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Conserved domains on  [gi|56550691|gb|AAV97799|]
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At5g15330 [Arabidopsis thaliana]

Protein Classification

SPX domain-containing protein( domain architecture ID 10199673)

SPX (Syg1, Pho81 and XPR1) domain-containing protein may be involved in G-protein associated signal transduction

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
2-176 3.42e-79

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: 237.55  E-value: 3.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRTHLEETLPEWRDKFLCYKPLKKLLKYYPYYSADFGPANSDHNDSRpvfadttnissaaddggvvpGVRPSEDL 81
Cdd:cd14481   1 KFGKSLKRQIEETLPEWRDKFLSYKELKKLLKLISPGNADKPNSKRDRRGGG--------------------AARAMTKE 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  82 QGSFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIEQVKEkngefaSESEFSEEMMDIRRDLVTIHGEMVLLKNYSSL 161
Cdd:cd14481  61 EADFVRLLNAELDKFNAFFVEKEEEYVIRLKELQDRVAEAKE------TPRDSNEELMRIRREIVDFHGEMVLLENYSSL 134
                       170
                ....*....|....*
gi 56550691 162 NFAGLVKILKKYDKR 176
Cdd:cd14481 135 NYTGLVKILKKYDKR 149
 
Name Accession Description Interval E-value
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
2-176 3.42e-79

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: 237.55  E-value: 3.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRTHLEETLPEWRDKFLCYKPLKKLLKYYPYYSADFGPANSDHNDSRpvfadttnissaaddggvvpGVRPSEDL 81
Cdd:cd14481   1 KFGKSLKRQIEETLPEWRDKFLSYKELKKLLKLISPGNADKPNSKRDRRGGG--------------------AARAMTKE 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  82 QGSFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIEQVKEkngefaSESEFSEEMMDIRRDLVTIHGEMVLLKNYSSL 161
Cdd:cd14481  61 EADFVRLLNAELDKFNAFFVEKEEEYVIRLKELQDRVAEAKE------TPRDSNEELMRIRREIVDFHGEMVLLENYSSL 134
                       170
                ....*....|....*
gi 56550691 162 NFAGLVKILKKYDKR 176
Cdd:cd14481 135 NYTGLVKILKKYDKR 149
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-178 5.48e-11

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: 62.58  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691     1 MKFGKEFRTHLEetlPEWRDKFLCYKPLKKLLK-----------------YYPYYSADFGPANSDHNDSRPVF------- 56
Cdd:pfam03105   1 MKFGKELEENLV---PEWRDAYLDYKQLKKLIKkiqrelestppssspssSDSGSAASPSDSTTSLPLRDPLSrsssldr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691    57 -----------ADTTNISSAADDGGVVPGVRPSEDLQGS-----------------------FVRILNDELEKFNDFYVD 102
Cdd:pfam03105  78 afgglvpsppsSSSSSSSDSSSSSNSSSSSSSSSPSLLRrlpsesddssesyettpldsedeFFERLDSELNKVNKFYKE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   103 KEEDFVIRLQELKERIEQVKEK-------------------------NGEFASESEFSEEMMDIRRDLVTIHGEMV---- 153
Cdd:pfam03105 158 KEEEFLERLEALNKQLEALRDFrikliresksdlyrwrepfglyssdSSVFFSTSELDSGNSSESSVDDEVEEELErngw 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   154 ------------------------------------------------------------------LLKNYSSLNFAGLV 167
Cdd:pfam03105 238 ispikskdkkkrpsealdkvktpdrtlkgfldasrrdylnrinkvnlrkakkklkkafielyrgleLLKSYSELNRTAFR 317
                         330
                  ....*....|.
gi 56550691   168 KILKKYDKRTG 178
Cdd:pfam03105 318 KILKKFDKVTS 328
 
Name Accession Description Interval E-value
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
2-176 3.42e-79

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: 237.55  E-value: 3.42e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRTHLEETLPEWRDKFLCYKPLKKLLKYYPYYSADFGPANSDHNDSRpvfadttnissaaddggvvpGVRPSEDL 81
Cdd:cd14481   1 KFGKSLKRQIEETLPEWRDKFLSYKELKKLLKLISPGNADKPNSKRDRRGGG--------------------AARAMTKE 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  82 QGSFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIEQVKEkngefaSESEFSEEMMDIRRDLVTIHGEMVLLKNYSSL 161
Cdd:cd14481  61 EADFVRLLNAELDKFNAFFVEKEEEYVIRLKELQDRVAEAKE------TPRDSNEELMRIRREIVDFHGEMVLLENYSSL 134
                       170
                ....*....|....*
gi 56550691 162 NFAGLVKILKKYDKR 176
Cdd:cd14481 135 NYTGLVKILKKYDKR 149
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
2-175 7.00e-33

