NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|226463148|gb|EEH60426|]
View 

vacuolar transport chaperone protein [Micromonas pusilla CCMP1545]

Protein Classification

SPX and EXS domain-containing protein; SPX domain-containing protein( domain architecture ID 10199281)

SPX (Syg1, Pho81 and XPR1) and EXS (ERD1, XPR1, and SYG1) domain-containing protein similar to plant PHO1 family phosphate transporters| SPX (Syg1, Pho81 and XPR1) domain-containing protein may be involved in G-protein associated signal transduction

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PolyPPase_VTC4_like cd07751
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein ...
 288-603 2.36e-149

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: 441.03  E-value: 2.36e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 288 GAQDFVRTTRKYWVSPEDVSGVKQNIAQHLPVFLVERERVKGLVEAaagesgdgvapgfagltLPSHADSQMTNSVYLDN 367
Cdd:cd07751    1 PPQTFVRRTTKYWVHPRDVVPVKLAILKHLPVLVFNGSKEEEKEKE-----------------DVPPRDDSAITSVYFDN 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 368 VHLELYHARLKKAPRAIAIRLRWYGP-APTGSVYVERKTHRESWTGEESVKERFALPAAYIVPYLQCKHTWEKEESRLRA 446
Cdd:cd07751   64 ENLDLYHGRLERDEGAELIRLRWYGGmQDTDTVFVERKTHHESWTGEKSVKERFALKEKYVNSFLKGKYTVDKVFRKLRK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 447 QHAKndrerptSGAELKKIKTLFTEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLAMLVENPAGGPSCTAL 526
Cdd:cd07751  144 EGKK-------SEAEIEKLEALATEIQYVILKRKLKPVVRTFYRRTAFQLPDDNRVRISLDTELCMIDERGRDGRRRTTL 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 527 ERWyrdPSVPLHRTEVTRFPHAVLEIKLALGEGVAAPDWVNELVASGALTEVHKFSKFMHGCAVLFPDTAQEVPYWV 603
Cdd:cd07751  217 NDW---PFKQLPDNEIVRFPYAVLEVKLQTQEGEEPPEWVEELLNSHLVEEVYKFSKFLHGCATLFPDKVDSIPYWL 290
DUF202 super family cl09954
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 743-863 7.66e-19

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: 83.19  E-value: 7.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 743 SVPMRVEPKTFFANERTFLSWLHTAVLIGTIGAALVGvhlggspSGaphkdvhgnDRSTAPLVIAMTMLSASVCLcaYAT 822
Cdd:COG5264   18 AGPVRVEPKVWFANERTFLSWLSVTVLLGGLGFALYN-------SG---------DRLGMISAYVFTIVAIFCGF--YAL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226463148 823 WTFVWRGRAIAARRTVAFHDPTGPVVMGAIMMCAMVVVIIV 863
Cdd:COG5264   80 MLYLKRAVNIRQRSAGPYDDRLGPTLVCVVLLVALIVNFFL 120
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-228 2.60e-18

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: 82.23  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIVASRDEAAALgddagaerftppkslaqfsltlSPRKPQGNASAQATETR 81
Cdd:cd14447    1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNS----------------------SEALELSESGGEEFESE 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  82 FFELLDDDMDRVRDFVTSTLSRLKddvascaaEIDDAVRRDLPTIAATCGSKTSSiaslesvssvvaaaaaeggengsgs 161
Cdd:cd14447   59 FFEALDAELEKVNEFYQELLEELQ--------ELLKRLEALEPDLPALRGSLKEE------------------------- 105

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 162 asassgedqdqgspfstlsgdvveeatrvVDALRERLQRVQDEFLRIEKFANLNMMACYKILKKHDK 228
Cdd:cd14447  106 -----------------------------LEDLRKELVESYSELEELERFVELNYTAFRKILKKYDK 143
 
Name Accession Description Interval E-value
PolyPPase_VTC4_like cd07751
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein ...
 288-603 2.36e-149

