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Conserved domains on  [gi|237845515|ref|XP_002372055|]
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vacuolar transporter chaperone VTC2 [Toxoplasma gondii ME49]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF202 super family cl09954
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 1066-1173 5.18e-28

Domain of unknown function (DUF202); This family consists of hypothetical proteins some of which are putative membrane proteins. No functional information or experimental verification of function is known. This domain is around 100 amino acids long.


The actual alignment was detected with superfamily member COG5264:

Pssm-ID: 447870  Cd Length: 126  Bit Score: 110.16  E-value: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515 1066 SGPsVRVEPKTFFANERTLLQWMNTAVLIATISITLMNFGNPVGRIAGLLMSPVAVFFIGYSFWVYLRRARALERKEPIA 1145
Cdd:COG5264    18 AGP-VRVEPKVWFANERTFLSWLSVTVLLGGLGFALYNSGDRLGMISAYVFTIVAIFCGFYALMLYLKRAVNIRQRSAGP 96

                          90       100
                  ....*....|....*....|....*...
gi 237845515 1146 YNDKLGPSILVVTLMLSLSAVIALNLLY 1173
Cdd:COG5264    97 YDDRLGPTLVCVVLLVALIVNFFLAFKA 124
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-128 1.30e-14

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: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLSAQADLRYLNEYISYKDLKKAIKVITGSDVQVCTVQDVVSnfrqtnaLTGSIFRPPESRFQELLNHELDKINSF 81
Cdd:cd14447     1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNSSEALE-------LSESGGEEFESEFFEALDAELEKVNEF 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 237845515   82 SK---REVEAILDQLAVALVIMWRLHAALT--LLRLAPDSPGYAEAQALLKR 128
Cdd:cd14447    74 YQellEELQELLKRLEALEPDLPALRGSLKeeLEDLRKELVESYSELEELER 125
CYTH-like_Pase super family cl11964
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 669-827 1.24e-09

CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like superfamily enzymes hydrolyze triphosphate-containing substrates and require metal cations as cofactors. They have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB), and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions.


The actual alignment was detected with superfamily member cd07751:

Pssm-ID: 448368  Cd Length: 290  Bit Score: 60.84  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  669 AVQQRGVSPSVRTWFYRTEF-MSEDGVAWISVDEDIRFSREMNRTPPAN-QWIRSETEALSTDDVHPFPWGLLDVSfLVR 746
Cdd:cd07751   165 VILKRKLKPVVRTFYRRTAFqLPDDNRVRISLDTELCMIDERGRDGRRRtTLNDWPFKQLPDNEIVRFPYAVLEVK-LQT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  747 DNGVALPQhavqqakdfhplvgrddledFVADLRGLSTLTEVPGFSLFAHGTAYFYTPRlqalqarmsgyeqaVHLIPLW 826
Cdd:cd07751   244 QEGEEPPE--------------------WVEELLNSHLVEEVYKFSKFLHGCATLFPDK--------------VDSIPYW 289


                  .
gi 237845515  827 L 827
Cdd:cd07751   290 L 290
SPX super family cl28943
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 58-286 1.30e-09

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.


The actual alignment was detected with superfamily member pfam03105:

Pssm-ID: 460807 [Multi-domain]  Cd Length: 339  Bit Score: 61.42  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    58 SIFRPPESRFQELLNHELDKINSFSKREVEAIldqlavalvimwrlhaaltllrlapdspgYAEAQALLKRLEQ-REQEI 136
Cdd:pfam03105  131 TTPLDSEDEFFERLDSELNKVNKFYKEKEEEF-----------------------------LERLEALNKQLEAlRDFRI 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   137 RnalVVYPQKRGRATEQDKAGSPSSN------------PRCRGVSDEPSSSSEERELGAEGDDFSSAGGKTSSRGEGDAK 204
Cdd:pfam03105  182 K---LIRESKSDLYRWREPFGLYSSDssvffstseldsGNSSESSVDDEVEEELERNGWISPIKSKDKKKRPSEALDKVK 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   205 --RRQGDEDGGEGEQDDAKR----SVAEALILLEKDVLEVEGVLEaqsqeivFLDSFVRLNFTGFRKITKKYDKHNQSSA 278
Cdd:pfam03105  259 tpDRTLKGFLDASRRDYLNRinkvNLRKAKKKLKKAFIELYRGLE-------LLKSYSELNRTAFRKILKKFDKVTSLNA 331


