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Conserved domains on  [gi|2088002125|gb|KAG9385055|]
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SPX domain-containing protein [Pyrenophora tritici-repentis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PolyPPase_VTC2-3_like cd07892
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
 218-512 3.41e-180

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: 518.84  E-value: 3.41e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 218 NAVGEDFTSYKFWVHMDNLFEVKTVILRRLPVLVYNPQTSKVAE----GTQRDPTITSIYFDNPNFSLYTDKVNGKPDAA 293
Cdd:cd07892     1 NSSDDNFKSYKFWVHPDNLMEVKTRILRHLPVLVYNNQSSEDDDdvlgAGSEDPTITTLYFDNPNFDLYNDKLLKLNEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 294 SLRLRWYGHLNEKPEIVFEKKVIKEG-DAAEEVRFPIKAKYVQSFLEDHYHMEKSIEKMEYRpnkdQKKLDNFKKAVTDI 372
Cdd:cd07892    81 TLRLRWTGKLSDKPDIFVEKKTFDENtSSFEEDKLQLKEKYINGFIFGKYKFEKKLQKMEKR----GADLENLKKDVENI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 373 QGFIKEQKLQPMVRANYTRTAFQIPGDDRVRISLDTNLALIREDALDLDRPCRDPDDWHRRDIDNAQmEFPFKAIKKGEI 452
Cdd:cd07892   157 QDFIRENKLQPVLRAVYTRTAFQIPGDDRIRVSIDSDIAFIREDSFDKDRPIRDPNDWHRTDIDDSN-SNPFKFLRKGEY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2088002125 453 HKFPYALLEIKVKG-----MKKYEWIEDLMHSHLVKESPRFSKFVHGVAKLFE--DNVNTFPFWLSE 512
Cdd:cd07892   236 SKFPYSVLEIKVKEslnknRKHYEWVNDLTNSHLVKEVPKFSKFVQGVASLFEedDKLNILPFWLPD 302
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
 2-160 1.34e-49

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: 170.80  E-value: 1.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSVYAPWKDKYIDYDKLKKLLKDNEDDDSWTADDESAFVDELANVQLEKVHNFITDISQKLRDRTSACEKKLE 81
Cdd:cd14480     1 KFGKTLKSSIYPPWKDYYIDYDKLKKLLKERETDRGWWTEDDERFFVELLEVELEKVYTFQKEKYSELRRRIDACEKKVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2088002125  82 PLaigiqddkenkdsqpegasadagdATRKPEPSQQEREKLLKEVLSELDNITKETKELEAFSRINFTAVIKATKKHDK 160
Cdd:cd14480    81 EL------------------------VSNLDSSEDDPSEEDFKELEEELDDILADVHDLAKFTRLNYTGFLKIVKKHDK 135
DUF202 super family cl09954
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 655-780 6.13e-39

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: 140.59  E-value: 6.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 655 IQLPPGIRDPGVWIKDQGPVRVEAKVWLANQRTFIKWQHVSVLLASLSLGLYNAAGEannIARALAVVYTCIAAFTLAWG 734
Cdd:COG5264     2 SVLPPLVKKPVPGKRIAGPVRVEPKVWFANERTFLSWLSVTVLLGGLGFALYNSGDR---LGMISAYVFTIVAIFCGFYA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2088002125 735 YGMYVYRAKLIRERSGKDFDAITGPLVVCVGLAVALCLNFGFKYNA 780
Cdd:COG5264    79 LMLYLKRAVNIRQRSAGPYDDRLGPTLVCVVLLVALIVNFFLAFKA 124
 
Name Accession Description Interval E-value
PolyPPase_VTC2-3_like cd07892
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
 218-512 3.41e-180