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: 441.03  E-value: 2.36e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 288 GAQDFVRTTRKYWVSPEDVSGVKQNIAQHLPVFLVERERVKGLVEAaagesgdgvapgfagltLPSHADSQMTNSVYLDN 367
Cdd:cd07751    1 PPQTFVRRTTKYWVHPRDVVPVKLAILKHLPVLVFNGSKEEEKEKE-----------------DVPPRDDSAITSVYFDN 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 368 VHLELYHARLKKAPRAIAIRLRWYGP-APTGSVYVERKTHRESWTGEESVKERFALPAAYIVPYLQCKHTWEKEESRLRA 446
Cdd:cd07751   64 ENLDLYHGRLERDEGAELIRLRWYGGmQDTDTVFVERKTHHESWTGEKSVKERFALKEKYVNSFLKGKYTVDKVFRKLRK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 447 QHAKndrerptSGAELKKIKTLFTEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLAMLVENPAGGPSCTAL 526
Cdd:cd07751  144 EGKK-------SEAEIEKLEALATEIQYVILKRKLKPVVRTFYRRTAFQLPDDNRVRISLDTELCMIDERGRDGRRRTTL 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 527 ERWyrdPSVPLHRTEVTRFPHAVLEIKLALGEGVAAPDWVNELVASGALTEVHKFSKFMHGCAVLFPDTAQEVPYWV 603
Cdd:cd07751  217 NDW---PFKQLPDNEIVRFPYAVLEVKLQTQEGEEPPEWVEELLNSHLVEEVYKFSKFLHGCATLFPDKVDSIPYWL 290
VTC pfam09359
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
 293-592 1.27e-59

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: 202.95  E-value: 1.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  293 VRTTRKYWVSPEDVSGVKQNIAQHLPVflverervkgLVEAAAGESGDgvapgfagltlpshadsQMTNSVYLDNVHLEL 372
Cdd:pfam09359   1 NRRETKYWVHPDNLMELKTRILRHLPV----------LVYNKTPGSED-----------------YTITSLYFDNPDFDL 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  373 YHARLKKAPRAIAIRLRWYGPAPTGSVYVERKTHresWTGEESVKERFALPAAYIVPYLqckhtwEKEESRLRAQHAKND 452
Cdd:pfam09359  54 YNQKLSGREGREKIRLRWYGKLSDDDIFLEIKTK---WSGEVSSKRRLPLKEKYVLDFL------EGIIEKLKEDGKEKL 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  453 RErptsgaelkkiktLFTEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLAMLVEnpaggpsctalerWYRD 532
Cdd:pfam09359 125 KR-------------LANEIQSFILEYNLQPVLRTSYRRTAFQIPGDDRVRITIDTNLRYIRE-------------WHRL 178

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226463148  533 PSVP-LHRTEVTRFPHAVLEIKLalgeGVAAPDWVNELVASGALTEVHKFSKFMHGCAVLF 592
Cdd:pfam09359 179 DIDKfLRKGEVSRFPYAVLEIKL----KNKIPEWIEELLNSHLVEEVPKFSKYCHGVASLF 235
VTC1 COG5264
Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];
743-863 7.66e-19

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


Pssm-ID: 227589  Cd Length: 126  Bit Score: 83.19  E-value: 7.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 743 SVPMRVEPKTFFANERTFLSWLHTAVLIGTIGAALVGvhlggspSGaphkdvhgnDRSTAPLVIAMTMLSASVCLcaYAT 822
Cdd:COG5264   18 AGPVRVEPKVWFANERTFLSWLSVTVLLGGLGFALYN-------SG---------DRLGMISAYVFTIVAIFCGF--YAL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226463148 823 WTFVWRGRAIAARRTVAFHDPTGPVVMGAIMMCAMVVVIIV 863
Cdd:COG5264   80 MLYLKRAVNIRQRSAGPYDDRLGPTLVCVVLLVALIVNFFL 120
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-228 2.60e-18