                   ....*...
gi 237845515   279 ASWYMSRV 286
Cdd:pfam03105  332 SKDYMKEV 339
 
Name Accession Description Interval E-value
VTC1 COG5264
Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];
1066-1173 5.18e-28

Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227589  Cd Length: 126  Bit Score: 110.16  E-value: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515 1066 SGPsVRVEPKTFFANERTLLQWMNTAVLIATISITLMNFGNPVGRIAGLLMSPVAVFFIGYSFWVYLRRARALERKEPIA 1145
Cdd:COG5264    18 AGP-VRVEPKVWFANERTFLSWLSVTVLLGGLGFALYNSGDRLGMISAYVFTIVAIFCGFYALMLYLKRAVNIRQRSAGP 96

                          90       100
                  ....*....|....*....|....*...
gi 237845515 1146 YNDKLGPSILVVTLMLSLSAVIALNLLY 1173
Cdd:COG5264    97 YDDRLGPTLVCVVLLVALIVNFFLAFKA 124
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-128 1.30e-14

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: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLSAQADLRYLNEYISYKDLKKAIKVITGSDVQVCTVQDVVSnfrqtnaLTGSIFRPPESRFQELLNHELDKINSF 81
Cdd:cd14447     1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNSSEALE-------LSESGGEEFESEFFEALDAELEKVNEF 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 237845515   82 SK---REVEAILDQLAVALVIMWRLHAALT--LLRLAPDSPGYAEAQALLKR 128
Cdd:cd14447    74 YQellEELQELLKRLEALEPDLPALRGSLKeeLEDLRKELVESYSELEELER 125
DUF202 pfam02656
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 1075-1137 1.08e-13

Domain of unknown function (DUF202); This family consists of hypothetical proteins some of which are putative membrane proteins. No functional information or experimental verification of function is known. This domain is around 100 amino acids long.


Pssm-ID: 396980  Cd Length: 68  Bit Score: 66.87  E-value: 1.08e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 237845515  1075 KTFFANERTLLQWMNTAVLIATISITLMNFGN-----PVGRIAGLLMSPVAVFFIGYSFWVYLRRARA 1137
Cdd:pfam02656    1 RDGLANERTFLAWLRTSLALIALGVALLRFFLhggptGLALILGLILIVLGILTLLYGLRRYLRRVRA 68
PolyPPase_VTC4_like cd07751
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein ...
 669-827 1.24e-09

Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein VTC4, and similar proteins; Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2,-3, and -4 contain polyP polymerase domains. S. cerevisiae VTC4 belongs to this subgroup. For VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143623  Cd Length: 290  Bit Score: 60.84  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  669 AVQQRGVSPSVRTWFYRTEF-MSEDGVAWISVDEDIRFSREMNRTPPAN-QWIRSETEALSTDDVHPFPWGLLDVSfLVR 746
Cdd:cd07751   165 VILKRKLKPVVRTFYRRTAFqLPDDNRVRISLDTELCMIDERGRDGRRRtTLNDWPFKQLPDNEIVRFPYAVLEVK-LQT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  747 DNGVALPQhavqqakdfhplvgrddledFVADLRGLSTLTEVPGFSLFAHGTAYFYTPRlqalqarmsgyeqaVHLIPLW 826
Cdd:cd07751   244 QEGEEPPE--------------------WVEELLNSHLVEEVYKFSKFLHGCATLFPDK--------------VDSIPYW 289


                  .
gi 237845515  827 L 827
Cdd:cd07751   290 L 290
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 58-286 1.30e-09

