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Conserved domains on  [gi|162312135|ref|NP_588554|]
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SPX/EXS domain-containing protein [Schizosaccharomyces pombe]

Protein Classification

SPX and EXS domain-containing protein( domain architecture ID 11475064)

SPX and EXS domain-containing protein such as protein SYG1 that may function in G-protein coupled signal transduction

PubMed:  22403821
TCDB:  2.A.94

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG5409 COG5409
EXS domain-containing protein [Signal transduction mechanisms];
271-641 7.05e-141

EXS domain-containing protein [Signal transduction mechanisms];


:

Pssm-ID: 227696  Cd Length: 384  Bit Score: 416.89  E-value: 7.05e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 271 NSMRFGLLFGAGLPLAIEAACYYNATEQSSY----LLQIWGGFFLVIFAFVLFDLDCYVWEKTRVNYMLIFEFNQRKS-- 344
Cdd:COG5409    1 DLEVVGLEKGVSLSLGLYIQNLLNVGEPQSFivliLLALWGGWILVFFLAFLFDVSCYILTRTPINYRFIFLFEQLSSta 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 345 --LNWRQHLEIVGAVFFIFSLFFFLCMRN---FFPGFTIYFPALFLGVVGTFLIAP-VIVPYWRmRRYLIIQLIRVFLSG 418
Cdd:COG5409   81 rnFNLDFHRIIIPFHFFTTSLFIFLNAVEglkFILLFVYFLPLLQVGTVFWFLLKPfQIIYYWS-RRYLIESLIRVFLFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 419 LSTVHFQDFFFADQMVSLTYACGNISLFFCLYKRLWRQPqLCNSSHSPLLGFFTTLPGILRVFQCFRRYSDSLKSFPHLV 498
Cdd:COG5409  160 YSLVRFTDFFFGDILISLTYALGDIYIFFCVYSLLFREP-LCKSSHSDLSGLAALLPVIVRFLQCLRRYRDSLHEFPHLL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 499 NALKYIFNILAQMFLSLWRIHPG-LKYRVLYTIFAGVNSLFSYTWDILMDWNLLVRKDGR-WQFREHRILKqlwpYIIAM 576
Cdd:COG5409  239 NALKYSLNIPVLFCLWLYRVYEGeERLFHLQIWFALLNSIYTSFWDVFMDWSLDSLTSLRsWSKRAVTLLK----YHIAM 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312135 577 ILNFIVRSSFIFYCIFPNHIQHSSGISFF-VTLAEIMRRCMWNILRVEHEEIYNRENLRAARELKP 641
Cdd:COG5409  315 IINFLLRFSWIVYYLPPNHIQHSADIFIFiMQLLEILRRFVWVFFRVEAEHSINFASFRAAGELKV 380
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-272 1.23e-90

SPX domain-containing protein [Signal transduction mechanisms];


:

Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 284.03  E-value: 1.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   1 MKFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAKNPSEGLYGTSGILgETPEEAIVKRGQIHRF-HPLFQEFLDQQANKV 79
Cdd:COG5408    1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQLSSYHGVSDND-ETRDEAGEPSNWRDRFnHALKKELSPLQANYV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  80 EEFFENLVS-DARERMDLISDQVDIYEKLRAFKKG---TLESGSVVLIQKQHSKLRQRLDSILNFSRLQPAYHIPARKSV 155
Cdd:COG5408   80 AKFFENYISeEAIKLDEFYSQGQYIAYKKREFRKIsskFFYSERKALVQKEENTASSNYDTFLNLQTDEGAYVADARKRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 156 PTDAYTPMVSYRKLKSKLKTTL--LDFYDYLKLVSQYQHLN--------QQAFRKIVKKYDKTLHTDLQGF---WVDYMS 222
Cdd:COG5408  160 EAKSYDPFDSLRIDTSKEGLTKrnLNLPDYEKIVSGTDEEVpsndqddeDQDFDYLAKKNDNTALLDLSQFnfkIVKYQK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312135 223 RYTFTDFSITTNWQLHVEDIYARLFTNHNKKLALEHLKSFRQKEHFSANS 272
Cdd:COG5408  240 RSLLKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNLRHEYMS 289
 
Name Accession Description Interval E-value
COG5409 COG5409
EXS domain-containing protein [Signal transduction mechanisms];
271-641 7.05e-141