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: 118.82  E-value: 7.00e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRthlEETLPEWRDKFLCYKPLKKLLKYYPYYSADFGPANSDHNDSRpvfadttnissaaddggvvpgvRPSEDL 81
Cdd:cd14447   1 KFGKRLR---EEAVPEWRDKYVDYKALKKLIKNLVASADEASNSSEALELSE----------------------SGGEEF 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  82 QGSFVRILNDELEKFNDFYVDKEEdfviRLQELKERIEQVKEKNGEFASESEfsEEMMDIRRDLVTIHGEMVLLKNYSSL 161
Cdd:cd14447  56 ESEFFEALDAELEKVNEFYQELLE----ELQELLKRLEALEPDLPALRGSLK--EELEDLRKELVESYSELEELERFVEL 129
                       170
                ....*....|....
gi 56550691 162 NFAGLVKILKKYDK 175
Cdd:cd14447 130 NYTAFRKILKKYDK 143
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
2-178 1.85e-18

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: 79.99  E-value: 1.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRTHLeetLPEWRDKFLCYKPLKKLLK----YYPYYSADFGpansdhndsrpvfadttnisSAADDGGvvpgvrp 77
Cdd:cd14476   1 KFGKEFESQM---VPEWQEAYVDYKQLKKDLKriqkFRDEYETTFL--------------------EAAEEGG------- 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  78 seDLQGSFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIE-----QVKEKNGEFasesefseemmdirrdlvtiHGEM 152
Cdd:cd14476  51 --EYELVFFRRLDDELNKVNKFYRSKVEEVLKEAAALNKQMDaliafRVKVENPQF--------------------YRKL 108
                       170       180
                ....*....|....*....|....*.
gi 56550691 153 VLLKNYSSLNFAGLVKILKKYDKRTG 178
Cdd:cd14476 109 RLLKSYSFLNMLAFSKILKKYDKVTS 134
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
2-176 9.97e-18

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: 78.83  E-value: 9.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEF-RTHLEetLPEWRDKFLCYKPLKKLLKyypyySADFGPANSDHNDSRPVFADTTNISSAADdggvvpgvrPSED 80
Cdd:cd14483   1 KFGKYIqARQLE--LPEYSAYFLDYKALKKLIK-----SLAAPRVAAAAALLAGGRPLSPDGTDESD---------AQTS 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  81 LQ---GSFVRILNDELEKFNDFYVDKEEDFVIRLQEL--KERIEQ--VKEKNGEFASESEFSEEMMDIRRDLVTihgemv 153
Cdd:cd14483  65 LQankAAFFFKLERELEKVNAFYLQKEAELKLRLDTLldKKRVLQsrGKLASKKSASFVTLEEGFRQFERDLNK------ 138
                       170       180
                ....*....|....*....|...
gi 56550691 154 lLKNYSSLNFAGLVKILKKYDKR 176
Cdd:cd14483 139 -LQQFVELNATGFSKILKKWDKR 160
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
2-175 3.94e-16

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: 73.73  E-value: 3.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRTHLeetLPEWRDKFLCYKPLKKLLKyypyysadfgpansDHNDSRPVFadttnissaaddggvvpgvrpSEDL 81
Cdd:cd14480   1 KFGKTLKSSI---YPPWKDYYIDYDKLKKLLK--------------ERETDRGWW---------------------TEDD 42
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  82 QGSFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIEQVKEKNGEfASESEFSEEMMDIRRDLVTIHGEMVLLKNYSSL 161
Cdd:cd14480  43 ERFFVELLEVELEKVYTFQKEKYSELRRRIDACEKKVKELVSNLDS-SEDDPSEEDFKELEEELDDILADVHDLAKFTRL 121
                       170
                ....*....|....
gi 56550691 162 NFAGLVKILKKYDK 175
Cdd:cd14480 122 NYTGFLKIVKKHDK 135
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
1-178 1.76e-15

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: 71.93  E-value: 1.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   1 MKFGKEFrthLEETLPEWRDKFLCYKPLKKLLKYYPyysadfgpansdhndsrpvfadttnisSAADDGGvvpgvRPSED 80
Cdd:cd14479   1 VNFGKKL---KEDQIPEWEGYYINYKLLKKKVKQYV---------------------------QQTQDGG-----QDRRD 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  81 LQGSFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIEQVKEKNgEFASESEFSEEMMDIRRDLVTihgemvLLKnYSS 160
Cdd:cd14479  46 VLKDFSKLLDDQIEKIVLFLLEQQGLLASRLEKLGEQREALQEQP-DLSQISELREAYRAVGLDLLK------LLK-FVE 117
                       170
                ....*....|....*...
gi 56550691 161 LNFAGLVKILKKYDKRTG 178
Cdd:cd14479 118 LNATGLRKILKKFDKRFG 135
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
2-175 1.81e-15

SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus binds directly to the G-protein beta subunit and inhibits transduction of the mating pheromone signal, and it co-occurs with a C-terminal domain from the EXS family.


