpHSGDIIATVFAPLEV 536
Cdd:pfam03124 238 SLYSFYWDVKMDWGLLQLFKNKNWFLRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHLHSF--QHSELGIFLLALLEV 315

                         330
                  ....*....|....*.
gi 208609982  537 FRRFVWNFFRLENEHL 552
Cdd:pfam03124 316 FRRFIWNFFRVENEHL 331
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
 2-165 1.62e-102

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: 308.06  E-value: 1.62e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQ 81
Cdd:cd14477    1 KFGEHLSAHITPEWRKQYINYEELKAMLYAAVEQAPSPEVTDEDVVKRYFAKFEEEFFQECDKELAKVNTFFSEKLAEAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  82 RRFATLQNELQSSLDAQKESTGVTTLRQRrkpVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILK 161
Cdd:cd14477   81 RKFATLKNELLSSLEAQGESGAASSLIRR---VFALLRKERVKPRKLRDLKLAFSEFYLSLILLQNYQNLNFTGFRKILK 157


                 ....
gi 208609982 162 KHDK 165
Cdd:cd14477  158 KHDK 161
 
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 ...
 268-552 1.40e-102

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: 314.90  E-value: 1.40e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  268 LIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRSNLSHQHLFEIAGFLGILWCLSLLACFFApISVIPTYVY 347
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLL-FWVDPLEYI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  348 PLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSleLKWDESK 427
Cdd:pfam03124  80 PLLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYA--SGWSGGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  428 GLLPNNSEE---------------------------------------------------RGHSDTMVFFYLWIVFYIIS 456
Cdd:pfam03124 158 NQCGSSSRGlvpllaalpylirflqclrryrdtgdwfphllnalkystaipviilsalyrIYKSDENPLFVLWILFAVIN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  457 SCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITSTTLlpHSGDIIATVFAPLEV 536
Cdd:pfam03124 238 SLYSFYWDVKMDWGLLQLFKNKNWFLRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHLHSF--QHSELGIFLLALLEV 315

                         330
                  ....*....|....*.
gi 208609982  537 FRRFVWNFFRLENEHL 552
Cdd:pfam03124 316 FRRFIWNFFRVENEHL 331
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
 2-165 1.62e-102

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: 308.06  E-value: 1.62e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQ 81
Cdd:cd14477    1 KFGEHLSAHITPEWRKQYINYEELKAMLYAAVEQAPSPEVTDEDVVKRYFAKFEEEFFQECDKELAKVNTFFSEKLAEAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  82 RRFATLQNELQSSLDAQKESTGVTTLRQRrkpVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILK 161
Cdd:cd14477   81 RKFATLKNELLSSLEAQGESGAASSLIRR---VFALLRKERVKPRKLRDLKLAFSEFYLSLILLQNYQNLNFTGFRKILK 157


                 ....
gi 208609982 162 KHDK 165
Cdd:cd14477  158 KHDK 161
COG5409 COG5409
EXS domain-containing protein [Signal transduction mechanisms];
286-568 2.41e-33

EXS domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227696  Cd Length: 384  Bit Score: 131.85  E-value: 2.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 286 GINTYGWRQAGVNHVLIFELNPRSNLSHQHL--FEIAGFLGILWCLSL--LACFFAPISVIPTYVYPLALY--GFMVFFL 359
Cdd:COG5409   54 DVSCYILTRTPINYRFIFLFEQLSSTARNFNldFHRIIIPFHFFTTSLfiFLNAVEGLKFILLFVYFLPLLqvGTVFWFL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 360 INPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSL-----ELKWDESK-----GL 429
Cdd:COG5409  134 LKPFQIIYYWSRRYLIESLIRVFLFGYSLVRFTDFFFGDILISLTYALGDIYIFFCVYSLlfrepLCKSSHSDlsglaAL 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 430 LPN------------------------------------NSEERGHSDTMVFFYLWIVFYIISSCYTLIWDLKMDWGLFD 473
Cdd:COG5409  214 LPVivrflqclrryrdslhefphllnalkyslnipvlfcLWLYRVYEGEERLFHLQIWFALLNSIYTSFWDVFMDWSLDS 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 474 KNAGENTFLREEIVYpqkaYYYCAIIEDVILRFAWTIQIsiTSTTLLPHSGDIIATVFAPLEVFRRFVWNFFRLENEHLN 553
Cdd:COG5409  294 LTSLRSWSKRAVTLL----KYHIAMIINFLLRFSWIVYY--LPPNHIQHSADIFIFIMQLLEILRRFVWVFFRVEAEHSI 367