EXS domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227696  Cd Length: 384  Bit Score: 416.89  E-value: 7.05e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 271 NSMRFGLLFGAGLPLAIEAACYYNATEQSSY----LLQIWGGFFLVIFAFVLFDLDCYVWEKTRVNYMLIFEFNQRKS-- 344
Cdd:COG5409    1 DLEVVGLEKGVSLSLGLYIQNLLNVGEPQSFivliLLALWGGWILVFFLAFLFDVSCYILTRTPINYRFIFLFEQLSSta 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 345 --LNWRQHLEIVGAVFFIFSLFFFLCMRN---FFPGFTIYFPALFLGVVGTFLIAP-VIVPYWRmRRYLIIQLIRVFLSG 418
Cdd:COG5409   81 rnFNLDFHRIIIPFHFFTTSLFIFLNAVEglkFILLFVYFLPLLQVGTVFWFLLKPfQIIYYWS-RRYLIESLIRVFLFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 419 LSTVHFQDFFFADQMVSLTYACGNISLFFCLYKRLWRQPqLCNSSHSPLLGFFTTLPGILRVFQCFRRYSDSLKSFPHLV 498
Cdd:COG5409  160 YSLVRFTDFFFGDILISLTYALGDIYIFFCVYSLLFREP-LCKSSHSDLSGLAALLPVIVRFLQCLRRYRDSLHEFPHLL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 499 NALKYIFNILAQMFLSLWRIHPG-LKYRVLYTIFAGVNSLFSYTWDILMDWNLLVRKDGR-WQFREHRILKqlwpYIIAM 576
Cdd:COG5409  239 NALKYSLNIPVLFCLWLYRVYEGeERLFHLQIWFALLNSIYTSFWDVFMDWSLDSLTSLRsWSKRAVTLLK----YHIAM 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312135 577 ILNFIVRSSFIFYCIFPNHIQHSSGISFF-VTLAEIMRRCMWNILRVEHEEIYNRENLRAARELKP 641
Cdd:COG5409  315 IINFLLRFSWIVYYLPPNHIQHSADIFIFiMQLLEILRRFVWVFFRVEAEHSINFASFRAAGELKV 380
EXS pfam03124
EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family ...
302-627 4.05e-101

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: 312.59  E-value: 4.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  302 LLQIWGGFFLVIFAFVLFDLDCYVWEKTRVNYMLIFEFNQRKSLNWRQHLEIVGAVFFIFSLFFFLCMRNFFPGFTIYFP 381
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLLFWVDPLEYIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  382 ALFLGVVGTFLIAPVIVPYWRMRRYLIIQLIRVFLSGLSTVHFQDFFFADQMVSLTYACGNISLFFCLYKRLWRQPQ-LC 460
Cdd:pfam03124  81 LLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYASGWSGGDnQC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  461 NSSHSPLLGFFTTLPGILRVFQCFRRYSDSLKSFPHLVNALKYIFNILAQMFLSLWRIHPGLK--YRVLYTIFAGVNSLF 538
Cdd:pfam03124 161 GSSSRGLVPLLAALPYLIRFLQCLRRYRDTGDWFPHLLNALKYSTAIPVIILSALYRIYKSDEnpLFVLWILFAVINSLY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  539 SYTWDILMDWNLLVRKDGRWQF-REHRILKQLWPYIIAMILNFIVRSSFIFYCIFP-NHIQHSSGISFFVTLAEIMRRCM 616
Cdd:pfam03124 241 SFYWDVKMDWGLLQLFKNKNWFlRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHlHSFQHSELGIFLLALLEVFRRFI 320
                         330
                  ....*....|.
gi 162312135  617 WNILRVEHEEI 627
Cdd:pfam03124 321 WNFFRVENEHL 331
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-272 1.23e-90

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 284.03  E-value: 1.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   1 MKFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAKNPSEGLYGTSGILgETPEEAIVKRGQIHRF-HPLFQEFLDQQANKV 79
Cdd:COG5408    1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQLSSYHGVSDND-ETRDEAGEPSNWRDRFnHALKKELSPLQANYV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  80 EEFFENLVS-DARERMDLISDQVDIYEKLRAFKKG---TLESGSVVLIQKQHSKLRQRLDSILNFSRLQPAYHIPARKSV 155
Cdd:COG5408   80 AKFFENYISeEAIKLDEFYSQGQYIAYKKREFRKIsskFFYSERKALVQKEENTASSNYDTFLNLQTDEGAYVADARKRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 156 PTDAYTPMVSYRKLKSKLKTTL--LDFYDYLKLVSQYQHLN--------QQAFRKIVKKYDKTLHTDLQGF---WVDYMS 222
Cdd:COG5408  160 EAKSYDPFDSLRIDTSKEGLTKrnLNLPDYEKIVSGTDEEVpsndqddeDQDFDYLAKKNDNTALLDLSQFnfkIVKYQK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312135 223 RYTFTDFSITTNWQLHVEDIYARLFTNHNKKLALEHLKSFRQKEHFSANS 272
Cdd:COG5408  240 RSLLKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNLRHEYMS 289
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
2-207 1.92e-40