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: 61.42  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    58 SIFRPPESRFQELLNHELDKINSFSKREVEAIldqlavalvimwrlhaaltllrlapdspgYAEAQALLKRLEQ-REQEI 136
Cdd:pfam03105  131 TTPLDSEDEFFERLDSELNKVNKFYKEKEEEF-----------------------------LERLEALNKQLEAlRDFRI 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   137 RnalVVYPQKRGRATEQDKAGSPSSN------------PRCRGVSDEPSSSSEERELGAEGDDFSSAGGKTSSRGEGDAK 204
Cdd:pfam03105  182 K---LIRESKSDLYRWREPFGLYSSDssvffstseldsGNSSESSVDDEVEEELERNGWISPIKSKDKKKRPSEALDKVK 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   205 --RRQGDEDGGEGEQDDAKR----SVAEALILLEKDVLEVEGVLEaqsqeivFLDSFVRLNFTGFRKITKKYDKHNQSSA 278
Cdd:pfam03105  259 tpDRTLKGFLDASRRDYLNRinkvNLRKAKKKLKKAFIELYRGLE-------LLKSYSELNRTAFRKILKKFDKVTSLNA 331


                   ....*...
gi 237845515   279 ASWYMSRV 286
Cdd:pfam03105  332 SKDYMKEV 339
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-287 2.83e-08

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 56.76  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    1 MKFSKQLSAQADLRYLNEYISYKDLKKAIKVITGSDVqvcTVQDVVSNFRQTNALTGSiFRPPESRFqellNHELDKINS 80
Cdd:COG5408     1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQL---SSYHGVSDNDETRDEAGE-PSNWRDRF----NHALKKELS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   81 FSKRE-----VEAILDQLAVALVIM--WRLHAA--LTLLRLAPDSPGYAE----AQALLKRLEQREQEIRNALVVYPQKR 147
Cdd:COG5408    73 PLQANyvakfFENYISEEAIKLDEFysQGQYIAykKREFRKISSKFFYSErkalVQKEENTASSNYDTFLNLQTDEGAYV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  148 GRATEQdkAGSPSSNPRCRGVSDEPSSSSEERELgaegdDFSSAGGKTSSRGEGDAKRRQGDEDGGEGEQDDAKRSVAEA 227
Cdd:COG5408   153 ADARKR--AEAKSYDPFDSLRIDTSKEGLTKRNL-----NLPDYEKIVSGTDEEVPSNDQDDEDQDFDYLAKKNDNTALL 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 237845515  228 LILL--------EKDVLEVEGVLEAQSQEIVfLDSFVRLNFTGFRKITKKYDKHNQSSAASWYMSRVV 287
Cdd:COG5408   226 DLSQfnfkivkyQKRSLLKKRIIELYIQLHQ-LKSFIELNYTGFSKITKKYDKTLHQNLRHEYMSRSV 292
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
 231-272 4.01e-08

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: 53.70  E-value: 4.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 237845515  231 LEKDVLEVEGVLEAQSQEIVF-------------LDSFVRLNFTGFRKITKKYDK 272
Cdd:cd14478    94 LLKDVEEFEEENYLYDSRISLkkriinlyvslseLKSYIELNRTGFSKILKKYDK 148
VTC pfam09359
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
 649-802 6.38e-04

VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins VTC2, VTC3 and VTC4. This domain is also found in a variety of bacterial proteins.


Pssm-ID: 401343  Cd Length: 235  Bit Score: 42.70  E-value: 6.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   649 ALTKQKrKADMLQVLQTVWDAVQQRGVSPSVRTWFYRTEFM-SEDGVAWISVDEDIRFSREmnrtppanqWIRSETEALS 727
Cdd:pfam09359  115 KLKEDG-KEKLKRLANEIQSFILEYNLQPVLRTSYRRTAFQiPGDDRVRITIDTNLRYIRE---------WHRLDIDKFL 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237845515   728 TD-DVHPFPWGLLDVsflvrdngvalpqhavqQAKDFHPLvgrddledFVADLRGLSTLTEVPGFSLFAHGTAYFY 802
Cdd:pfam09359  185 RKgEVSRFPYAVLEI-----------------KLKNKIPE--------WIEELLNSHLVEEVPKFSKYCHGVASLF 235
 
Name Accession Description Interval E-value
VTC1 COG5264
Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];
1066-1173 5.18e-28

Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227589  Cd Length: 126  Bit Score: 110.16  E-value: 5.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515 1066 SGPsVRVEPKTFFANERTLLQWMNTAVLIATISITLMNFGNPVGRIAGLLMSPVAVFFIGYSFWVYLRRARALERKEPIA 1145
Cdd:COG5264    18 AGP-VRVEPKVWFANERTFLSWLSVTVLLGGLGFALYNSGDRLGMISAYVFTIVAIFCGFYALMLYLKRAVNIRQRSAGP 96