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: 82.23  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIVASRDEAAALgddagaerftppkslaqfsltlSPRKPQGNASAQATETR 81
Cdd:cd14447    1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNS----------------------SEALELSESGGEEFESE 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  82 FFELLDDDMDRVRDFVTSTLSRLKddvascaaEIDDAVRRDLPTIAATCGSKTSSiaslesvssvvaaaaaeggengsgs 161
Cdd:cd14447   59 FFEALDAELEKVNEFYQELLEELQ--------ELLKRLEALEPDLPALRGSLKEE------------------------- 105

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 162 asassgedqdqgspfstlsgdvveeatrvVDALRERLQRVQDEFLRIEKFANLNMMACYKILKKHDK 228
Cdd:cd14447  106 -----------------------------LEDLRKELVESYSELEELERFVELNYTAFRKILKKYDK 143
COG5036 COG5036
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion ...
 292-584 2.06e-15

SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion transport and metabolism, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444047  Cd Length: 241  Bit Score: 76.57  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 292 FVRTTRKYWVSPEDVSGVKQNIAQHLPVFlverervkglveAAAGESGDGVapgfagltlpshadsqmTNSVYLDNVHLE 371
Cdd:COG5036    7 FNRYELKYLIPEEQADALREALKTYMEPD------------KYSDESGFYT-----------------IRSLYFDTPDLE 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 372 LYHARLKKAPRAIAIRLRWYG-PAPTGSVYVERKthreSWTGEESVKERFALPAAYIVPYLqcKHTWEKEESRLRAQHAK 450
Cdd:COG5036   58 LYRESIEGPKYREKLRLRSYGdPTPESPVFLEIK----KKVDGVVYKRRAPVPLEEARAFL--KGGSLPAHDNPSNKQLL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 451 NdrerptsgaelkkiktlftEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLamlvenpaggpsctaleRWy 530
Cdd:COG5036  132 R-------------------EIDYFLARYNLRPKVLVAYDREAFAGKDDGDLRITFDTNI-----------------RF- 174

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 226463148 531 RDPSVPLHRTEvTRFPH-----AVLEIKLalgeGVAAPDWVNELVASGALTEVhKFSKF 584
Cdd:COG5036  175 RDDDLRLDKGE-HGEPLvppgyVLLEIKY----DGRMPLWLSDLLSRLNLFRT-SFSKY 227
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 1-241 1.54e-13

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: 72.98  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148    1 MKFGQYLDENAVREWKEHYVRYNALKKVLKAIVA------------SRDEAAALGDDAGAERFTPPKSLAQFSLT----- 63
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRelestppssspsSSDSGSAASPSDSTTSLPLRDPLSRSSSLdrafg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   64 -LSPRKPQGNASAQAT----------------------------------------ETRFFELLDDDMDRVRDF------ 96
Cdd:pfam03105  81 gLVPSPPSSSSSSSSDsssssnssssssssspsllrrlpsesddssesyettpldsEDEFFERLDSELNKVNKFykekee 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   97 -VTSTLSRLKDDV----ASCAAEIDDAvRRDLPTIAATCGSKT--SSIASLESVSSVVAAAAAEGGENGSGSASASSGED 169
Cdd:pfam03105 161 eFLERLEALNKQLealrDFRIKLIRES-KSDLYRWREPFGLYSsdSSVFFSTSELDSGNSSESSVDDEVEEELERNGWIS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  170 QDQGSPFSTLSGDVVEEATRVVDALRERLQRVQDEFLR------------------IE---------KFANLNMMACYKI 222
Cdd:pfam03105 240 PIKSKDKKKRPSEALDKVKTPDRTLKGFLDASRRDYLNrinkvnlrkakkklkkafIElyrglellkSYSELNRTAFRKI 319

                         330
                  ....*....|....*....
gi 226463148  223 LKKHDKLCpHTVCCRYYLE 241
Cdd:pfam03105 320 LKKFDKVT-SLNASKDYMK 337
DUF202 pfam02656
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 751-831 1.24e-11