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: 144.63  E-value: 1.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   2 KFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAknpseglygtsgilgetpeeaivkrgqihrfhplFQEFLDQQANKVEE 81
Cdd:cd14475    1 KFAKYLEENLVPEWRKKYLDYKGGKKKIKARE----------------------------------FFEFLDSELDKVES 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  82 FFENLVSDARERMDLISDQVDIYEKLRAFKkgtlesgsvvliqkqhsklrqrldsilnfsrlqpaYHIPARKSV--PTDA 159
Cdd:cd14475   47 FYKEKEDEARERLDLLRDQLHELRDHRIQE-----------------------------------ADDGRRDYSrrPEQN 91
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 162312135 160 YTPMVSYRKLKSKLKTTLLDFYDYLKLVSQYQHLNQQAFRKIVKKYDK 207
Cdd:cd14475   92 AHDPVSYRSARRKLKKALQEYYRGLELLKSYRLLNRTAFRKINKKFDK 139
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-222 1.51e-20

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: 93.40  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135    1 MKFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAK-----------------------------------NPSEGLYGTSG 45
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRelestppssspsssdsgsaaspsdsttslplrdplSRSSSLDRAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   46 ILGETPEEAIVKRG-------------------QIHRFHPL------------------FQEFLDQQANKVEEFFENLVS 88
Cdd:pfam03105  81 GLVPSPPSSSSSSSsdsssssnssssssssspsLLRRLPSEsddssesyettpldsedeFFERLDSELNKVNKFYKEKEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   89 DARERMDLISDQVDIyekLRAFKK-------------------GTLESGSVVLIQKQHSKLRQRLDSILNFS-------- 141
Cdd:pfam03105 161 EFLERLEALNKQLEA---LRDFRIkliresksdlyrwrepfglYSSDSSVFFSTSELDSGNSSESSVDDEVEeelerngw 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  142 --RLQPAYHIPARKSVPTDAYTPM--------------------VSYRKLKSKLKTTLLDFYDYLKLVSQYQHLNQQAFR 199
Cdd:pfam03105 238 isPIKSKDKKKRPSEALDKVKTPDrtlkgfldasrrdylnrinkVNLRKAKKKLKKAFIELYRGLELLKSYSELNRTAFR 317
                         330       340
                  ....*....|....*....|...
gi 162312135  200 KIVKKYDKTLHTDLQGfwvDYMS 222
Cdd:pfam03105 318 KILKKFDKVTSLNASK---DYMK 337
 
Name Accession Description Interval E-value
COG5409 COG5409
EXS domain-containing protein [Signal transduction mechanisms];
271-641 7.05e-141

EXS domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227696  Cd Length: 384  Bit Score: 416.89  E-value: 7.05e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 271 NSMRFGLLFGAGLPLAIEAACYYNATEQSSY----LLQIWGGFFLVIFAFVLFDLDCYVWEKTRVNYMLIFEFNQRKS-- 344
Cdd:COG5409    1 DLEVVGLEKGVSLSLGLYIQNLLNVGEPQSFivliLLALWGGWILVFFLAFLFDVSCYILTRTPINYRFIFLFEQLSSta 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 345 --LNWRQHLEIVGAVFFIFSLFFFLCMRN---FFPGFTIYFPALFLGVVGTFLIAP-VIVPYWRmRRYLIIQLIRVFLSG 418
Cdd:COG5409   81 rnFNLDFHRIIIPFHFFTTSLFIFLNAVEglkFILLFVYFLPLLQVGTVFWFLLKPfQIIYYWS-RRYLIESLIRVFLFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 419 LSTVHFQDFFFADQMVSLTYACGNISLFFCLYKRLWRQPqLCNSSHSPLLGFFTTLPGILRVFQCFRRYSDSLKSFPHLV 498
Cdd:COG5409  160 YSLVRFTDFFFGDILISLTYALGDIYIFFCVYSLLFREP-LCKSSHSDLSGLAALLPVIVRFLQCLRRYRDSLHEFPHLL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 499 NALKYIFNILAQMFLSLWRIHPG-LKYRVLYTIFAGVNSLFSYTWDILMDWNLLVRKDGR-WQFREHRILKqlwpYIIAM 576
Cdd:COG5409  239 NALKYSLNIPVLFCLWLYRVYEGeERLFHLQIWFALLNSIYTSFWDVFMDWSLDSLTSLRsWSKRAVTLLK----YHIAM 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312135 577 ILNFIVRSSFIFYCIFPNHIQHSSGISFF-VTLAEIMRRCMWNILRVEHEEIYNRENLRAARELKP 641
Cdd:COG5409  315 IINFLLRFSWIVYYLPPNHIQHSADIFIFiMQLLEILRRFVWVFFRVEAEHSINFASFRAAGELKV 380
EXS pfam03124
EXS family; We have named this region the EXS family after (ERD1, XPR1, and SYG1). This family ...
302-627 4.05e-101