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: 518.84  E-value: 3.41e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 218 NAVGEDFTSYKFWVHMDNLFEVKTVILRRLPVLVYNPQTSKVAE----GTQRDPTITSIYFDNPNFSLYTDKVNGKPDAA 293
Cdd:cd07892     1 NSSDDNFKSYKFWVHPDNLMEVKTRILRHLPVLVYNNQSSEDDDdvlgAGSEDPTITTLYFDNPNFDLYNDKLLKLNEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 294 SLRLRWYGHLNEKPEIVFEKKVIKEG-DAAEEVRFPIKAKYVQSFLEDHYHMEKSIEKMEYRpnkdQKKLDNFKKAVTDI 372
Cdd:cd07892    81 TLRLRWTGKLSDKPDIFVEKKTFDENtSSFEEDKLQLKEKYINGFIFGKYKFEKKLQKMEKR----GADLENLKKDVENI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 373 QGFIKEQKLQPMVRANYTRTAFQIPGDDRVRISLDTNLALIREDALDLDRPCRDPDDWHRRDIDNAQmEFPFKAIKKGEI 452
Cdd:cd07892   157 QDFIRENKLQPVLRAVYTRTAFQIPGDDRIRVSIDSDIAFIREDSFDKDRPIRDPNDWHRTDIDDSN-SNPFKFLRKGEY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2088002125 453 HKFPYALLEIKVKG-----MKKYEWIEDLMHSHLVKESPRFSKFVHGVAKLFE--DNVNTFPFWLSE 512
Cdd:cd07892   236 SKFPYSVLEIKVKEslnknRKHYEWVNDLTNSHLVKEVPKFSKFVQGVASLFEedDKLNILPFWLPD 302
VTC pfam09359
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
 224-499 1.00e-88

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: 279.99  E-value: 1.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 224 FTSYKFWVHMDNLFEVKTVILRRLPVLVYNPQTSKVaegtqrDPTITSIYFDNPNFSLYTDKVNGKPDAASLRLRWYGHL 303
Cdd:pfam09359   2 RRETKYWVHPDNLMELKTRILRHLPVLVYNKTPGSE------DYTITSLYFDNPDFDLYNQKLSGREGREKIRLRWYGKL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 304 NEKPeIVFEKKVIKEGDAAEEVRFPIKAKYVQSFLEdhyhmeKSIEKMeyrpnKDQKKlDNFKKAVTDIQGFIKEQKLQP 383
Cdd:pfam09359  76 SDDD-IFLEIKTKWSGEVSSKRRLPLKEKYVLDFLE------GIIEKL-----KEDGK-EKLKRLANEIQSFILEYNLQP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 384 MVRANYTRTAFQIPGDDRVRISLDTNLALIREdaldldrpcrdpddWHRRDIDnaqmefpfKAIKKGEIHKFPYALLEIK 463
Cdd:pfam09359 143 VLRTSYRRTAFQIPGDDRVRITIDTNLRYIRE--------------WHRLDID--------KFLRKGEVSRFPYAVLEIK 200

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2088002125 464 VKGmKKYEWIEDLMHSHLVKESPRFSKFVHGVAKLF 499
Cdd:pfam09359 201 LKN-KIPEWIEELLNSHLVEEVPKFSKYCHGVASLF 235
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
 2-160 1.34e-49

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: 170.80  E-value: 1.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSVYAPWKDKYIDYDKLKKLLKDNEDDDSWTADDESAFVDELANVQLEKVHNFITDISQKLRDRTSACEKKLE 81
Cdd:cd14480     1 KFGKTLKSSIYPPWKDYYIDYDKLKKLLKERETDRGWWTEDDERFFVELLEVELEKVYTFQKEKYSELRRRIDACEKKVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2088002125  82 PLaigiqddkenkdsqpegasadagdATRKPEPSQQEREKLLKEVLSELDNITKETKELEAFSRINFTAVIKATKKHDK 160
Cdd:cd14480    81 EL------------------------VSNLDSSEDDPSEEDFKELEEELDDILADVHDLAKFTRLNYTGFLKIVKKHDK 135
VTC1 COG5264
Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];
655-780 6.13e-39