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: 60.70  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  751 KTFFANERTFLSWLHTAVLIGTIGAALVGVHLGGSPSGAPHkdvhgndrstaplVIAMTMLSASVCLCAYATWTFVWRGR 830
Cdd:pfam02656   1 RDGLANERTFLAWLRTSLALIALGVALLRFFLHGGPTGLAL-------------ILGLILIVLGILTLLYGLRRYLRRVR 67


                  .
gi 226463148  831 A 831
Cdd:pfam02656  68 A 68
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-32 1.06e-04

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 45.21  E-value: 1.06e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 226463148   1 MKFGQYLDENAVREWKEHYVRYNALKKVLKAI 32
Cdd:COG5408    1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSL 32
 
Name Accession Description Interval E-value
PolyPPase_VTC4_like cd07751
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein ...
 288-603 2.36e-149

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: 441.03  E-value: 2.36e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 288 GAQDFVRTTRKYWVSPEDVSGVKQNIAQHLPVFLVERERVKGLVEAaagesgdgvapgfagltLPSHADSQMTNSVYLDN 367
Cdd:cd07751    1 PPQTFVRRTTKYWVHPRDVVPVKLAILKHLPVLVFNGSKEEEKEKE-----------------DVPPRDDSAITSVYFDN 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 368 VHLELYHARLKKAPRAIAIRLRWYGP-APTGSVYVERKTHRESWTGEESVKERFALPAAYIVPYLQCKHTWEKEESRLRA 446
Cdd:cd07751   64 ENLDLYHGRLERDEGAELIRLRWYGGmQDTDTVFVERKTHHESWTGEKSVKERFALKEKYVNSFLKGKYTVDKVFRKLRK 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 447 QHAKndrerptSGAELKKIKTLFTEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLAMLVENPAGGPSCTAL 526
Cdd:cd07751  144 EGKK-------SEAEIEKLEALATEIQYVILKRKLKPVVRTFYRRTAFQLPDDNRVRISLDTELCMIDERGRDGRRRTTL 216

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 527 ERWyrdPSVPLHRTEVTRFPHAVLEIKLALGEGVAAPDWVNELVASGALTEVHKFSKFMHGCAVLFPDTAQEVPYWV 603
Cdd:cd07751  217 NDW---PFKQLPDNEIVRFPYAVLEVKLQTQEGEEPPEWVEELLNSHLVEEVYKFSKFLHGCATLFPDKVDSIPYWL 290
VTC pfam09359
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
 293-592 1.27e-59

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: 202.95  E-value: 1.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  293 VRTTRKYWVSPEDVSGVKQNIAQHLPVflverervkgLVEAAAGESGDgvapgfagltlpshadsQMTNSVYLDNVHLEL 372
Cdd:pfam09359   1 NRRETKYWVHPDNLMELKTRILRHLPV----------LVYNKTPGSED-----------------YTITSLYFDNPDFDL 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  373 YHARLKKAPRAIAIRLRWYGPAPTGSVYVERKTHresWTGEESVKERFALPAAYIVPYLqckhtwEKEESRLRAQHAKND 452
Cdd:pfam09359  54 YNQKLSGREGREKIRLRWYGKLSDDDIFLEIKTK---WSGEVSSKRRLPLKEKYVLDFL------EGIIEKLKEDGKEKL 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  453 RErptsgaelkkiktLFTEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLAMLVEnpaggpsctalerWYRD 532
Cdd:pfam09359 125 KR-------------LANEIQSFILEYNLQPVLRTSYRRTAFQIPGDDRVRITIDTNLRYIRE-------------WHRL 178

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226463148  533 PSVP-LHRTEVTRFPHAVLEIKLalgeGVAAPDWVNELVASGALTEVHKFSKFMHGCAVLF 592
Cdd:pfam09359 179 DIDKfLRKGEVSRFPYAVLEIKL----KNKIPEWIEELLNSHLVEEVPKFSKYCHGVASLF 235
PolyPPase_VTC2-3_like cd07892
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
 286-605 1.55e-53