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: 312.59  E-value: 4.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  302 LLQIWGGFFLVIFAFVLFDLDCYVWEKTRVNYMLIFEFNQRKSLNWRQHLEIVGAVFFIFSLFFFLCMRNFFPGFTIYFP 381
Cdd:pfam03124   1 LPLLYRGLFLVILGLWLWGLNLYIWRKYGINYVFIFELDPRHHLSYRQLFELAAFLTLLWLLFLLLFFLLFWVDPLEYIP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  382 ALFLGVVGTFLIAPVIVPYWRMRRYLIIQLIRVFLSGLSTVHFQDFFFADQMVSLTYACGNISLFFCLYKRLWRQPQ-LC 460
Cdd:pfam03124  81 LLLLLILLLLLFNPFPIFYRSSRFWLLRTLWRILLAPLYPVEFRDFFLADQLTSLAKVLGDLEYFFCYYASGWSGGDnQC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  461 NSSHSPLLGFFTTLPGILRVFQCFRRYSDSLKSFPHLVNALKYIFNILAQMFLSLWRIHPGLK--YRVLYTIFAGVNSLF 538
Cdd:pfam03124 161 GSSSRGLVPLLAALPYLIRFLQCLRRYRDTGDWFPHLLNALKYSTAIPVIILSALYRIYKSDEnpLFVLWILFAVINSLY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  539 SYTWDILMDWNLLVRKDGRWQF-REHRILKQLWPYIIAMILNFIVRSSFIFYCIFP-NHIQHSSGISFFVTLAEIMRRCM 616
Cdd:pfam03124 241 SFYWDVKMDWGLLQLFKNKNWFlRDKLLYPKKWVYYFAIVLDLILRFTWILKLSPHlHSFQHSELGIFLLALLEVFRRFI 320
                         330
                  ....*....|.
gi 162312135  617 WNILRVEHEEI 627
Cdd:pfam03124 321 WNFFRVENEHL 331
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-272 1.23e-90

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 284.03  E-value: 1.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   1 MKFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAKNPSEGLYGTSGILgETPEEAIVKRGQIHRF-HPLFQEFLDQQANKV 79
Cdd:COG5408    1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQLSSYHGVSDND-ETRDEAGEPSNWRDRFnHALKKELSPLQANYV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  80 EEFFENLVS-DARERMDLISDQVDIYEKLRAFKKG---TLESGSVVLIQKQHSKLRQRLDSILNFSRLQPAYHIPARKSV 155
Cdd:COG5408   80 AKFFENYISeEAIKLDEFYSQGQYIAYKKREFRKIsskFFYSERKALVQKEENTASSNYDTFLNLQTDEGAYVADARKRA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135 156 PTDAYTPMVSYRKLKSKLKTTL--LDFYDYLKLVSQYQHLN--------QQAFRKIVKKYDKTLHTDLQGF---WVDYMS 222
Cdd:COG5408  160 EAKSYDPFDSLRIDTSKEGLTKrnLNLPDYEKIVSGTDEEVpsndqddeDQDFDYLAKKNDNTALLDLSQFnfkIVKYQK 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 162312135 223 RYTFTDFSITTNWQLHVEDIYARLFTNHNKKLALEHLKSFRQKEHFSANS 272
Cdd:COG5408  240 RSLLKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNLRHEYMS 289
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
2-207 1.92e-40