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


Pssm-ID: 227589  Cd Length: 126  Bit Score: 140.59  E-value: 6.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 655 IQLPPGIRDPGVWIKDQGPVRVEAKVWLANQRTFIKWQHVSVLLASLSLGLYNAAGEannIARALAVVYTCIAAFTLAWG 734
Cdd:COG5264     2 SVLPPLVKKPVPGKRIAGPVRVEPKVWFANERTFLSWLSVTVLLGGLGFALYNSGDR---LGMISAYVFTIVAIFCGFYA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2088002125 735 YGMYVYRAKLIRERSGKDFDAITGPLVVCVGLAVALCLNFGFKYNA 780
Cdd:COG5264    79 LMLYLKRAVNIRQRSAGPYDDRLGPTLVCVVLLVALIVNFFLAFKA 124
COG5036 COG5036
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion ...
 227-495 8.36e-23

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: 98.14  E-value: 8.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 227 YKFWVHMDNLFEVKTVILRRLPVLVYNPQtskvaegtQRDPTITSIYFDNPNFSLYTDKVNGKPDAASLRLRWYGHLNEK 306
Cdd:COG5036    12 LKYLIPEEQADALREALKTYMEPDKYSDE--------SGFYTIRSLYFDTPDLELYRESIEGPKYREKLRLRSYGDPTPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 307 PEIVFEKK------VIKEgdaaeevRFPIKAKYVQSFLEdhyhmeksiekmeyRPNKDQKKLDNFKKAVTDIQGFIKEQK 380
Cdd:COG5036    84 SPVFLEIKkkvdgvVYKR-------RAPVPLEEARAFLK--------------GGSLPAHDNPSNKQLLREIDYFLARYN 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 381 LQPMVRANYTRTAFQIPGDDRVRISLDTNLaLIREDALDLDRPcrdpdDWHRRDIDNaqmefpfkaikkgeihkfPYALL 460
Cdd:COG5036   143 LRPKVLVAYDREAFAGKDDGDLRITFDTNI-RFRDDDLRLDKG-----EHGEPLVPP------------------GYVLL 198

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2088002125 461 EIKVKGMKKYeWIEDLM-HSHLVKESprFSKFVHGV 495
Cdd:COG5036   199 EIKYDGRMPL-WLSDLLsRLNLFRTS--FSKYGNGY 231
DUF202 pfam02656
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 679-743 8.52e-14

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: 8.52e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2088002125 679 KVWLANQRTFIKWQHVSVLLASLSLGLYNAAGEANN--IARALAVVYTCIAAFTLAWGYGMYVYRAK 743
Cdd:pfam02656   1 RDGLANERTFLAWLRTSLALIALGVALLRFFLHGGPtgLALILGLILIVLGILTLLYGLRRYLRRVR 67
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 1-147 2.89e-05

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: 47.17  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   1 MKFGTTLRKSVYAPWKDKYIDYDKLKKLLK-------DNEDDDSWTADDESAFVDELANVQLEKVHNFITDISQKLRDRT 73
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKkiqreleSTPPSSSPSSSDSGSAASPSDSTTSLPLRDPLSRSSSLDRAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  74 SACEKKLEPLAIGIQDDKENKDSQPEGAS----------ADAGDATRKPEPSQQEREKLLKEVL-SELDNITK--ETKEL 140
Cdd:pfam03105  81 GLVPSPPSSSSSSSSDSSSSSNSSSSSSSsspsllrrlpSESDDSSESYETTPLDSEDEFFERLdSELNKVNKfyKEKEE 160


                  ....*..
gi 2088002125 141 EAFSRIN 147
Cdd:pfam03105 161 EFLERLE 167
 
Name Accession Description Interval E-value
PolyPPase_VTC2-3_like cd07892
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
 218-512 3.41e-180