                        330
                 ....*....|....*
gi 208609982 554 NCGEFRAVRDISVAP 568
Cdd:COG5409  368 NFASFRAAGELKVTP 382
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 1-173 1.60e-22

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: 99.17  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982    1 MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQD---------------------------------------------- 34
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRelestppssspsssdsgsaaspsdsttslplrdplsrsssldrafg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   35 ---------------------------------QAPSVEVTDEDTVKRY---FAKFEEKFFQTCEKELAKINTFYSEKLA 78
Cdd:pfam03105  81 glvpsppssssssssdsssssnssssssssspsLLRRLPSESDDSSESYettPLDSEDEFFERLDSELNKVNKFYKEKEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   79 EAQRRFATLQNELQ--------------------------SSLDA----------------------------------- 97
Cdd:pfam03105 161 EFLERLEALNKQLEalrdfrikliresksdlyrwrepfglYSSDSsvffstseldsgnssessvddeveeelerngwisp 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   98 --------------QKESTGVTTLRQRRKPVFH--LSHEERVQHRNIKD-LKLAFSEFYLSLILLQNYQNLNFTGFRKIL 160
Cdd:pfam03105 241 ikskdkkkrpsealDKVKTPDRTLKGFLDASRRdyLNRINKVNLRKAKKkLKKAFIELYRGLELLKSYSELNRTAFRKIL 320

                         330
                  ....*....|...
gi 208609982  161 KKHDKIleTSRGA 173
Cdd:pfam03105 321 KKFDKV--TSLNA 331
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-171 7.00e-08

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 54.45  E-value: 7.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   1 MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQ-------------DQAPSVEVTDEDTVKRYFAKF------------E 55
Cdd:COG5408    1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQkdqlssyhgvsdnDETRDEAGEPSNWRDRFNHALkkelsplqanyvA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  56 EKFFQTCEKELAKINTFYSEKLAEAQRRFATLQ---------------------------------NELQSSLDAQK--- 99
Cdd:COG5408   81 KFFENYISEEAIKLDEFYSQGQYIAYKKREFRKisskffyserkalvqkeentassnydtflnlqtDEGAYVADARKrae 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 100 ------------------ESTGVTTLRQRRKPVFHLSHE-----------------------------------ERVQHR 126
Cdd:COG5408  161 aksydpfdslridtskegLTKRNLNLPDYEKIVSGTDEEvpsndqddedqdfdylakkndntalldlsqfnfkiVKYQKR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 208609982 127 NIkdLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSR 171
Cdd:COG5408  241 SL--LKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNL 283
 
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 ...
 268-552 1.40e-102

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: 314.90  E-value: 1.40e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  268 LIRIYRGGFLLIEFLFLLGINTYGWRQAGVNHVLIFELNPRSNLSHQHLFEIAGFLGILWCLSLLACFFApISVIPTYVY 347
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLL-FWVDPLEYI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  348 PLALYGFMVFFLINPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSleLKWDESK 427
Cdd:pfam03124  80 PLLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYA--SGWSGGD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  428 GLLPNNSEE---------------------------------------------------RGHSDTMVFFYLWIVFYIIS 456
Cdd:pfam03124 158 NQCGSSSRGlvpllaalpylirflqclrryrdtgdwfphllnalkystaipviilsalyrIYKSDENPLFVLWILFAVIN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  457 SCYTLIWDLKMDWGLFDKNAGENTFLREEIVYPQKAYYYCAIIEDVILRFAWTIQISITSTTLlpHSGDIIATVFAPLEV 536
Cdd:pfam03124 238 SLYSFYWDVKMDWGLLQLFKNKNWFLRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHLHSF--QHSELGIFLLALLEV 315

                         330
                  ....*....|....*.
gi 208609982  537 FRRFVWNFFRLENEHL 552
Cdd:pfam03124 316 FRRFIWNFFRVENEHL 331
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
 2-165 1.62e-102

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: 308.06  E-value: 1.62e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYSEKLAEAQ 81
Cdd:cd14477    1 KFGEHLSAHITPEWRKQYINYEELKAMLYAAVEQAPSPEVTDEDVVKRYFAKFEEEFFQECDKELAKVNTFFSEKLAEAQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  82 RRFATLQNELQSSLDAQKESTGVTTLRQRrkpVFHLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILK 161
Cdd:cd14477   81 RKFATLKNELLSSLEAQGESGAASSLIRR---VFALLRKERVKPRKLRDLKLAFSEFYLSLILLQNYQNLNFTGFRKILK 157