                          90       100
                  ....*....|....*....|....*...
gi 237845515 1146 YNDKLGPSILVVTLMLSLSAVIALNLLY 1173
Cdd:COG5264    97 YDDRLGPTLVCVVLLVALIVNFFLAFKA 124
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-128 1.30e-14

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: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLSAQADLRYLNEYISYKDLKKAIKVITGSDVQVCTVQDVVSnfrqtnaLTGSIFRPPESRFQELLNHELDKINSF 81
Cdd:cd14447     1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNSSEALE-------LSESGGEEFESEFFEALDAELEKVNEF 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 237845515   82 SK---REVEAILDQLAVALVIMWRLHAALT--LLRLAPDSPGYAEAQALLKR 128
Cdd:cd14447    74 YQellEELQELLKRLEALEPDLPALRGSLKeeLEDLRKELVESYSELEELER 125
DUF202 pfam02656
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 1075-1137 1.08e-13

Domain of unknown function (DUF202); This family consists of hypothetical proteins some of which are putative membrane proteins. No functional information or experimental verification of function is known. This domain is around 100 amino acids long.


Pssm-ID: 396980  Cd Length: 68  Bit Score: 66.87  E-value: 1.08e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 237845515  1075 KTFFANERTLLQWMNTAVLIATISITLMNFGN-----PVGRIAGLLMSPVAVFFIGYSFWVYLRRARA 1137
Cdd:pfam02656    1 RDGLANERTFLAWLRTSLALIALGVALLRFFLhggptGLALILGLILIVLGILTLLYGLRRYLRRVRA 68
PolyPPase_VTC4_like cd07751
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein ...
 669-827 1.24e-09

Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein VTC4, and similar proteins; Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2,-3, and -4 contain polyP polymerase domains. S. cerevisiae VTC4 belongs to this subgroup. For VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143623  Cd Length: 290  Bit Score: 60.84  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  669 AVQQRGVSPSVRTWFYRTEF-MSEDGVAWISVDEDIRFSREMNRTPPAN-QWIRSETEALSTDDVHPFPWGLLDVSfLVR 746
Cdd:cd07751   165 VILKRKLKPVVRTFYRRTAFqLPDDNRVRISLDTELCMIDERGRDGRRRtTLNDWPFKQLPDNEIVRFPYAVLEVK-LQT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  747 DNGVALPQhavqqakdfhplvgrddledFVADLRGLSTLTEVPGFSLFAHGTAYFYTPRlqalqarmsgyeqaVHLIPLW 826
Cdd:cd07751   244 QEGEEPPE--------------------WVEELLNSHLVEEVYKFSKFLHGCATLFPDK--------------VDSIPYW 289


                  .
gi 237845515  827 L 827
Cdd:cd07751   290 L 290
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 58-286 1.30e-09

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: 61.42  E-value: 1.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    58 SIFRPPESRFQELLNHELDKINSFSKREVEAIldqlavalvimwrlhaaltllrlapdspgYAEAQALLKRLEQ-REQEI 136
Cdd:pfam03105  131 TTPLDSEDEFFERLDSELNKVNKFYKEKEEEF-----------------------------LERLEALNKQLEAlRDFRI 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   137 RnalVVYPQKRGRATEQDKAGSPSSN------------PRCRGVSDEPSSSSEERELGAEGDDFSSAGGKTSSRGEGDAK 204
Cdd:pfam03105  182 K---LIRESKSDLYRWREPFGLYSSDssvffstseldsGNSSESSVDDEVEEELERNGWISPIKSKDKKKRPSEALDKVK 258

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   205 --RRQGDEDGGEGEQDDAKR----SVAEALILLEKDVLEVEGVLEaqsqeivFLDSFVRLNFTGFRKITKKYDKHNQSSA 278
Cdd:pfam03105  259 tpDRTLKGFLDASRRDYLNRinkvNLRKAKKKLKKAFIELYRGLE-------LLKSYSELNRTAFRKILKKFDKVTSLNA 331