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: 518.84  E-value: 3.41e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 218 NAVGEDFTSYKFWVHMDNLFEVKTVILRRLPVLVYNPQTSKVAE----GTQRDPTITSIYFDNPNFSLYTDKVNGKPDAA 293
Cdd:cd07892     1 NSSDDNFKSYKFWVHPDNLMEVKTRILRHLPVLVYNNQSSEDDDdvlgAGSEDPTITTLYFDNPNFDLYNDKLLKLNEAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 294 SLRLRWYGHLNEKPEIVFEKKVIKEG-DAAEEVRFPIKAKYVQSFLEDHYHMEKSIEKMEYRpnkdQKKLDNFKKAVTDI 372
Cdd:cd07892    81 TLRLRWTGKLSDKPDIFVEKKTFDENtSSFEEDKLQLKEKYINGFIFGKYKFEKKLQKMEKR----GADLENLKKDVENI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 373 QGFIKEQKLQPMVRANYTRTAFQIPGDDRVRISLDTNLALIREDALDLDRPCRDPDDWHRRDIDNAQmEFPFKAIKKGEI 452
Cdd:cd07892   157 QDFIRENKLQPVLRAVYTRTAFQIPGDDRIRVSIDSDIAFIREDSFDKDRPIRDPNDWHRTDIDDSN-SNPFKFLRKGEY 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2088002125 453 HKFPYALLEIKVKG-----MKKYEWIEDLMHSHLVKESPRFSKFVHGVAKLFE--DNVNTFPFWLSE 512
Cdd:cd07892   236 SKFPYSVLEIKVKEslnknRKHYEWVNDLTNSHLVKEVPKFSKFVQGVASLFEedDKLNILPFWLPD 302
VTC pfam09359
VTC domain; This presumed domain is found in the yeast vacuolar transport chaperone proteins ...
 224-499 1.00e-88

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: 279.99  E-value: 1.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 224 FTSYKFWVHMDNLFEVKTVILRRLPVLVYNPQTSKVaegtqrDPTITSIYFDNPNFSLYTDKVNGKPDAASLRLRWYGHL 303
Cdd:pfam09359   2 RRETKYWVHPDNLMELKTRILRHLPVLVYNKTPGSE------DYTITSLYFDNPDFDLYNQKLSGREGREKIRLRWYGKL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 304 NEKPeIVFEKKVIKEGDAAEEVRFPIKAKYVQSFLEdhyhmeKSIEKMeyrpnKDQKKlDNFKKAVTDIQGFIKEQKLQP 383
Cdd:pfam09359  76 SDDD-IFLEIKTKWSGEVSSKRRLPLKEKYVLDFLE------GIIEKL-----KEDGK-EKLKRLANEIQSFILEYNLQP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 384 MVRANYTRTAFQIPGDDRVRISLDTNLALIREdaldldrpcrdpddWHRRDIDnaqmefpfKAIKKGEIHKFPYALLEIK 463
Cdd:pfam09359 143 VLRTSYRRTAFQIPGDDRVRITIDTNLRYIRE--------------WHRLDID--------KFLRKGEVSRFPYAVLEIK 200

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2088002125 464 VKGmKKYEWIEDLMHSHLVKESPRFSKFVHGVAKLF 499
Cdd:pfam09359 201 LKN-KIPEWIEELLNSHLVEEVPKFSKYCHGVASLF 235
PolyPPase_VTC4_like cd07751
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) protein ...
 225-510 3.78e-82

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: 264.61  E-value: 3.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 225 TSYKFWVHMDNLFEVKTVILRRLPVLVYNPQTSKVAEGTQRDPT----ITSIYFDNPNFSLYTDKVNGKPDAASLRLRWY 300
Cdd:cd07751     8 RTTKYWVHPRDVVPVKLAILKHLPVLVFNGSKEEEKEKEDVPPRddsaITSVYFDNENLDLYHGRLERDEGAELIRLRWY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 301 GHLNEKPEIVFEKKVIKE---GDAAEEVRFPIKAKYVQSFLEDHYHMEKSIEKMEYRPNKDQKKLDNFKKAVTDIQGFIK 377
Cdd:cd07751    88 GGMQDTDTVFVERKTHHEswtGEKSVKERFALKEKYVNSFLKGKYTVDKVFRKLRKEGKKSEAEIEKLEALATEIQYVIL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 378 EQKLQPMVRANYTRTAFQIPGDDRVRISLDTNLALIREdaldldrpcrDPDDWHRRDIDNaqmEFPFKAIKKGEIHKFPY 457
Cdd:cd07751   168 KRKLKPVVRTFYRRTAFQLPDDNRVRISLDTELCMIDE----------RGRDGRRRTTLN---DWPFKQLPDNEIVRFPY 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2088002125 458 ALLEIKVK---GMKKYEWIEDLMHSHLVKESPRFSKFVHGVAKLFEDNVNTFPFWL 510
Cdd:cd07751   235 AVLEVKLQtqeGEEPPEWVEELLNSHLVEEVYKFSKFLHGCATLFPDKVDSIPYWL 290
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
 2-160 1.34e-49