                 ....
gi 208609982 162 KHDK 165
Cdd:cd14477  158 KHDK 161
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
 2-165 1.27e-33

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: 124.98  E-value: 1.27e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLysaqdqapsvevtdedtvKRyfakfeEKFFQTCEKELAKINTFYSEKLAEAQ 81
Cdd:cd14475    1 KFAKYLEENLVPEWRKKYLDYKGGKKKI------------------KA------REFFEFLDSELDKVESFYKEKEDEAR 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  82 RRFATLQNELQSSLDAQKESTGVTTLR-QRRKPVFHLSHEERVQHRniKDLKLAFSEFYLSLILLQNYQNLNFTGFRKIL 160
Cdd:cd14475   57 ERLDLLRDQLHELRDHRIQEADDGRRDySRRPEQNAHDPVSYRSAR--RKLKKALQEYYRGLELLKSYRLLNRTAFRKIN 134


                 ....*
gi 208609982 161 KKHDK 165
Cdd:cd14475  135 KKFDK 139
COG5409 COG5409
EXS domain-containing protein [Signal transduction mechanisms];
286-568 2.41e-33

EXS domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227696  Cd Length: 384  Bit Score: 131.85  E-value: 2.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 286 GINTYGWRQAGVNHVLIFELNPRSNLSHQHL--FEIAGFLGILWCLSL--LACFFAPISVIPTYVYPLALY--GFMVFFL 359
Cdd:COG5409   54 DVSCYILTRTPINYRFIFLFEQLSSTARNFNldFHRIIIPFHFFTTSLfiFLNAVEGLKFILLFVYFLPLLqvGTVFWFL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 360 INPTKTFYYKSRFWLLKLLFRVFTAPFHKVGFADFWLADQLNSLSVILMDLEYMICFYSL-----ELKWDESK-----GL 429
Cdd:COG5409  134 LKPFQIIYYWSRRYLIESLIRVFLFGYSLVRFTDFFFGDILISLTYALGDIYIFFCVYSLlfrepLCKSSHSDlsglaAL 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 430 LPN------------------------------------NSEERGHSDTMVFFYLWIVFYIISSCYTLIWDLKMDWGLFD 473
Cdd:COG5409  214 LPVivrflqclrryrdslhefphllnalkyslnipvlfcLWLYRVYEGEERLFHLQIWFALLNSIYTSFWDVFMDWSLDS 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 474 KNAGENTFLREEIVYpqkaYYYCAIIEDVILRFAWTIQIsiTSTTLLPHSGDIIATVFAPLEVFRRFVWNFFRLENEHLN 553
Cdd:COG5409  294 LTSLRSWSKRAVTLL----KYHIAMIINFLLRFSWIVYY--LPPNHIQHSADIFIFIMQLLEILRRFVWVFFRVEAEHSI 367

                        330
                 ....*....|....*
gi 208609982 554 NCGEFRAVRDISVAP 568
Cdd:COG5409  368 NFASFRAAGELKVTP 382
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-165 7.49e-29

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: 111.89  E-value: 7.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDT--VKRYFAKFEEKFFQTCEKELAKINTFYSEKLAE 79
Cdd:cd14447    1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNSSEALelSESGGEEFESEFFEALDAELEKVNEFYQELLEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  80 AQrrfatlqnELQSSLDAQKEStgvttlrqrrkpvfhLSHEERVQHRNIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKI 159
Cdd:cd14447   81 LQ--------ELLKRLEALEPD---------------LPALRGSLKEELEDLRKELVESYSELEELERFVELNYTAFRKI 137


                 ....*.
gi 208609982 160 LKKHDK 165
Cdd:cd14447  138 LKKYDK 143
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 1-173 1.60e-22

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: 99.17  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982    1 MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQD---------------------------------------------- 34
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRelestppssspsssdsgsaaspsdsttslplrdplsrsssldrafg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   35 ---------------------------------QAPSVEVTDEDTVKRY---FAKFEEKFFQTCEKELAKINTFYSEKLA 78
Cdd:pfam03105  81 glvpsppssssssssdsssssnssssssssspsLLRRLPSESDDSSESYettPLDSEDEFFERLDSELNKVNKFYKEKEE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   79 EAQRRFATLQNELQ--------------------------SSLDA----------------------------------- 97
Cdd:pfam03105 161 EFLERLEALNKQLEalrdfrikliresksdlyrwrepfglYSSDSsvffstseldsgnssessvddeveeelerngwisp 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   98 --------------QKESTGVTTLRQRRKPVFH--LSHEERVQHRNIKD-LKLAFSEFYLSLILLQNYQNLNFTGFRKIL 160
Cdd:pfam03105 241 ikskdkkkrpsealDKVKTPDRTLKGFLDASRRdyLNRINKVNLRKAKKkLKKAFIELYRGLELLKSYSELNRTAFRKIL 320