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: 188.34  E-value: 1.55e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 286 RDGAQDFvrTTRKYWVSPEDVSGVKQNIAQHLPVflverervkgLVeaAAGESG-DGVAPGFAGLTLPShadsqmTNSVY 364
Cdd:cd07892    1 NSSDDNF--KSYKFWVHPDNLMEVKTRILRHLPV----------LV--YNNQSSeDDDDVLGAGSEDPT------ITTLY 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 365 LDNVHLELYHARLKKAPRAIAIRLRWYGP-APTGSVYVERKTHRESWTgeESVKERFALPAAYIVPYLQCKHTWEKEESR 443
Cdd:cd07892   61 FDNPNFDLYNDKLLKLNEAPTLRLRWTGKlSDKPDIFVEKKTFDENTS--SFEEDKLQLKEKYINGFIFGKYKFEKKLQK 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 444 lraqhakndRERPtsGAELKKIKTLFTEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLAMLVEN------P 517
Cdd:cd07892  139 ---------MEKR--GADLENLKKDVENIQDFIRENKLQPVLRAVYTRTAFQIPGDDRIRVSIDSDIAFIREDsfdkdrP 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 518 AGGPsctalERWYR---DPSVP-----LHRTEVTRFPHAVLEIKLALGEGVAA--PDWVNELVASGALTEVHKFSKFMHG 587
Cdd:cd07892  208 IRDP-----NDWHRtdiDDSNSnpfkfLRKGEYSKFPYSVLEIKVKESLNKNRkhYEWVNDLTNSHLVKEVPKFSKFVQG 282

                        330       340
                 ....*....|....*....|
gi 226463148 588 CAVLF--PDTAQEVPYWVDD 605
Cdd:cd07892  283 VASLFeeDDKLNILPFWLPD 302
PolyPPase_VTC_like cd07750
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
 294-584 1.15e-25

Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins VTC-2, -3 and- 4, 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. For S. cerevisiae 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: 143622  Cd Length: 214  Bit Score: 105.86  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 294 RTTRKYWVSPEDVSGVKQNIAQHLPVFLVERERVkglveaaagesgdgvapgfagltlpshadsQMTNSVYLDNVHLELY 373
Cdd:cd07750    1 RYERKYLVPASQLEALLAALKPHLRVDEYAGNRD------------------------------YTIRSLYFDTPDLDLY 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 374 HARLKKAPRAIAIRLRWYGPApTGSVYVERKTHRESWTgeesVKERFALPAAYIVPYLQCKHTWEKEESRLraqhakndr 453
Cdd:cd07750   51 REKLNGRRRREKVRIRSYGDS-DGLIFLEVKTKRGRVT----YKRRLPLSPEDAERLLAGGYFFLLESQDP--------- 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 454 erptsgaelkkiktLFTEVQRAIESKQLQPTLRTVYMRTAFQVPyDASVRCSLDTSLamlvenpaggpsctalerWYRDP 533
Cdd:cd07750  117 --------------LAEEFYFRMRYKQLRPVLLVSYRREALVSP-DGGVRITFDTNL------------------RYRDE 163

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 226463148 534 S----VPLHRTEVTRFPHAVLEIKlALGEGvaaPDWVNELVASGALTEVhKFSKF 584
Cdd:cd07750  164 DgdlfSGNLGTPILPPDLVILEVK-YDGAL---PLWLADLLSSHGLEPT-SFSKY 213
VTC1 COG5264
Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];
743-863 7.66e-19

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


Pssm-ID: 227589  Cd Length: 126  Bit Score: 83.19  E-value: 7.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 743 SVPMRVEPKTFFANERTFLSWLHTAVLIGTIGAALVGvhlggspSGaphkdvhgnDRSTAPLVIAMTMLSASVCLcaYAT 822
Cdd:COG5264   18 AGPVRVEPKVWFANERTFLSWLSVTVLLGGLGFALYN-------SG---------DRLGMISAYVFTIVAIFCGF--YAL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226463148 823 WTFVWRGRAIAARRTVAFHDPTGPVVMGAIMMCAMVVVIIV 863
Cdd:COG5264   80 MLYLKRAVNIRQRSAGPYDDRLGPTLVCVVLLVALIVNFFL 120
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-228 2.60e-18