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: 144.63  E-value: 1.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   2 KFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAknpseglygtsgilgetpeeaivkrgqihrfhplFQEFLDQQANKVEE 81
Cdd:cd14475    1 KFAKYLEENLVPEWRKKYLDYKGGKKKIKARE----------------------------------FFEFLDSELDKVES 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  82 FFENLVSDARERMDLISDQVDIYEKLRAFKkgtlesgsvvliqkqhsklrqrldsilnfsrlqpaYHIPARKSV--PTDA 159
Cdd:cd14475   47 FYKEKEDEARERLDLLRDQLHELRDHRIQE-----------------------------------ADDGRRDYSrrPEQN 91
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 162312135 160 YTPMVSYRKLKSKLKTTLLDFYDYLKLVSQYQHLNQQAFRKIVKKYDK 207
Cdd:cd14475   92 AHDPVSYRSARRKLKKALQEYYRGLELLKSYRLLNRTAFRKINKKFDK 139
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-222 1.51e-20

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: 93.40  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135    1 MKFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAK-----------------------------------NPSEGLYGTSG 45
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRelestppssspsssdsgsaaspsdsttslplrdplSRSSSLDRAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   46 ILGETPEEAIVKRG-------------------QIHRFHPL------------------FQEFLDQQANKVEEFFENLVS 88
Cdd:pfam03105  81 GLVPSPPSSSSSSSsdsssssnssssssssspsLLRRLPSEsddssesyettpldsedeFFERLDSELNKVNKFYKEKEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   89 DARERMDLISDQVDIyekLRAFKK-------------------GTLESGSVVLIQKQHSKLRQRLDSILNFS-------- 141
Cdd:pfam03105 161 EFLERLEALNKQLEA---LRDFRIkliresksdlyrwrepfglYSSDSSVFFSTSELDSGNSSESSVDDEVEeelerngw 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  142 --RLQPAYHIPARKSVPTDAYTPM--------------------VSYRKLKSKLKTTLLDFYDYLKLVSQYQHLNQQAFR 199
Cdd:pfam03105 238 isPIKSKDKKKRPSEALDKVKTPDrtlkgfldasrrdylnrinkVNLRKAKKKLKKAFIELYRGLELLKSYSELNRTAFR 317
                         330       340
                  ....*....|....*....|...
gi 162312135  200 KIVKKYDKTLHTDLQGfwvDYMS 222
Cdd:pfam03105 318 KILKKFDKVTSLNASK---DYMK 337
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
2-207 6.58e-15

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: 72.21  E-value: 6.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   2 KFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAKNPSEGlygtsgilGETPEEAIVKRGQIHRFHPLFQEFLDQQANKVEE 81
Cdd:cd14447    1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEA--------SNSSEALELSESGGEEFESEFFEALDAELEKVNE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  82 FFENLVSDARErmdlisdqvdIYEKLRAFKKGTLESGSVvlIQKQHSKLRQRLDSIlnfsrlqpayhiparksvptdayt 161
Cdd:cd14447   73 FYQELLEELQE----------LLKRLEALEPDLPALRGS--LKEELEDLRKELVES------------------------ 116
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 162312135 162 pmvsyrklksklkttlldfYDYLKLVSQYQHLNQQAFRKIVKKYDK 207
Cdd:cd14447  117 -------------------YSELEELERFVELNYTAFRKILKKYDK 143
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
2-208 1.50e-11

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: 62.28  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   2 KFGKVIEGQSVAEWASAYFDYKKGKKIIAGIaKNPSEGLYGTSGILGETPEEAIVkrgqihrfhpLFQEFLDQQANKVEE 81
Cdd:cd14476    1 KFGKEFESQMVPEWQEAYVDYKQLKKDLKRI-QKFRDEYETTFLEAAEEGGEYEL----------VFFRRLDDELNKVNK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  82 FFENLVSDARERMDLISDQVDIyeklrafkkgtlesgsvvLIQkqhskLRQRLDsilnfsrlQPAYhiparksvptdayt 161
Cdd:cd14476   70 FYRSKVEEVLKEAAALNKQMDA------------------LIA-----FRVKVE--------NPQF-------------- 104
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 162312135 162 pmvsYRKLKsklkttlldfydYLKlvsQYQHLNQQAFRKIVKKYDKT 208
Cdd:cd14476  105 ----YRKLR------------LLK---SYSFLNMLAFSKILKKYDKV 132
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
2-207 7.50e-11