                         330
                  ....*....|...
gi 208609982  161 KKHDKIleTSRGA 173
Cdd:pfam03105 321 KKFDKV--TSLNA 331
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
 2-165 1.82e-19

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: 84.90  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDtvkryfaKFEEKFfqtcEKELAKINTFYSEKLAEAQ 81
Cdd:cd14480    1 KFGKTLKSSIYPPWKDYYIDYDKLKKLLKERETDRGWWTEDDER-------FFVELL----EVELEKVYTFQKEKYSELR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  82 RRFATLQNELQSsLDAQKESTGVTTLRQRrkpvFHLSHEErvqhrnikdlklafsefyLSLIL-----LQNYQNLNFTGF 156
Cdd:cd14480   70 RRIDACEKKVKE-LVSNLDSSEDDPSEED----FKELEEE------------------LDDILadvhdLAKFTRLNYTGF 126


                 ....*....
gi 208609982 157 RKILKKHDK 165
Cdd:cd14480  127 LKIVKKHDK 135
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
 13-165 2.67e-16

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: 76.04  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  13 PEWRKQYIQYEAFKDMLYSAQDQAPSVEVTDEDTVKRYFAKF--------EEKFFQTCEKELAKINTFYSEKLAEAQRRF 84
Cdd:cd14478   12 PEWSDHYIAYSNLKKLIYQLEKDQLQLQNGGDDEEEEESSLLllstdedpDDVFVRALDKELEKIDSFYKEKEAELYAEV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  85 ATLQNELQS-SLDAQKESTGVTtLRQRrkpvfhlsheervqhrnIKDLKLAFSEfylslilLQNYQNLNFTGFRKILKKH 163
Cdd:cd14478   92 DELLKDVEEfEEENYLYDSRIS-LKKR-----------------IINLYVSLSE-------LKSYIELNRTGFSKILKKY 146


                 ..
gi 208609982 164 DK 165
Cdd:cd14478  147 DK 148
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
 2-165 8.62e-16

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: 74.61  E-value: 8.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHIT---PEWRKQYIQYEAFKDML----YSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKELAKINTFYS 74
Cdd:cd14481    1 KFGKSLKRQIEetlPEWRDKFLSYKELKKLLklisPGNADKPNSKRDRRGGGAARAMTKEEADFVRLLNAELDKFNAFFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  75 EKLAEaqrrFATLQNELQSSldaqkestgvttlRQRRKPVFHLSHEE--RVQhRNIKDlklafseFYLSLILLQNYQNLN 152
Cdd:cd14481   81 EKEEE----YVIRLKELQDR-------------VAEAKETPRDSNEElmRIR-REIVD-------FHGEMVLLENYSSLN 135

                        170
                 ....*....|...
gi 208609982 153 FTGFRKILKKHDK 165
Cdd:cd14481  136 YTGLVKILKKYDK 148
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
 2-165 5.13e-15

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: 73.05  E-value: 5.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHIT--PEWRKQYIQYEAFK-------------DMLYSAQDQAPSVEVTDEDTVKRYFAKFEEKFFQTCEKEL 66
Cdd:cd14483    1 KFGKYIQARQLelPEYSAYFLDYKALKklikslaaprvaaAAALLAGGRPLSPDGTDESDAQTSLQANKAAFFFKLEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  67 AKINTFYSEKLAEAQRRFATLQ---NELQSSLD-AQKESTGVTTLRQrrkpvfhlsheervqhrnikdlklAFSEFYLSL 142
Cdd:cd14483   81 EKVNAFYLQKEAELKLRLDTLLdkkRVLQSRGKlASKKSASFVTLEE------------------------GFRQFERDL 136

                        170       180
                 ....*....|....*....|...
gi 208609982 143 ILLQNYQNLNFTGFRKILKKHDK 165
Cdd:cd14483  137 NKLQQFVELNATGFSKILKKWDK 159
SPX_GDE1_like cd14484
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ...
 2-167 1.69e-14

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: 70.64  E-value: 1.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQApsvevtdEDTVKRYFAKFeekFFQTcEKELAKINTFYSEKLAEAQ 81
Cdd:cd14484    1 KFGKNLPRNQVPEWSSSYINYKGLKKLIKAIAEQQ-------KEGVKVDLAEF---FFAL-DRNLEDVDTFYNKKFAEYS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  82 RRFATLQNELQSSLDAQKestgvttlrqrrkpvfHLSHEErvqhrnIKDLKLAFSEFYLSLILLQNYQNLNFTGFRKILK 161
Cdd:cd14484   70 RRLKLLLDRYGFSPDLVQ----------------NLDSDE------LEELMGALLELRSQLRNLQWFGELNRRGFVKILK 127