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: 82.23  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIVASRDEAAALgddagaerftppkslaqfsltlSPRKPQGNASAQATETR 81
Cdd:cd14447    1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNS----------------------SEALELSESGGEEFESE 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  82 FFELLDDDMDRVRDFVTSTLSRLKddvascaaEIDDAVRRDLPTIAATCGSKTSSiaslesvssvvaaaaaeggengsgs 161
Cdd:cd14447   59 FFEALDAELEKVNEFYQELLEELQ--------ELLKRLEALEPDLPALRGSLKEE------------------------- 105

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 162 asassgedqdqgspfstlsgdvveeatrvVDALRERLQRVQDEFLRIEKFANLNMMACYKILKKHDK 228
Cdd:cd14447  106 -----------------------------LEDLRKELVESYSELEELERFVELNYTAFRKILKKYDK 143
COG5036 COG5036
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion ...
 292-584 2.06e-15

SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion transport and metabolism, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444047  Cd Length: 241  Bit Score: 76.57  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 292 FVRTTRKYWVSPEDVSGVKQNIAQHLPVFlverervkglveAAAGESGDGVapgfagltlpshadsqmTNSVYLDNVHLE 371
Cdd:COG5036    7 FNRYELKYLIPEEQADALREALKTYMEPD------------KYSDESGFYT-----------------IRSLYFDTPDLE 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 372 LYHARLKKAPRAIAIRLRWYG-PAPTGSVYVERKthreSWTGEESVKERFALPAAYIVPYLqcKHTWEKEESRLRAQHAK 450
Cdd:COG5036   58 LYRESIEGPKYREKLRLRSYGdPTPESPVFLEIK----KKVDGVVYKRRAPVPLEEARAFL--KGGSLPAHDNPSNKQLL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 451 NdrerptsgaelkkiktlftEVQRAIESKQLQPTLRTVYMRTAFQVPYDASVRCSLDTSLamlvenpaggpsctaleRWy 530
Cdd:COG5036  132 R-------------------EIDYFLARYNLRPKVLVAYDREAFAGKDDGDLRITFDTNI-----------------RF- 174

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 226463148 531 RDPSVPLHRTEvTRFPH-----AVLEIKLalgeGVAAPDWVNELVASGALTEVhKFSKF 584
Cdd:COG5036  175 RDDDLRLDKGE-HGEPLvppgyVLLEIKY----DGRMPLWLSDLLSRLNLFRT-SFSKY 227
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 1-241 1.54e-13

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: 72.98  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148    1 MKFGQYLDENAVREWKEHYVRYNALKKVLKAIVA------------SRDEAAALGDDAGAERFTPPKSLAQFSLT----- 63
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRelestppssspsSSDSGSAASPSDSTTSLPLRDPLSRSSSLdrafg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   64 -LSPRKPQGNASAQAT----------------------------------------ETRFFELLDDDMDRVRDF------ 96
Cdd:pfam03105  81 gLVPSPPSSSSSSSSDsssssnssssssssspsllrrlpsesddssesyettpldsEDEFFERLDSELNKVNKFykekee 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   97 -VTSTLSRLKDDV----ASCAAEIDDAvRRDLPTIAATCGSKT--SSIASLESVSSVVAAAAAEGGENGSGSASASSGED 169
Cdd:pfam03105 161 eFLERLEALNKQLealrDFRIKLIRES-KSDLYRWREPFGLYSsdSSVFFSTSELDSGNSSESSVDDEVEEELERNGWIS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  170 QDQGSPFSTLSGDVVEEATRVVDALRERLQRVQDEFLR------------------IE---------KFANLNMMACYKI 222
Cdd:pfam03105 240 PIKSKDKKKRPSEALDKVKTPDRTLKGFLDASRRDYLNrinkvnlrkakkklkkafIElyrglellkSYSELNRTAFRKI 319