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: 61.15  E-value: 7.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   2 KFGKVIEGQSVAEWASAYFDYKKGKKII-AGIAKNPSEglygtsgilgETPEEAIVKRgQIHRFHPLFQEFLDQQANKVE 80
Cdd:cd14477    1 KFGEHLSAHITPEWRKQYINYEELKAMLyAAVEQAPSP----------EVTDEDVVKR-YFAKFEEEFFQECDKELAKVN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  81 EFFENLVSDARERMDLISDQvdiyekLRAFKKGTLESGSvvliqkqHSKLRQRLDSILNFSRLQPayhiparksvptday 160
Cdd:cd14477   70 TFFSEKLAEAQRKFATLKNE------LLSSLEAQGESGA-------ASSLIRRVFALLRKERVKP--------------- 121
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 162312135 161 tpmvsyRKLKsKLKTTLLDFYDYLKLVSQYQHLNQQAFRKIVKKYDK 207
Cdd:cd14477  122 ------RKLR-DLKLAFSEFYLSLILLQNYQNLNFTGFRKILKKHDK 161
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
2-210 7.74e-09

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: 55.33  E-value: 7.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   2 KFGKVIEGQSV--AEWASAYFDYKKGKKIIAGIAKNP--SEGLYGTSGILGETPEEAIVKRGQihrfhplfqeflDQQAN 77
Cdd:cd14483    1 KFGKYIQARQLelPEYSAYFLDYKALKKLIKSLAAPRvaAAAALLAGGRPLSPDGTDESDAQT------------SLQAN 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  78 KVEEFFEnlvsdaRERmDLisdqvdiyEKLRAFkkgtlesgsvvLIQKQhSKLRQRLDSILNFSR-LQPAYHIPARKSVp 156
Cdd:cd14483   69 KAAFFFK------LER-EL--------EKVNAF-----------YLQKE-AELKLRLDTLLDKKRvLQSRGKLASKKSA- 120
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 162312135 157 tdaytpmvSYRKLKSKLKttllDFY-DYLKLvSQYQHLNQQAFRKIVKKYDKTLH 210
Cdd:cd14483  121 --------SFVTLEEGFR----QFErDLNKL-QQFVELNATGFSKILKKWDKRSK 162
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
11-207 9.23e-06

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: 45.99  E-value: 9.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  11 SVAEWASAYFDYKKGKKIIAGIAKNPSEGLYGTsgilGETPEEAIVKRGQIHRFHP--LFQEFLDQQANKVEEFFENLVS 88
Cdd:cd14478   10 AVPEWSDHYIAYSNLKKLIYQLEKDQLQLQNGG----DDEEEEESSLLLLSTDEDPddVFVRALDKELEKIDSFYKEKEA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  89 DARERMDLISDQVDIYEKlrafkkgtlesgSVVLIQKQhSKLRQRLdsilnfsrlqpayhiparksvpTDAYtpmVSYRK 168
Cdd:cd14478   86 ELYAEVDELLKDVEEFEE------------ENYLYDSR-ISLKKRI----------------------INLY---VSLSE 127
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 162312135 169 LKSklkttlldfydylklvsqYQHLNQQAFRKIVKKYDK 207
Cdd:cd14478  128 LKS------------------YIELNRTGFSKILKKYDK 148
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
1-209 3.43e-05

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: 44.20  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135   1 MKFGKVIEGQSVAEWASAYFDYKKGKKiiagiaknpseglygtsgILGETPEEAivKRGQIHRFHPL--FQEFLDQQANK 78
Cdd:cd14479    1 VNFGKKLKEDQIPEWEGYYINYKLLKK------------------KVKQYVQQT--QDGGQDRRDVLkdFSKLLDDQIEK 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312135  79 VEEFFenlvsdaRERMDLISDQVdiyEKLRafkkgtlesgsvvliqKQHSKLrQRLDSILNFSRLQPAYHIPARksvptd 158
Cdd:cd14479   61 IVLFL-------LEQQGLLASRL---EKLG----------------EQREAL-QEQPDLSQISELREAYRAVGL------ 107
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 162312135 159 aytpmvsyrklksklkttlldfyDYLKLVsQYQHLNQQAFRKIVKKYDKTL 209
Cdd:cd14479  108 -----------------------DLLKLL-KFVELNATGLRKILKKFDKRF 134
SPX_GDE1_like cd14484
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ...
2-39 3.82e-03

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: 37.90  E-value: 3.82e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 162312135   2 KFGKVIEGQSVAEWASAYFDYKKGKKIIAGIAKNPSEG 39
Cdd:cd14484    1 KFGKNLPRNQVPEWSSSYINYKGLKKLIKAIAEQQKEG 38
 
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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