Pssm-ID: 269896 [Multi-domain]  Cd Length: 139  Bit Score: 71.83  E-value: 1.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKefrtHLEETL-PEWRDKFLCYKPLKKLLKyypyysadfgpansdhndsrpvfadttnissAADdggvvpgvrpsed 80
Cdd:cd14475   1 KFAK----YLEENLvPEWRKKYLDYKGGKKKIK-------------------------------ARE------------- 32
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  81 lqgsFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIEQVKEKNGEFASESEfseemMDIRRDLVTIHGEMV------- 153
Cdd:cd14475  33 ----FFEFLDSELDKVESFYKEKEDEARERLDLLRDQLHELRDHRIQEADDGR-----RDYSRRPEQNAHDPVsyrsarr 103
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 56550691 154 --------------LLKNYSSLNFAGLVKILKKYDK 175
Cdd:cd14475 104 klkkalqeyyrgleLLKSYRLLNRTAFRKINKKFDK 139
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
16-175 2.42e-15

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: 71.80  E-value: 2.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  16 PEWRDKFLCYKPLKKLLkyypyYS-------ADFGPANSDHNDSRPvfadttnissaaddggvvPGVRPSEDLQGSFVRI 88
Cdd:cd14478  12 PEWSDHYIAYSNLKKLI-----YQlekdqlqLQNGGDDEEEEESSL------------------LLLSTDEDPDDVFVRA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  89 LNDELEKFNDFYVDKEEDFVIRLQELKERIEqvkekngEFASESEFSEEMMDIRRDLVTIHGEMVLLKNYSSLNFAGLVK 168
Cdd:cd14478  69 LDKELEKIDSFYKEKEAELYAEVDELLKDVE-------EFEEENYLYDSRISLKKRIINLYVSLSELKSYIELNRTGFSK 141

                ....*..
gi 56550691 169 ILKKYDK 175
Cdd:cd14478 142 ILKKYDK 148
SPX_GDE1_like cd14484
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ...
2-178 3.07e-15

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: 71.41  E-value: 3.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRTHleeTLPEWRDKFLCYKPLKKLLKyypyysadfgpansdhndsrpvfadttNISSAADDGGvvpgvrpSEDL 81
Cdd:cd14484   1 KFGKNLPRN---QVPEWSSSYINYKGLKKLIK---------------------------AIAEQQKEGV-------KVDL 43
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  82 qGSFVRILNDELEKFNDFYVDKEEDFVIRLQELKERIEQVKEkngefASESEFSEEMMDIRRDLVTIHGEMVLLKNYSSL 161
Cdd:cd14484  44 -AEFFFALDRNLEDVDTFYNKKFAEYSRRLKLLLDRYGFSPD-----LVQNLDSDELEELMGALLELRSQLRNLQWFGEL 117
                       170
                ....*....|....*..
gi 56550691 162 NFAGLVKILKKYDKRTG 178
Cdd:cd14484 118 NRRGFVKILKKLDKKVP 134
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-178 5.48e-11

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: 62.58  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691     1 MKFGKEFRTHLEetlPEWRDKFLCYKPLKKLLK-----------------YYPYYSADFGPANSDHNDSRPVF------- 56
Cdd:pfam03105   1 MKFGKELEENLV---PEWRDAYLDYKQLKKLIKkiqrelestppssspssSDSGSAASPSDSTTSLPLRDPLSrsssldr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691    57 -----------ADTTNISSAADDGGVVPGVRPSEDLQGS-----------------------FVRILNDELEKFNDFYVD 102
Cdd:pfam03105  78 afgglvpsppsSSSSSSSDSSSSSNSSSSSSSSSPSLLRrlpsesddssesyettpldsedeFFERLDSELNKVNKFYKE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   103 KEEDFVIRLQELKERIEQVKEK-------------------------NGEFASESEFSEEMMDIRRDLVTIHGEMV---- 153
Cdd:pfam03105 158 KEEEFLERLEALNKQLEALRDFrikliresksdlyrwrepfglyssdSSVFFSTSELDSGNSSESSVDDEVEEELErngw 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   154 ------------------------------------------------------------------LLKNYSSLNFAGLV 167
Cdd:pfam03105 238 ispikskdkkkrpsealdkvktpdrtlkgfldasrrdylnrinkvnlrkakkklkkafielyrgleLLKSYSELNRTAFR 317
                         330
                  ....*....|.
gi 56550691   168 KILKKYDKRTG 178
Cdd:pfam03105 318 KILKKFDKVTS 328
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
2-175 1.58e-09

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: 55.76  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691   2 KFGKEFRTHLEetlPEWRDKFLCYKPLKKLLkyypYYSADFGPAnsdhndsrpvfadttnissaADDGGVVPGVRPSEDL 81
Cdd:cd14477   1 KFGEHLSAHIT---PEWRKQYINYEELKAML----YAAVEQAPS--------------------PEVTDEDVVKRYFAKF 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56550691  82 QGSFVRILNDELEKFNDFYVDK--EedfVIR----LQ-ELKERIEQVKEKNGEFASESEFSEEMMDIRRDLVTIHgEM-- 152
Cdd:cd14477  54 EEEFFQECDKELAKVNTFFSEKlaE---AQRkfatLKnELLSSLEAQGESGAASSLIRRVFALLRKERVKPRKLR-DLkl 129
                       170       180       190
                ....*....|....*....|....*....|..
gi 56550691 153 ---------VLLKNYSSLNFAGLVKILKKYDK 175
Cdd:cd14477 130 afsefylslILLQNYQNLNFTGFRKILKKHDK 161
 
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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