                         330
                  ....*....|....*....
gi 226463148  223 LKKHDKLCpHTVCCRYYLE 241
Cdd:pfam03105 320 LKKFDKVT-SLNASKDYMK 337
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
 2-228 2.32e-12

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: 64.87  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIVASRDEaaalgddagaerFTppkslaqfsltlsprkpqgnasaQATETR 81
Cdd:cd14480    1 KFGKTLKSSIYPPWKDYYIDYDKLKKLLKERETDRGW------------WT-----------------------EDDERF 45

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  82 FFELLDDDMDRVRDFVTSTLSRLKDDVASCAAEIDDAVRRDlptiaatcgsktssiaslesvssvvaaaaaeggengsgs 161
Cdd:cd14480   46 FVELLEVELEKVYTFQKEKYSELRRRIDACEKKVKELVSNL--------------------------------------- 86

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 162 asassgedqdqgspfstlSGDVVEEATRVVDALRERLQRVQDEFLRIEKFANLNMMACYKILKKHDK 228
Cdd:cd14480   87 ------------------DSSEDDPSEEDFKELEEELDDILADVHDLAKFTRLNYTGFLKIVKKHDK 135
DUF202 pfam02656
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 751-831 1.24e-11

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: 60.70  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  751 KTFFANERTFLSWLHTAVLIGTIGAALVGVHLGGSPSGAPHkdvhgndrstaplVIAMTMLSASVCLCAYATWTFVWRGR 830
Cdd:pfam02656   1 RDGLANERTFLAWLRTSLALIALGVALLRFFLHGGPTGLAL-------------ILGLILIVLGILTLLYGLRRYLRRVR 67


                  .
gi 226463148  831 A 831
Cdd:pfam02656  68 A 68
YidH COG2149
Uncharacterized membrane protein YidH, DUF202 family [Function unknown];
750-866 7.87e-10

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


Pssm-ID: 441752  Cd Length: 126  Bit Score: 57.63  E-value: 7.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148 750 PKTFFANERTFLSWLHTAV-LIGtIGAALVGVHLGGSPSGAPHkdvhgndrSTAPLVIAMTMLSASVCLCAYATWTFVWR 828
Cdd:COG2149   18 PRFHLANERTFLAWIRTALaLIA-FGFAIERFGLFLRPLALSL--------PGLSRVLGLALVLLGALLAVLAYIRYRRV 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 226463148 829 GRAIaaRRTVAFHDPTGPVVMGAIMMCAMVVVIIVTIL 866
Cdd:COG2149   89 ERAL--RRGEPLPSSRLALLLAVAVALLGLLLLVYLLL 124
SPX_YDR089W cd14474
SPX domain of the yeast protein YDR089W and related proteins; This region has been named the ...
 2-228 3.87e-06

SPX domain of the yeast protein YDR089W and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The uncharacterized yeast protein YDR089W has not been shown to be involved in phosphate homeostasis, in contrast to most of the other SPX-domain containing proteins.


Pssm-ID: 269895 [Multi-domain]  Cd Length: 144  Bit Score: 47.23  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIvASRDEAAALGDDAGAERFtppkslaqfsltlsprkpqgnasaqatETR 81
Cdd:cd14474    1 KFGEQLLQRSVPEWKLYNIDYNELKHLIKEH-TTRDQGTAIAIPSALEKF---------------------------EDS 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148  82 FFELLDDDMDRVRDFVTSTlsrlkddvascAAEIDdavRRdLPTIAatcgsktSSIASLesvssvvaaaaaeggengsgs 161
Cdd:cd14474   53 LYNEFCEQFDRVNLFVSSK-----------ADEIS---RR-LEHLE-------SSILRL--------------------- 89

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463148 162 asaSSGEDQDQGSPFStlsgdvveeATRVVDALRERLQRVQDEFLRIEKFANLNMMACYKILKKHDK 228
Cdd:cd14474   90 ---LERSASNSGSRRR---------QKRRLAKIEQELLRCGEELQKLSRFIIAQKIAFRKILKKYKK 144
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
 2-123 8.85e-06