                   ....*...
gi 237845515   279 ASWYMSRV 286
Cdd:pfam03105  332 SKDYMKEV 339
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-287 2.83e-08

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 56.76  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    1 MKFSKQLSAQADLRYLNEYISYKDLKKAIKVITGSDVqvcTVQDVVSNFRQTNALTGSiFRPPESRFqellNHELDKINS 80
Cdd:COG5408     1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQL---SSYHGVSDNDETRDEAGE-PSNWRDRF----NHALKKELS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   81 FSKRE-----VEAILDQLAVALVIM--WRLHAA--LTLLRLAPDSPGYAE----AQALLKRLEQREQEIRNALVVYPQKR 147
Cdd:COG5408    73 PLQANyvakfFENYISEEAIKLDEFysQGQYIAykKREFRKISSKFFYSErkalVQKEENTASSNYDTFLNLQTDEGAYV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  148 GRATEQdkAGSPSSNPRCRGVSDEPSSSSEERELgaegdDFSSAGGKTSSRGEGDAKRRQGDEDGGEGEQDDAKRSVAEA 227
Cdd:COG5408   153 ADARKR--AEAKSYDPFDSLRIDTSKEGLTKRNL-----NLPDYEKIVSGTDEEVPSNDQDDEDQDFDYLAKKNDNTALL 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 237845515  228 LILL--------EKDVLEVEGVLEAQSQEIVfLDSFVRLNFTGFRKITKKYDKHNQSSAASWYMSRVV 287
Cdd:COG5408   226 DLSQfnfkivkyQKRSLLKKRIIELYIQLHQ-LKSFIELNYTGFSKITKKYDKTLHQNLRHEYMSRSV 292
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
 231-272 4.01e-08

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: 53.70  E-value: 4.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 237845515  231 LEKDVLEVEGVLEAQSQEIVF-------------LDSFVRLNFTGFRKITKKYDK 272
Cdd:cd14478    94 LLKDVEEFEEENYLYDSRISLkkriinlyvslseLKSYIELNRTGFSKILKKYDK 148
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
 2-81 5.14e-08

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: 53.43  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLSAQADlRYLNEY----ISYKDLKKAIKVITGSDVQVCTVQDVVSNFRQTNALTgsifrPPESRFQELLNHELDK 77
Cdd:cd14481     1 KFGKSLKRQIE-ETLPEWrdkfLSYKELKKLLKLISPGNADKPNSKRDRRGGGAARAMT-----KEEADFVRLLNAELDK 74


                  ....
gi 237845515   78 INSF 81
Cdd:cd14481    75 FNAF 78
YidH COG2149
Uncharacterized membrane protein YidH, DUF202 family [Function unknown];
1074-1169 6.04e-08

Uncharacterized membrane protein YidH, DUF202 family [Function unknown];


Pssm-ID: 441752  Cd Length: 126  Bit Score: 52.62  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515 1074 PKTFFANERTLLQWMNTA-------VLIATISI---TLMNFGNPVGRIAGLLMSPVAVFFIGYSFWVYLRRARALERKEP 1143
Cdd:COG2149    18 PRFHLANERTFLAWIRTAlaliafgFAIERFGLflrPLALSLPGLSRVLGLALVLLGALLAVLAYIRYRRVERALRRGEP 97

                          90       100
                  ....*....|....*....|....*.
gi 237845515 1144 IAYNdklgPSILVVTLMLSLSAVIAL 1169
Cdd:COG2149    98 LPSS----RLALLLAVAVALLGLLLL 119
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
 2-96 1.27e-05

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: 46.00  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLsaQADL----RYlnEYISYKDLKKAIKVITgSDVQVCTVQDvvsnfrqtnaltgsifrppESRFQELLNHELDK 77
Cdd:cd14480     1 KFGKTL--KSSIyppwKD--YYIDYDKLKKLLKERE-TDRGWWTEDD-------------------ERFFVELLEVELEK 56

                          90
                  ....*....|....*....
gi 237845515   78 INSFSKREVEAILDQLAVA 96
Cdd:cd14480    57 VYTFQKEKYSELRRRIDAC 75
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
 231-272 2.27e-05