                 ....*.
gi 208609982 162 KHDKIL 167
Cdd:cd14484  128 KLDKKV 133
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
 2-173 1.35e-12

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: 65.36  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQDQAPSVEVTD----EDTvkryfAKFEEKFFQTCEKELAKINTFYSEKL 77
Cdd:cd14476    1 KFGKEFESQMVPEWQEAYVDYKQLKKDLKRIQKFRDEYETTFleaaEEG-----GEYELVFFRRLDDELNKVNKFYRSKV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  78 AEAQRRFATLQNELQsSLDAQKEstgvttlrqrrkpvfhlsheervqhrnikdlKLAFSEFYLSLILLQNYQNLNFTGFR 157
Cdd:cd14476   76 EEVLKEAAALNKQMD-ALIAFRV-------------------------------KVENPQFYRKLRLLKSYSFLNMLAFS 123

                        170
                 ....*....|....*.
gi 208609982 158 KILKKHDKIleTSRGA 173
Cdd:cd14476  124 KILKKYDKV--TSRNA 137
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
 1-165 3.05e-11

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: 61.53  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   1 MKFAEHLSAHITPEWRKQYIQYEAFKDML--YSAQDQAPSVEvtDEDTVKRyfakfeekFFQTCEKELAKINTFYSEKLA 78
Cdd:cd14479    1 VNFGKKLKEDQIPEWEGYYINYKLLKKKVkqYVQQTQDGGQD--RRDVLKD--------FSKLLDDQIEKIVLFLLEQQG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  79 EAQRRFATL---QNELQSSLDAQKESTGVTTLRQRRKPVFHLsheervqhrnikdlkLAFSEfylslillqnyqnLNFTG 155
Cdd:cd14479   71 LLASRLEKLgeqREALQEQPDLSQISELREAYRAVGLDLLKL---------------LKFVE-------------LNATG 122

                        170
                 ....*....|
gi 208609982 156 FRKILKKHDK 165
Cdd:cd14479  123 LRKILKKFDK 132
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-171 7.00e-08

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 54.45  E-value: 7.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   1 MKFAEHLSAHITPEWRKQYIQYEAFKDMLYSAQ-------------DQAPSVEVTDEDTVKRYFAKF------------E 55
Cdd:COG5408    1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQkdqlssyhgvsdnDETRDEAGEPSNWRDRFNHALkkelsplqanyvA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  56 EKFFQTCEKELAKINTFYSEKLAEAQRRFATLQ---------------------------------NELQSSLDAQK--- 99
Cdd:COG5408   81 KFFENYISEEAIKLDEFYSQGQYIAYKKREFRKisskffyserkalvqkeentassnydtflnlqtDEGAYVADARKrae 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982 100 ------------------ESTGVTTLRQRRKPVFHLSHE-----------------------------------ERVQHR 126
Cdd:COG5408  161 aksydpfdslridtskegLTKRNLNLPDYEKIVSGTDEEvpsndqddedqdfdylakkndntalldlsqfnfkiVKYQKR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 208609982 127 NIkdLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDKILETSR 171
Cdd:COG5408  241 SL--LKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNL 283
SPX_YDR089W cd14474
SPX domain of the yeast protein YDR089W and related proteins; This region has been named the ...
 2-165 1.20e-07

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: 51.08  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982   2 KFAEHLSAHITPEWRKQYIQYEAFKD--MLYSAQDQAPSVEVTDEDTvkryfaKFEEKFFQTCEKELAKINTFYSEKLAE 79
Cdd:cd14474    1 KFGEQLLQRSVPEWKLYNIDYNELKHliKEHTTRDQGTAIAIPSALE------KFEDSLYNEFCEQFDRVNLFVSSKADE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208609982  80 AQRRFATLQNELQsSLDAQKESTGVTTLRQRRKPVFHLSHEERVQHrnikDLKlafsefylsliLLQNYQNLNFTGFRKI 159
Cdd:cd14474   75 ISRRLEHLESSIL-RLLERSASNSGSRRRQKRRLAKIEQELLRCGE----ELQ-----------KLSRFIIAQKIAFRKI 138


                 ....*.
gi 208609982 160 LKKHDK 165
Cdd:cd14474  139 LKKYKK 144
 
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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