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: 170.80  E-value: 1.34e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSVYAPWKDKYIDYDKLKKLLKDNEDDDSWTADDESAFVDELANVQLEKVHNFITDISQKLRDRTSACEKKLE 81
Cdd:cd14480     1 KFGKTLKSSIYPPWKDYYIDYDKLKKLLKERETDRGWWTEDDERFFVELLEVELEKVYTFQKEKYSELRRRIDACEKKVK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2088002125  82 PLaigiqddkenkdsqpegasadagdATRKPEPSQQEREKLLKEVLSELDNITKETKELEAFSRINFTAVIKATKKHDK 160
Cdd:cd14480    81 EL------------------------VSNLDSSEDDPSEEDFKELEEELDDILADVHDLAKFTRLNYTGFLKIVKKHDK 135
VTC1 COG5264
Vacuolar transporter chaperone [Posttranslational modification, protein turnover, chaperones];
655-780 6.13e-39

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


Pssm-ID: 227589  Cd Length: 126  Bit Score: 140.59  E-value: 6.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 655 IQLPPGIRDPGVWIKDQGPVRVEAKVWLANQRTFIKWQHVSVLLASLSLGLYNAAGEannIARALAVVYTCIAAFTLAWG 734
Cdd:COG5264     2 SVLPPLVKKPVPGKRIAGPVRVEPKVWFANERTFLSWLSVTVLLGGLGFALYNSGDR---LGMISAYVFTIVAIFCGFYA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2088002125 735 YGMYVYRAKLIRERSGKDFDAITGPLVVCVGLAVALCLNFGFKYNA 780
Cdd:COG5264    79 LMLYLKRAVNIRQRSAGPYDDRLGPTLVCVVLLVALIVNFFLAFKA 124
PolyPPase_VTC_like cd07750
Polyphosphate(polyP) polymerase domain of yeast vacuolar transport chaperone (VTC) proteins ...
 228-492 6.34e-33

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: 126.66  E-value: 6.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 228 KFWVHMDNLFEVKTVILRRLPVLVYnpqtskvaeGTQRDPTITSIYFDNPNFSLYTDKVNGKPDAASLRLRWYGhlNEKP 307
Cdd:cd07750     5 KYLVPASQLEALLAALKPHLRVDEY---------AGNRDYTIRSLYFDTPDLDLYREKLNGRRRREKVRIRSYG--DSDG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 308 EIVFEKKvIKEGDAAEEVRFPIKAKYVQSFLEDHYHMEKSIEKMEYRpnkdqkkldnfkkavtDIQGFIKEQKLQPMVRA 387
Cdd:cd07750    74 LIFLEVK-TKRGRVTYKRRLPLSPEDAERLLAGGYFFLLESQDPLAE----------------EFYFRMRYKQLRPVLLV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 388 NYTRTAFQIPgDDRVRISLDTNLAliredaldldrpCRDPDDWHRRDIDNAqmefpfkaikkgEIHKFPYALLEIKVKGM 467
Cdd:cd07750   137 SYRREALVSP-DGGVRITFDTNLR------------YRDEDGDLFSGNLGT------------PILPPDLVILEVKYDGA 191

                         250       260
                  ....*....|....*....|....*
gi 2088002125 468 KKyEWIEDLMHSHLVKESpRFSKFV 492
Cdd:cd07750   192 LP-LWLADLLSSHGLEPT-SFSKYC 214
COG5036 COG5036
SPX domain-containing protein involved in vacuolar polyphosphate accumulation [Inorganic ion ...
 227-495 8.36e-23

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: 98.14  E-value: 8.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 227 YKFWVHMDNLFEVKTVILRRLPVLVYNPQtskvaegtQRDPTITSIYFDNPNFSLYTDKVNGKPDAASLRLRWYGHLNEK 306
Cdd:COG5036    12 LKYLIPEEQADALREALKTYMEPDKYSDE--------SGFYTIRSLYFDTPDLELYRESIEGPKYREKLRLRSYGDPTPE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 307 PEIVFEKK------VIKEgdaaeevRFPIKAKYVQSFLEdhyhmeksiekmeyRPNKDQKKLDNFKKAVTDIQGFIKEQK 380
Cdd:COG5036    84 SPVFLEIKkkvdgvVYKR-------RAPVPLEEARAFLK--------------GGSLPAHDNPSNKQLLREIDYFLARYN 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 381 LQPMVRANYTRTAFQIPGDDRVRISLDTNLaLIREDALDLDRPcrdpdDWHRRDIDNaqmefpfkaikkgeihkfPYALL 460
Cdd:COG5036   143 LRPKVLVAYDREAFAGKDDGDLRITFDTNI-RFRDDDLRLDKG-----EHGEPLVPP------------------GYVLL 198

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2088002125 461 EIKVKGMKKYeWIEDLM-HSHLVKESprFSKFVHGV 495
Cdd:COG5036   199 EIKYDGRMPL-WLSDLLsRLNLFRTS--FSKYGNGY 231
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
 2-160 2.22e-17

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: 79.53  E-value: 2.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSVYAPWKDKYIDYDKLKKLLKDNEDDDS--------------WTADDESAFVDELaNVQLEKVHNFitdiSQ 67
Cdd:cd14447     1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADeasnssealelsesGGEEFESEFFEAL-DAELEKVNEF----YQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  68 KLRDRTSACEKKLEPLaigiqddkenkdsqpegasadagDATRKPEPSQQEREklLKEVLSELDNITKETKELEAFSRIN 147
Cdd:cd14447    76 ELLEELQELLKRLEAL-----------------------EPDLPALRGSLKEE--LEDLRKELVESYSELEELERFVELN 130

                         170
                  ....*....|...
gi 2088002125 148 FTAVIKATKKHDK 160
Cdd:cd14447   131 YTAFRKILKKYDK 143
DUF202 pfam02656
Domain of unknown function (DUF202); This family consists of hypothetical proteins some of ...
 679-743 8.52e-14

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: 8.52e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2088002125 679 KVWLANQRTFIKWQHVSVLLASLSLGLYNAAGEANN--IARALAVVYTCIAAFTLAWGYGMYVYRAK 743
Cdd:pfam02656   1 RDGLANERTFLAWLRTSLALIALGVALLRFFLHGGPtgLALILGLILIVLGILTLLYGLRRYLRRVR 67
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
 2-160 4.29e-07

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: 49.96  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSV---YAPWKDKYIDYDKLKKLLK---------DNEDDDSWTADDESAFVDELA------NVQLEKVHNFIT 63
Cdd:cd14481     1 KFGKSLKRQIeetLPEWRDKFLSYKELKKLLKlispgnadkPNSKRDRRGGGAARAMTKEEAdfvrllNAELDKFNAFFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  64 D------ISQK-LRDRtsacekkleplaigiqddkenkdsqpegasadAGDATRKPEPSQQEREKLLKEVLseldNITKE 136
Cdd:cd14481    81 EkeeeyvIRLKeLQDR--------------------------------VAEAKETPRDSNEELMRIRREIV----DFHGE 124

                         170       180
                  ....*....|....*....|....
gi 2088002125 137 TKELEAFSRINFTAVIKATKKHDK 160
Cdd:cd14481   125 MVLLENYSSLNYTGLVKILKKYDK 148
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
 2-160 5.97e-07

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: 49.49  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSVYAPWKDKYIDYDKLKKLLKdnedddswtADDESAFVDElanvQLEKVHNFitdisqkLRDRTSACEKKLE 81
Cdd:cd14475     1 KFAKYLEENLVPEWRKKYLDYKGGKKKIK---------AREFFEFLDS----ELDKVESF-------YKEKEDEARERLD 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  82 PLAIGIQDDKENKDsqpEGASADAGDATRKPEPSQQERE------KLLKEVLSE----LDnitketkELEAFSRINFTAV 151
Cdd:cd14475    61 LLRDQLHELRDHRI---QEADDGRRDYSRRPEQNAHDPVsyrsarRKLKKALQEyyrgLE-------LLKSYRLLNRTAF 130


                  ....*....
gi 2088002125 152 IKATKKHDK 160
Cdd:cd14475   131 RKINKKFDK 139
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 228-430 9.49e-06

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.


Pssm-ID: 143620  Cd Length: 174  Bit Score: 46.68  E-value: 9.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 228 KFWVHMDNLfevktvilrrLPVLVYNPQTskVAEGTQRDPTITSIYFDNPNFSLytdkvngkpDAASLRLRWYghlNEKP 307
Cdd:cd07374     5 KFRVPDDAV----------LPLLLGVPGV--LGVGEPETVQLRAIYFDTPDLRL---------ARAGLRLRRR---TGGA 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 308 EIVFEKKVIKEGDAAEEVRFPIKakyvqsfledhyhmeksiekmeyRPNKDQKKLDnfkkAVTDIQGFIKEQKLQPMVRA 387
Cdd:cd07374    61 DAGWHLKLPGGISRRTEVRAPLG-----------------------DAAAVAPLLL----AAALVLAVTRGLPLRPVATI 113

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2088002125 388 NYTRTAFQIPGDDRVRISLDTNlaliREDALDLDrpCRDPDDW 430
Cdd:cd07374   114 ETTRTVYRLLDAGGVLAELDLD----TVTARVLD--GGGTQYW 150
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
 2-160 1.25e-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: 46.13  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSVYAPWKDKYIDYDKLKKLLKDNEDD--DSWTADDE------SAFVDE---LANVQLEKVHNFitdISQKLr 70
Cdd:cd14477     1 KFGEHLSAHITPEWRKQYINYEELKAMLYAAVEQapSPEVTDEDvvkryfAKFEEEffqECDKELAKVNTF---FSEKL- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  71 drtSACEKKLEPLAIGIQDDKENKDSQPEGASADAGDATRKPEPSQQER-EKLLKEVLSE-------LDNitketkelea 142
Cdd:cd14477    77 ---AEAQRKFATLKNELLSSLEAQGESGAASSLIRRVFALLRKERVKPRkLRDLKLAFSEfylslilLQN---------- 143

                         170
                  ....*....|....*...
gi 2088002125 143 FSRINFTAVIKATKKHDK 160
Cdd:cd14477   144 YQNLNFTGFRKILKKHDK 161
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
 1-147 2.89e-05

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: 47.17  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   1 MKFGTTLRKSVYAPWKDKYIDYDKLKKLLK-------DNEDDDSWTADDESAFVDELANVQLEKVHNFITDISQKLRDRT 73
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKkiqreleSTPPSSSPSSSDSGSAASPSDSTTSLPLRDPLSRSSSLDRAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  74 SACEKKLEPLAIGIQDDKENKDSQPEGAS----------ADAGDATRKPEPSQQEREKLLKEVL-SELDNITK--ETKEL 140
Cdd:pfam03105  81 GLVPSPPSSSSSSSSDSSSSSNSSSSSSSsspsllrrlpSESDDSSESYETTPLDSEDEFFERLdSELNKVNKfyKEKEE 160


                  ....*..
gi 2088002125 141 EAFSRIN 147
Cdd:pfam03105 161 EFLERLE 167
SPX_YDR089W cd14474
SPX domain of the yeast protein YDR089W and related proteins; This region has been named the ...
 2-160 9.19e-05

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: 43.38  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLR-KSVyaP-WKDKYIDYDKLKKLLKDNEDDDSWTADD--------ESAFVDELANvQLEKVHNFItdiSQKLRD 71
Cdd:cd14474     1 KFGEQLLqRSV--PeWKLYNIDYNELKHLIKEHTTRDQGTAIAipsalekfEDSLYNEFCE-QFDRVNLFV---SSKADE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  72 rtsaCEKKLEPLAIGIQDDKENKDSQpegasadagdatrkpEPSQQEREKLLKEVLSELDNITKETKELEAFSRINFTAV 151
Cdd:cd14474    75 ----ISRRLEHLESSILRLLERSASN---------------SGSRRRQKRRLAKIEQELLRCGEELQKLSRFIIAQKIAF 135


                  ....*....
gi 2088002125 152 IKATKKHDK 160
Cdd:cd14474   136 RKILKKYKK 144
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
 1-160 2.50e-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: 41.89  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   1 MKFGTTLRKSVYAPWKDKYIDYDKLKKLLK---DNEDDDSWTADDESAFVDELANVQLEKVHNFITDISQKLRDRTSACE 77
Cdd:cd14479     1 VNFGKKLKEDQIPEWEGYYINYKLLKKKVKqyvQQTQDGGQDRRDVLKDFSKLLDDQIEKIVLFLLEQQGLLASRLEKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  78 KKLEPLAigiqddkenkdSQPEGAsadagDATRKPEPSQQEREKLLKevlseldnitketkeLEAFSRINFTAVIKATKK 157
Cdd:cd14479    81 EQREALQ-----------EQPDLS-----QISELREAYRAVGLDLLK---------------LLKFVELNATGLRKILKK 129


                  ...
gi 2088002125 158 HDK 160
Cdd:cd14479   130 FDK 132
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
 15-160 4.39e-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: 41.37  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  15 WKDKYIDYDKLKKLL----KD-------NEDDDSWTA---------DDESAFVDELaNVQLEKVHNFITDISQKLRDRTS 74
Cdd:cd14478    14 WSDHYIAYSNLKKLIyqleKDqlqlqngGDDEEEEESsllllstdeDPDDVFVRAL-DKELEKIDSFYKEKEAELYAEVD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125  75 ACEKKLEplaigiqddkenkDSQPEGASADAGDATRKpepsqqeREKLLKEVLSELDnitketkeleAFSRINFTAVIKA 154
Cdd:cd14478    93 ELLKDVE-------------EFEEENYLYDSRISLKK-------RIINLYVSLSELK----------SYIELNRTGFSKI 142


                  ....*.
gi 2088002125 155 TKKHDK 160
Cdd:cd14478   143 LKKYDK 148
YidH COG2149
Uncharacterized membrane protein YidH, DUF202 family [Function unknown];
682-770 1.03e-03

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


Pssm-ID: 441752  Cd Length: 126  Bit Score: 39.91  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125 682 LANQRTFIKWQHVS-------VLLASLSLGLYNAAGEANNIARALAVVYTCIAAFTLAWGYGMYV-YRAKLIRE--RSGK 751
Cdd:COG2149    22 LANERTFLAWIRTAlaliafgFAIERFGLFLRPLALSLPGLSRVLGLALVLLGALLAVLAYIRYRrVERALRRGepLPSS 101

                          90
                  ....*....|....*....
gi 2088002125 752 DFDAITGPLVVCVGLAVAL 770
Cdd:COG2149   102 RLALLLAVAVALLGLLLLV 120
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
 2-95 4.36e-03

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: 38.39  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2088002125   2 KFGTTLRKSVYAPWKDKYIDYDKLKKLLKD--NEDDDSWTADDESAFVDELANV--------QLEKVHNFITDISQKLRD 71
Cdd:cd14476     1 KFGKEFESQMVPEWQEAYVDYKQLKKDLKRiqKFRDEYETTFLEAAEEGGEYELvffrrlddELNKVNKFYRSKVEEVLK 80

                          90       100
                  ....*....|....*....|....
gi 2088002125  72 RTSACEKKLEPLaIGIQDDKENKD 95
Cdd:cd14476    81 EAAALNKQMDAL-IAFRVKVENPQ 103
 
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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