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: 45.61  E-value: 2.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 237845515  231 LEKDVLEVEGVLEaqsqEIVF----LDSFVRLNFTGFRKITKKYDK 272
Cdd:cd14480    94 SEEDFKELEEELD----DILAdvhdLAKFTRLNYTGFLKIVKKHDK 135
PolyPPase_VTC2-3_like cd07892
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
 394-828 3.86e-05

Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins VTC-2, and -3 , and similar proteins; Saccharomyces cerevisiae VTC-1, -2, -3, and -4 comprise the membrane-integral VTC complex. VTC-2, -3, and -4 contain polyP polymerase domains. S. cerevisiae VTC-2,and -3 belong to this subgroup. For VTC4 it has been shown that this domain generates polyP from ATP by a phosphotransfer reaction releasing ADP. This activity is metal ion-dependent. The ATP gamma phosphate may be cleaved and then transferred to an acceptor phosphate to form polyP. PolyP is ubiquitous. In prokaryotes, it is a store of phosphate and energy. In eukaryotes, polyPs have roles in bone calcification, and osmoregulation, and in phosphate transport in the symbiosis of mycorrhizal fungi and plants. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143630  Cd Length: 303  Bit Score: 47.36  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  394 EDIKVTKYLIAPDELMKVKVLILKHLPLLAAGGIPMDDSVLCPFenssqavaaedfsaaleaaasllrtsgtasdkrear 473
Cdd:cd07892     5 DNFKSYKFWVHPDNLMEVKTRILRHLPVLVYNNQSSEDDDDVLG------------------------------------ 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  474 qslGGSRVPTWE-VYLDNEEFTYYTNTRTRRDSpdscrgvAPSrrvVRVRWQGLPSLNSagrQVALE-LSRPDSSIADpq 551
Cdd:cd07892    49 ---AGSEDPTITtLYFDNPNFDLYNDKLLKLNE-------APT---LRLRWTGKLSDKP---DIFVEkKTFDENTSSF-- 110

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  552 EDITTPLASnapdvassaftvilrqkqllqllhglitpsKLLDQLMD---EMEASaagvatgeganaTAASHRTGArgaa 628
Cdd:cd07892   111 EEDKLQLKE------------------------------KYINGFIFgkyKFEKK------------LQKMEKRGA---- 144

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  629 nrgegsgggggnrgsddravALTKQKRKADMLQvlqtvwDAVQQRGVSPSVRTWFYRTEFM--SEDGVAwISVDEDIRFS 706
Cdd:cd07892   145 --------------------DLENLKKDVENIQ------DFIRENKLQPVLRAVYTRTAFQipGDDRIR-VSIDSDIAFI 197

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  707 REMN-------RTPpaNQWIRSETEA--------LSTDDVHPFPWGLLDVSFLVRDNgvalpqhavQQAKdfHPLvgrdd 771
Cdd:cd07892   198 REDSfdkdrpiRDP--NDWHRTDIDDsnsnpfkfLRKGEYSKFPYSVLEIKVKESLN---------KNRK--HYE----- 259

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 237845515  772 ledFVADLRGLSTLTEVPGFSLFAHGTAYFYtprlqalqarmsGYEQAVHLIPLWLQ 828
Cdd:cd07892   260 ---WVNDLTNSHLVKEVPKFSKFVQGVASLF------------EEDDKLNILPFWLP 301
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
 250-272 9.78e-05

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: 44.20  E-value: 9.78e-05
                          10        20
                  ....*....|....*....|...
gi 237845515  250 VFLDSFVRLNFTGFRKITKKYDK 272
Cdd:cd14477   139 ILLQNYQNLNFTGFRKILKKHDK 161
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
 193-273 1.20e-04

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: 43.43  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  193 GKTSSRGEGDAKRRQGDEDGGEGEQD----DAKRSVAealillekdvlevegvleaqsQEIVFLDSFVRLNFTGFRKITK 268
Cdd:cd14479    70 GLLASRLEKLGEQREALQEQPDLSQIselrEAYRAVG---------------------LDLLKLLKFVELNATGLRKILK 128


                  ....*
gi 237845515  269 KYDKH 273
Cdd:cd14479   129 KFDKR 133
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
 2-272 3.79e-04

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


Pssm-ID: 269896 [Multi-domain]  Cd Length: 139  Bit Score: 42.17  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLSAQADLRYLNEYISYKDLKKAIKvitgsdvqvctvqdvvsnfrqtnaltgsifrppESRFQELLNHELDKINSF 81
Cdd:cd14475     1 KFAKYLEENLVPEWRKKYLDYKGGKKKIK---------------------------------AREFFEFLDSELDKVESF 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   82 SKreveaildqlavalvimWRLHaaltllrlapdspgyaEAQALLKRLEQREQEIRNAlvvypqkrgRATEQDKAGSPSS 161
Cdd:cd14475    48 YK-----------------EKED----------------EARERLDLLRDQLHELRDH---------RIQEADDGRRDYS 85

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515  162 NPRcrgvsdepsssseeRELGAEGDDFSSAggktssrgegdakRRQgdedggegeqddakrsvaealilLEKDVLEVEGV 241
Cdd:cd14475    86 RRP--------------EQNAHDPVSYRSA-------------RRK-----------------------LKKALQEYYRG 115

                         250       260       270
                  ....*....|....*....|....*....|.
gi 237845515  242 LEaqsqeivFLDSFVRLNFTGFRKITKKYDK 272
Cdd:cd14475   116 LE-------LLKSYRLLNRTAFRKINKKFDK 139
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
 2-97 5.95e-04

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: 41.48  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLSAQADLRYLNEYISYKDLKKAIKVITGSDVQVCTVqdvvsnfRQTNALTGSifrPPESRFQELLNHELDKINSF 81
Cdd:cd14476     1 KFGKEFESQMVPEWQEAYVDYKQLKKDLKRIQKFRDEYETT-------FLEAAEEGG---EYELVFFRRLDDELNKVNKF 70

                          90
                  ....*....|....*.
gi 237845515   82 SKREVEAILDQlAVAL 97
Cdd:cd14476    71 YRSKVEEVLKE-AAAL 85
VTC pfam09359
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
 649-802 6.38e-04

VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins VTC2, VTC3 and VTC4. This domain is also found in a variety of bacterial proteins.


Pssm-ID: 401343  Cd Length: 235  Bit Score: 42.70  E-value: 6.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515   649 ALTKQKrKADMLQVLQTVWDAVQQRGVSPSVRTWFYRTEFM-SEDGVAWISVDEDIRFSREmnrtppanqWIRSETEALS 727
Cdd:pfam09359  115 KLKEDG-KEKLKRLANEIQSFILEYNLQPVLRTSYRRTAFQiPGDDRVRITIDTNLRYIRE---------WHRLDIDKFL 184

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237845515   728 TD-DVHPFPWGLLDVsflvrdngvalpqhavqQAKDFHPLvgrddledFVADLRGLSTLTEVPGFSLFAHGTAYFY 802
Cdd:pfam09359  185 RKgEVSRFPYAVLEI-----------------KLKNKIPE--------WIEELLNSHLVEEVPKFSKYCHGVASLF 235
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
 222-272 1.75e-03

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: 40.70  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 237845515  222 RSVAEALILLEKDVLEvegvleaqsqeivfLDSFVRLNFTGFRKITKKYDK 272
Cdd:cd14483   123 VTLEEGFRQFERDLNK--------------LQQFVELNATGFSKILKKWDK 159
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
 2-131 3.42e-03

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: 39.54  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237845515    2 KFSKQLSAQADL--RYLNEYISYKDLKKAIK-VITGSdvqvctVQDVVSNFRQTNALTGSIFRPPES--RFQEL------ 70
Cdd:cd14483     1 KFGKYIQARQLElpEYSAYFLDYKALKKLIKsLAAPR------VAAAAALLAGGRPLSPDGTDESDAqtSLQANkaafff 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 237845515   71 -LNHELDKINSFS-KREVEaildqLAVAL--VIMWRLHAALTLLRLAPDSPGYAEAQALLKRLEQ 131
Cdd:cd14483    75 kLERELEKVNAFYlQKEAE-----LKLRLdtLLDKKRVLQSRGKLASKKSASFVTLEEGFRQFER 134
 
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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