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: 46.49  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLD---ENAVREWKEHYVRYNALKKVLKAIvasrdeaaalgddagaerftPPKSLAQFSLTLSPRKPQGNASAQAT 78
Cdd:cd14481    1 KFGKSLKrqiEETLPEWRDKFLSYKELKKLLKLI--------------------SPGNADKPNSKRDRRGGGAARAMTKE 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226463148  79 ETRFFELLDDDMDRVRDFVTS-------TLSRLKDDVASCAAEIDD------AVRRDL 123
Cdd:cd14481   61 EADFVRLLNAELDKFNAFFVEkeeeyviRLKELQDRVAEAKETPRDsneelmRIRREI 118
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
 2-31 1.45e-05

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: 45.63  E-value: 1.45e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKA 31
Cdd:cd14475    1 KFAKYLEENLVPEWRKKYLDYKGGKKKIKA 30
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
 2-38 1.80e-05

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: 45.33  E-value: 1.80e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIVASRDE 38
Cdd:cd14476    1 KFGKEFESQMVPEWQEAYVDYKQLKKDLKRIQKFRDE 37
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
 1-34 6.37e-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: 43.81  E-value: 6.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 226463148   1 MKFGQYLDENAVREWKEHYVRYNALKKVLKAIVA 34
Cdd:cd14479    1 VNFGKKLKEDQIPEWEGYYINYKLLKKKVKQYVQ 34
SPX_GDE1_like cd14484
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ...
 2-38 7.53e-05

SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The yeast protein Gde1/Ypl110c is similar to both, NUC-2 and Pho81, in sharing their multi-domain architecture, which includes the SPX N-terminal domain followed by several ankyrin repeats and a C-terminal glycerophosphodiester phosphodiesterase domain (GDPD). Gde1 hydrolyzes intracellular glycerophosphocholine into glycerolphosphate and choline, and plays a role in the utilization of glycerophosphocholine as a source for phosphate.


Pssm-ID: 269905 [Multi-domain]  Cd Length: 134  Bit Score: 43.29  E-value: 7.53e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIVASRDE 38
Cdd:cd14484    1 KFGKNLPRNQVPEWSSSYINYKGLKKLIKAIAEQQKE 37
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-32 1.06e-04

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 45.21  E-value: 1.06e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 226463148   1 MKFGQYLDENAVREWKEHYVRYNALKKVLKAI 32
Cdd:COG5408    1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSL 32
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
 2-110 2.12e-04

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: 42.52  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVL----KAIVASRDEAAALGDDAGAERftppkslaqfsltlsprkpqGNASAQA 77
Cdd:cd14478    1 KFSHSLQFNAVPEWSDHYIAYSNLKKLIyqleKDQLQLQNGGDDEEEEESSLL--------------------LLSTDED 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 226463148  78 TETRFFELLDDDMDRVRDFVTST-------LSRLKDDVAS 110
Cdd:cd14478   61 PDDVFVRALDKELEKIDSFYKEKeaelyaeVDELLKDVEE 100
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
 2-96 6.66e-04

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: 41.08  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463148   2 KFGQYLDENAVR--EWKEHYVRYNALKKVLKAIVAsrdeaaalgddagaerfTPPKSLAQFSLTLSPRKPQGN------A 73
Cdd:cd14483    1 KFGKYIQARQLElpEYSAYFLDYKALKKLIKSLAA-----------------PRVAAAAALLAGGRPLSPDGTdesdaqT 63

                         90       100
                 ....*....|....*....|...
gi 226463148  74 SAQATETRFFELLDDDMDRVRDF 96
Cdd:cd14483   64 SLQANKAAFFFKLERELEKVNAF 86
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
 2-33 6.02e-03

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: 38.42  E-value: 6.02e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 226463148   2 KFGQYLDENAVREWKEHYVRYNALKKVLKAIV 33
Cdd:cd14477    1 KFGEHLSAHITPEWRKQYINYEELKAMLYAAV 32
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH