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Conserved domains on  [gi|19113202|ref|NP_596410|]
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phosphate transporter [Schizosaccharomyces pombe]

Protein Classification

SLC13 family permease( domain architecture ID 11475065)

SLC13 (solute carrier 13) family permease is a sodium-coupled symporter that facilitates the transport across biological membranes of various ions including sulfate or Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate; may function as a regulator

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SLC13_permease cd01115
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
435-858 4.14e-103

Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been shown to translocate Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate across plasma membranes rabbit, human, and rat kidney. It is related to renal and intestinal Na+/sulfate cotransporters and a few putative bacterial permeases. The SLC13-type proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium and various anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease is composed of 8-13 transmembrane helices.


:

Pssm-ID: 238535 [Multi-domain]  Cd Length: 382  Bit Score: 324.54  E-value: 4.14e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 435 LALLVMVSLLWATEAIPLFVTSFLVPFMTVFLKILRDengsplsgkestKVIFSSMWNPTIVLLLGGFTIAAALSKYHIA 514
Cdd:cd01115   1 LAILVFAAVLFVTEALPLDVTALLVPVLLVLLGVVPP------------KEAFSGFSDPAVILFLAGFILGAALTRTGLA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 515 KRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAESDFakiLIVGIALASNVGGIASPI 594
Cdd:cd01115  69 KRIATKLLKRAGKGERRLLLLLMLVTAFLSAFMSNTATVAIMLPVALGLAAKLDISPSR---LLMPLAFAASIGGMLTLI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 595 SSPQNIVALQNMDPAAGWGEWFAVSIPVSLLCIFSIWFLLSFgllkdehitlakirstkdtftgvqWFISIVTIGTIVLW 674
Cdd:cd01115 146 GTPPNLVASGYLESLGGQGFSFFEFTPIGLPLLIIGLLYLWF------------------------IFRLAVLIITIVLL 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 675 CLERRFDEVFGDMGVIALVPIIVFFGTGLLTKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVSSLNTFR 754
Cdd:cd01115 202 AALAAITGLLPVSVAIAIGAIVLVFGGVLLTKEDYKSIDWGIIFLFAGGIPLGKALESSGAAALIAEALISLLGGLPPFA 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 755 VLLIFSALTLVVSSFISHIVAAMVVLPIVheVGSRLADP-HPRLFVLASGMMCSLAMALPTSGFPNMTAImmeneaGKRY 833
Cdd:cd01115 282 ILLLLCLLTLVLTNFISNTATAVLLAPIA--LSIALSLGlPPEALLLAVAIGASCAFMLPVGTPPNAIVL------GPGG 353
                       410       420
                ....*....|....*....|....*
gi 19113202 834 LKVSDFLKAGIPATLISFVILLLIG 858
Cdd:cd01115 354 YKFSDFAKVGLPLSILSLVVSVTMI 378
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-301 1.39e-101

SPX domain-containing protein [Signal transduction mechanisms];


:

Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 317.16  E-value: 1.39e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   1 MKFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDE-ETRLLEHERRSPDDRFMFALDKELQGIVEFYAP 79
Cdd:COG5408   1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQLSSYHGVSDNdETRDEAGEPSNWRDRFNHALKKELSPLQANYVA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  80 KEKEIadqygrIKGEFETYENEYMSQGNNINYPTPERLQKSSASRKSGRMARSQELPRITSSNREIYLNGQTSDGGYAAP 159
Cdd:COG5408  81 KFFEN------YISEEAIKLDEFYSQGQYIAYKKREFRKISSKFFYSERKALVQKEENTASSNYDTFLNLQTDEGAYVAD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 160 AISRAESTAIQPSEPHDVDTSKNGLSKK--QHSEAQPEVQGNDDEVEEEDDDDDDEDEDEDEDEDNNNnnRWLLIEQYPS 237
Cdd:COG5408 155 ARKRAEAKSYDPFDSLRIDTSKEGLTKRnlNLPDYEKIVSGTDEEVPSNDQDDEDQDFDYLAKKNDNT--ALLDLSQFNF 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113202 238 DIVAYENFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDKTLGSSLRESYMKRVNQAYP 301
Cdd:COG5408 233 KIVKYQKRSLLKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNLRHEYMSRSVNEYY 296
 
Name Accession Description Interval E-value
SLC13_permease cd01115
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
435-858 4.14e-103

Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been shown to translocate Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate across plasma membranes rabbit, human, and rat kidney. It is related to renal and intestinal Na+/sulfate cotransporters and a few putative bacterial permeases. The SLC13-type proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium and various anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease is composed of 8-13 transmembrane helices.


Pssm-ID: 238535 [Multi-domain]  Cd Length: 382  Bit Score: 324.54  E-value: 4.14e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 435 LALLVMVSLLWATEAIPLFVTSFLVPFMTVFLKILRDengsplsgkestKVIFSSMWNPTIVLLLGGFTIAAALSKYHIA 514
Cdd:cd01115   1 LAILVFAAVLFVTEALPLDVTALLVPVLLVLLGVVPP------------KEAFSGFSDPAVILFLAGFILGAALTRTGLA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 515 KRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAESDFakiLIVGIALASNVGGIASPI 594
Cdd:cd01115  69 KRIATKLLKRAGKGERRLLLLLMLVTAFLSAFMSNTATVAIMLPVALGLAAKLDISPSR---LLMPLAFAASIGGMLTLI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 595 SSPQNIVALQNMDPAAGWGEWFAVSIPVSLLCIFSIWFLLSFgllkdehitlakirstkdtftgvqWFISIVTIGTIVLW 674
Cdd:cd01115 146 GTPPNLVASGYLESLGGQGFSFFEFTPIGLPLLIIGLLYLWF------------------------IFRLAVLIITIVLL 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 675 CLERRFDEVFGDMGVIALVPIIVFFGTGLLTKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVSSLNTFR 754
Cdd:cd01115 202 AALAAITGLLPVSVAIAIGAIVLVFGGVLLTKEDYKSIDWGIIFLFAGGIPLGKALESSGAAALIAEALISLLGGLPPFA 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 755 VLLIFSALTLVVSSFISHIVAAMVVLPIVheVGSRLADP-HPRLFVLASGMMCSLAMALPTSGFPNMTAImmeneaGKRY 833
Cdd:cd01115 282 ILLLLCLLTLVLTNFISNTATAVLLAPIA--LSIALSLGlPPEALLLAVAIGASCAFMLPVGTPPNAIVL------GPGG 353
                       410       420
                ....*....|....*....|....*
gi 19113202 834 LKVSDFLKAGIPATLISFVILLLIG 858
Cdd:cd01115 354 YKFSDFAKVGLPLSILSLVVSVTMI 378
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-301 1.39e-101

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 317.16  E-value: 1.39e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   1 MKFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDE-ETRLLEHERRSPDDRFMFALDKELQGIVEFYAP 79
Cdd:COG5408   1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQLSSYHGVSDNdETRDEAGEPSNWRDRFNHALKKELSPLQANYVA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  80 KEKEIadqygrIKGEFETYENEYMSQGNNINYPTPERLQKSSASRKSGRMARSQELPRITSSNREIYLNGQTSDGGYAAP 159
Cdd:COG5408  81 KFFEN------YISEEAIKLDEFYSQGQYIAYKKREFRKISSKFFYSERKALVQKEENTASSNYDTFLNLQTDEGAYVAD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 160 AISRAESTAIQPSEPHDVDTSKNGLSKK--QHSEAQPEVQGNDDEVEEEDDDDDDEDEDEDEDEDNNNnnRWLLIEQYPS 237
Cdd:COG5408 155 ARKRAEAKSYDPFDSLRIDTSKEGLTKRnlNLPDYEKIVSGTDEEVPSNDQDDEDQDFDYLAKKNDNT--ALLDLSQFNF 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113202 238 DIVAYENFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDKTLGSSLRESYMKRVNQAYP 301
Cdd:COG5408 233 KIVKYQKRSLLKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNLRHEYMSRSVNEYY 296
CitT COG0471
Di- and tricarboxylate antiporter [Carbohydrate transport and metabolism];
499-863 1.08e-64

Di- and tricarboxylate antiporter [Carbohydrate transport and metabolism];


Pssm-ID: 440239 [Multi-domain]  Cd Length: 369  Bit Score: 221.57  E-value: 1.08e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 499 LGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAESD--FAKI 576
Cdd:COG0471   1 LGGFVLAAALEKTGLGRRIALLLLKRFGGSPLRLLLGLMLATALLSAFISNTARAAMMLPIALSIAAALGSEKRskFGSA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 577 LIVGIALASNVGGIASPISSPQNIVALQNMDPAAG----WGEWFAVSIPVSLLCIFSIWFLLSFgLLKDEHITLAK---- 648
Cdd:COG0471  81 LLLPIAFAASIGGMGTLIGTPPNLIAAGLLEEATGipisFFEWMLVGLPVALVGLLLLWLVLYR-LLPPEIKEVPGskev 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 649 IRSTKDT---FTGVQWFISIVTIGTIVLWClerrFDEVFG-DMGVIALVPIIVFFGTGLLTKEDFNNFL-WTVIVLAMGG 723
Cdd:COG0471 160 IREELAElgpLSRREKIALAIFALTVLLWI----TGSLHGiPIAVVALLGAVLLLLTGVLTWKDAYKSIpWGVLLLFGGG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 724 VALGKVVSSSGLLELIALKIGNAVSSLNTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGSRLaDPHPRLFVLASG 803
Cdd:COG0471 236 LALGAALEKTGLAAWLADALLPLLGGLSPLLLLLLLALLTLLLTEFASNTATAALLLPIAISLAQAL-GVNPLPLALAVA 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 804 MMCSLAMALPTSGFPNmtAIMMeneaGKRYLKVSDFLKAGIPATLISFVILLLIGTPIMR 863
Cdd:COG0471 315 FAASCAFLLPVGTPPN--AIVY----GSGYYKFKDFLKVGLPLNLIGLVVLLLLGPLWWP 368
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
2-282 1.17e-50

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: 174.65  E-value: 1.17e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDEE----TRLLEHERRSPDDRFMFALDKELQGIVEFY 77
Cdd:cd14478   1 KFSHSLQFNAVPEWSDHYIAYSNLKKLIYQLEKDQLQLQNGGDDEEeeesSLLLLSTDEDPDDVFVRALDKELEKIDSFY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  78 APKEKEIADQYGRIKGEFETYENEYmsqgnninyptperlqkssasrksgrmarsqelpritssnreiylngqtsdggya 157
Cdd:cd14478  81 KEKEAELYAEVDELLKDVEEFEEEN------------------------------------------------------- 105
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 158 apaisraestaiqpsephdvdtsknglskkqhseaqpevqgnddeveeeddddddededededednnnnnrwllieqyps 237
Cdd:cd14478     --------------------------------------------------------------------------------
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 19113202 238 diVAYENFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDK 282
Cdd:cd14478 106 --YLYDSRISLKKRIINLYVSLSELKSYIELNRTGFSKILKKYDK 148
dass TIGR00785
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally ...
435-860 1.44e-50

anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally characterized proteins of the DASS family transport (1) organic di- and tricarboxylates of the Krebs Cycle as well as dicarboxylate amino acid, (2) inorganic sulfate and (3) phosphate. The animal NaDC-1 cotransport 3 Na+ with each dicarboxylate. Protonated tricarboxylates are also cotransported with 3Na+. [Transport and binding proteins, Anions, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273267 [Multi-domain]  Cd Length: 444  Bit Score: 184.47  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   435 LALLVMVSLLWATEAIPLFVTSFL-VPFMTVFLKILrdengsplsGKESTKVIFSSMWNPTIVLLLGGFTIAAALSKYHI 513
Cdd:TIGR00785  14 LAIFVAAIVGWILEPLPLPVTALLaIPIIAVLLGVL---------SAFKFKNALSGFADPTIWLFFGAFILATALVKTGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   514 AKRLATSILAHAG-RKPRSVLLTNMFVAMFASMWISNVAApvlCFSIIQPLLRNLPA---------ESDFAKILIVGIAL 583
Cdd:TIGR00785  85 GKRIAYKLVGKMGgTTLGLGYFLVFLETLLAPMWPSNTAR---AGGILLPIIKSLLPllgskpeksPRKIGKYLMLGIAY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   584 ASNVGGIASPISSPQNIVALQNMDPAAG----WGEWFAVSIPVSLLCIFSIWFLL-----SFGLLKDEHITLAKIR-STK 653
Cdd:TIGR00785 162 SASIGSSGFLTGSAPNALAAGILSKILGiqisWGDWFLAGLPLGIILLLLVPLLLyvlfpPELKLKDEVDLWAKEElEEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   654 DTFTGVQWFISIVTIGTIVLWclerrfdeVFG-----DMGVIALVPIIVFFGTGLLTKEDF--NNFLWTVIVLAMGGVAL 726
Cdd:TIGR00785 242 GPMSFREKALLGIFLLALLLW--------IFGgslgiNASVVALLAVVLMLFLGIVTWKDIqkNKVAWNTLILFGGLIGL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   727 GKVVSSSGLLELIALKIGNAVSSL-NTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGSRLADPhPRLFVLASGMM 805
Cdd:TIGR00785 314 AGGLKKSGFIKWFSEKLVGILDGLsPTIAVLVLVVLFYIILYFFASNTAHTAALVPIFFSVASAQGIP-LELLALALALS 392
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113202   806 CSLA-MALPTSGFPNMTAImmeneaGKRYLKVSDFLKAGIPATLISFVILLLIGTP 860
Cdd:TIGR00785 393 ASLMgFLTPYATPPNAIAY------GSGYVKIKDMWRVGAIIGIVGLIVLLLVGTL 442
CitMHS pfam03600
Citrate transporter;
443-801 5.98e-32

Citrate transporter;


Pssm-ID: 460985 [Multi-domain]  Cd Length: 342  Bit Score: 127.81  E-value: 5.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   443 LLWATEAIPLFVTSFLVPFMTVFLKILrdengsplsgkeSTKVIFSSMWNPTIVLLLGGFTIAAALSKYHIAKRLATSIL 522
Cdd:pfam03600   2 VLIITEKLPRDVVALLGAVLLVLLGVL------------TPEEALSGIDSPTILLLLGMMIIGAILERTGLFDRLALKLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   523 AHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLR--NLPaesdfAKILIVGIALASNVGGIASPISSPQNI 600
Cdd:pfam03600  70 RLAGGKPRRLLVALMLATALLSAFLSNDGTVLIMIPIVLALARrlGLP-----PSPLLIALAFAANIGGTATPIGDPPNI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   601 VALQNMDPAAGW---GEWFAVSIPVSLLCIFSIWFLLSFGLLKDEHITLAKIRSTKDTFTGVQWFISIVTIgtIVLWCLE 677
Cdd:pfam03600 145 IIASALGLSFGDfgfFMFPPVGVALLLVGLLPLLLIFRKLLPVRKEEEAELEELRKRAIKDKLLLAISALV--LALVILG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   678 RRFDEVFGDMGVIALVpiivfFGTGLLTKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVsslNTFRVLL 757
Cdd:pfam03600 223 FLLLSVLALAGALLLL-----LTGVLDPEEALKAVDWSTLLFFAGLFILVGALEKTGLADALADALGGLS---GLLVALA 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 19113202   758 IFSALTLVVSSFISHIVAAMVVLPIVHEV--GSRLADPHPRLFVLA 801
Cdd:pfam03600 295 LILWLSALLSAFISNVPTAALMAPIIVGMapAAGLGDPDPLAWALA 340
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-296 8.63e-30

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: 121.13  E-value: 8.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202     1 MKFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAP------------------------------------ 44
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRELESTPPSSSpsssdsgsaaspsdsttslplrdplsrsssldrafg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202    45 ------------------------------------------DEETRLLEHERRSPDDRFMFALDKELQGIVEFYAPKEK 82
Cdd:pfam03105  81 glvpsppssssssssdsssssnssssssssspsllrrlpsesDDSSESYETTPLDSEDEFFERLDSELNKVNKFYKEKEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202    83 EIADQYGRIKGEFEtyeneymsqgNNINYptpeRLQKSSASRKSgrMARSQELPRITSSNREIYLNGQTSDGGyAAPAIS 162
Cdd:pfam03105 161 EFLERLEALNKQLE----------ALRDF----RIKLIRESKSD--LYRWREPFGLYSSDSSVFFSTSELDSG-NSSESS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   163 RAESTAIQPSEPHDVDTSKNGLSKKQHSEAQPEVQgnddeveeeddddddededededeDNNNNNRWLLIEQYPSDIVAY 242
Cdd:pfam03105 224 VDDEVEEELERNGWISPIKSKDKKKRPSEALDKVK------------------------TPDRTLKGFLDASRRDYLNRI 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   243 ENF------VSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDKTLGSSLRESYMKRV 296
Cdd:pfam03105 280 NKVnlrkakKKLKKAFIELYRGLELLKSYSELNRTAFRKILKKFDKVTSLNASKDYMKEV 339
PLN00137 PLN00137
NHAD transporter family protein; Provisional
495-594 1.25e-03

NHAD transporter family protein; Provisional


Pssm-ID: 215071  Cd Length: 424  Bit Score: 42.37  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  495 IVLLLGGFTIAAALSKYHIAKRLATSILAhagRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSiiqpLLRNLPAESDFA 574
Cdd:PLN00137  69 VFFLLGAMTIVEIVDAHQGFKLVTDSITT---RSPRTLLWVVGFITFFLSSILDNLTTTIVMVS----LLRKLVPPSEYR 141
                         90       100
                 ....*....|....*....|
gi 19113202  575 KILIVGIALASNVGGIASPI 594
Cdd:PLN00137 142 KLLGAVVVVAANAGGAWTPI 161
 
Name Accession Description Interval E-value
SLC13_permease cd01115
Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been ...
435-858 4.14e-103

Permease SLC13 (solute carrier 13). The sodium/dicarboxylate cotransporter NaDC-1 has been shown to translocate Krebs cycle intermediates such as succinate, citrate, and alpha-ketoglutarate across plasma membranes rabbit, human, and rat kidney. It is related to renal and intestinal Na+/sulfate cotransporters and a few putative bacterial permeases. The SLC13-type proteins belong to the ArsB/NhaD superfamily of permeases that translocate sodium and various anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease is composed of 8-13 transmembrane helices.


Pssm-ID: 238535 [Multi-domain]  Cd Length: 382  Bit Score: 324.54  E-value: 4.14e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 435 LALLVMVSLLWATEAIPLFVTSFLVPFMTVFLKILRDengsplsgkestKVIFSSMWNPTIVLLLGGFTIAAALSKYHIA 514
Cdd:cd01115   1 LAILVFAAVLFVTEALPLDVTALLVPVLLVLLGVVPP------------KEAFSGFSDPAVILFLAGFILGAALTRTGLA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 515 KRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAESDFakiLIVGIALASNVGGIASPI 594
Cdd:cd01115  69 KRIATKLLKRAGKGERRLLLLLMLVTAFLSAFMSNTATVAIMLPVALGLAAKLDISPSR---LLMPLAFAASIGGMLTLI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 595 SSPQNIVALQNMDPAAGWGEWFAVSIPVSLLCIFSIWFLLSFgllkdehitlakirstkdtftgvqWFISIVTIGTIVLW 674
Cdd:cd01115 146 GTPPNLVASGYLESLGGQGFSFFEFTPIGLPLLIIGLLYLWF------------------------IFRLAVLIITIVLL 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 675 CLERRFDEVFGDMGVIALVPIIVFFGTGLLTKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVSSLNTFR 754
Cdd:cd01115 202 AALAAITGLLPVSVAIAIGAIVLVFGGVLLTKEDYKSIDWGIIFLFAGGIPLGKALESSGAAALIAEALISLLGGLPPFA 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 755 VLLIFSALTLVVSSFISHIVAAMVVLPIVheVGSRLADP-HPRLFVLASGMMCSLAMALPTSGFPNMTAImmeneaGKRY 833
Cdd:cd01115 282 ILLLLCLLTLVLTNFISNTATAVLLAPIA--LSIALSLGlPPEALLLAVAIGASCAFMLPVGTPPNAIVL------GPGG 353
                       410       420
                ....*....|....*....|....*
gi 19113202 834 LKVSDFLKAGIPATLISFVILLLIG 858
Cdd:cd01115 354 YKFSDFAKVGLPLSILSLVVSVTMI 378
COG5408 COG5408
SPX domain-containing protein [Signal transduction mechanisms];
1-301 1.39e-101

SPX domain-containing protein [Signal transduction mechanisms];


Pssm-ID: 227695 [Multi-domain]  Cd Length: 296  Bit Score: 317.16  E-value: 1.39e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   1 MKFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDE-ETRLLEHERRSPDDRFMFALDKELQGIVEFYAP 79
Cdd:COG5408   1 MKFGHSLQFNAVPEWSSKYIDYKQLKKLIYSLQKDQLSSYHGVSDNdETRDEAGEPSNWRDRFNHALKKELSPLQANYVA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  80 KEKEIadqygrIKGEFETYENEYMSQGNNINYPTPERLQKSSASRKSGRMARSQELPRITSSNREIYLNGQTSDGGYAAP 159
Cdd:COG5408  81 KFFEN------YISEEAIKLDEFYSQGQYIAYKKREFRKISSKFFYSERKALVQKEENTASSNYDTFLNLQTDEGAYVAD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 160 AISRAESTAIQPSEPHDVDTSKNGLSKK--QHSEAQPEVQGNDDEVEEEDDDDDDEDEDEDEDEDNNNnnRWLLIEQYPS 237
Cdd:COG5408 155 ARKRAEAKSYDPFDSLRIDTSKEGLTKRnlNLPDYEKIVSGTDEEVPSNDQDDEDQDFDYLAKKNDNT--ALLDLSQFNF 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113202 238 DIVAYENFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDKTLGSSLRESYMKRVNQAYP 301
Cdd:COG5408 233 KIVKYQKRSLLKKRIIELYIQLHQLKSFIELNYTGFSKITKKYDKTLHQNLRHEYMSRSVNEYY 296
CitT COG0471
Di- and tricarboxylate antiporter [Carbohydrate transport and metabolism];
499-863 1.08e-64

Di- and tricarboxylate antiporter [Carbohydrate transport and metabolism];


Pssm-ID: 440239 [Multi-domain]  Cd Length: 369  Bit Score: 221.57  E-value: 1.08e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 499 LGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAESD--FAKI 576
Cdd:COG0471   1 LGGFVLAAALEKTGLGRRIALLLLKRFGGSPLRLLLGLMLATALLSAFISNTARAAMMLPIALSIAAALGSEKRskFGSA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 577 LIVGIALASNVGGIASPISSPQNIVALQNMDPAAG----WGEWFAVSIPVSLLCIFSIWFLLSFgLLKDEHITLAK---- 648
Cdd:COG0471  81 LLLPIAFAASIGGMGTLIGTPPNLIAAGLLEEATGipisFFEWMLVGLPVALVGLLLLWLVLYR-LLPPEIKEVPGskev 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 649 IRSTKDT---FTGVQWFISIVTIGTIVLWClerrFDEVFG-DMGVIALVPIIVFFGTGLLTKEDFNNFL-WTVIVLAMGG 723
Cdd:COG0471 160 IREELAElgpLSRREKIALAIFALTVLLWI----TGSLHGiPIAVVALLGAVLLLLTGVLTWKDAYKSIpWGVLLLFGGG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 724 VALGKVVSSSGLLELIALKIGNAVSSLNTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGSRLaDPHPRLFVLASG 803
Cdd:COG0471 236 LALGAALEKTGLAAWLADALLPLLGGLSPLLLLLLLALLTLLLTEFASNTATAALLLPIAISLAQAL-GVNPLPLALAVA 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 804 MMCSLAMALPTSGFPNmtAIMMeneaGKRYLKVSDFLKAGIPATLISFVILLLIGTPIMR 863
Cdd:COG0471 315 FAASCAFLLPVGTPPN--AIVY----GSGYYKFKDFLKVGLPLNLIGLVVLLLLGPLWWP 368
ArsB_NhaD_permease cd00625
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
443-857 1.17e-57

Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, antimonite, sulfate and organic anions across biological membranes in all three kingdoms of life. A typical anion permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump.


Pssm-ID: 238344 [Multi-domain]  Cd Length: 396  Bit Score: 202.86  E-value: 1.17e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 443 LLWATEAIPLFVTSFLVPFMTVFLKILRDENgsplsgkestkvIFSSMWNPTIVLLLGGFTIAAALSKYHIAKRLATSIL 522
Cdd:cd00625   2 VLIRPEKLPRAVVALLGAVLLVLLGVVSPKE------------ALSAIDWETILLLFGMMILSAALEETGLFDRLAAKLA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 523 AhAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAesDFAKILIVGIALASNVGGIASPISSPQNIVA 602
Cdd:cd00625  70 R-ASKGSRRLLLLLMLLTAALSAFFSNDATAVLLTPIVLALLRKLGL--SPPVPLLLALAFAANIGGAATPIGNPPNLII 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 603 LQNMDPAAGWGEWFAVSIPVSLLCIFSIWFLLSFG--LLKDEHITLAKIRSTKDT-FTGVQWFISIVTIGTIVLWCLERR 679
Cdd:cd00625 147 ASLSGLGFLDFLAFMAPPALGLLLLLLGLLYLLFRkkLLLPDEDKLTVLAEPLPArPLLKKFLLLALLLLLLFVLLFFFL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 680 FDEVFGDMGVIALVPIIVFFgtGLLTKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIgNAVSSLNTFRVLLIF 759
Cdd:cd00625 227 IPLGLIALLGALLLLLLLVR--GLDPEEVLKSVDWGTLLFFAGLFVLVGALESTGLLEWLAELL-VALVGLPPLAALLLI 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 760 SALTLVVSSFISHIVAAMVVLPIVHEVGSR----LADPHPRLFVLASGMMCSLAMALPTSGFPNMTAimmeneagkrYLK 835
Cdd:cd00625 304 GLLSALLSNFISNVPTVALLLPIAASLAPPepawLALALGSTLGGNLTLIGSLANLIPLGAAENAGV----------GIS 373
                       410       420
                ....*....|....*....|..
gi 19113202 836 VSDFLKAGIPATLISFVILLLI 857
Cdd:cd00625 374 FGEFLKVGLPLTLLSLVVSLLY 395
SPX_PHO87_PHO90_like cd14478
SPX domain of the phosphate transporters Pho87, Pho90, Pho91, and related proteins; This ...
2-282 1.17e-50

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: 174.65  E-value: 1.17e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDEE----TRLLEHERRSPDDRFMFALDKELQGIVEFY 77
Cdd:cd14478   1 KFSHSLQFNAVPEWSDHYIAYSNLKKLIYQLEKDQLQLQNGGDDEEeeesSLLLLSTDEDPDDVFVRALDKELEKIDSFY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  78 APKEKEIADQYGRIKGEFETYENEYmsqgnninyptperlqkssasrksgrmarsqelpritssnreiylngqtsdggya 157
Cdd:cd14478  81 KEKEAELYAEVDELLKDVEEFEEEN------------------------------------------------------- 105
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 158 apaisraestaiqpsephdvdtsknglskkqhseaqpevqgnddeveeeddddddededededednnnnnrwllieqyps 237
Cdd:cd14478     --------------------------------------------------------------------------------
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 19113202 238 diVAYENFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDK 282
Cdd:cd14478 106 --YLYDSRISLKKRIINLYVSLSELKSYIELNRTGFSKILKKYDK 148
dass TIGR00785
anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally ...
435-860 1.44e-50

anion transporter; The Divalent Anion:Na+ Symporter (DASS) Family (TC 2.A.47) Functionally characterized proteins of the DASS family transport (1) organic di- and tricarboxylates of the Krebs Cycle as well as dicarboxylate amino acid, (2) inorganic sulfate and (3) phosphate. The animal NaDC-1 cotransport 3 Na+ with each dicarboxylate. Protonated tricarboxylates are also cotransported with 3Na+. [Transport and binding proteins, Anions, Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273267 [Multi-domain]  Cd Length: 444  Bit Score: 184.47  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   435 LALLVMVSLLWATEAIPLFVTSFL-VPFMTVFLKILrdengsplsGKESTKVIFSSMWNPTIVLLLGGFTIAAALSKYHI 513
Cdd:TIGR00785  14 LAIFVAAIVGWILEPLPLPVTALLaIPIIAVLLGVL---------SAFKFKNALSGFADPTIWLFFGAFILATALVKTGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   514 AKRLATSILAHAG-RKPRSVLLTNMFVAMFASMWISNVAApvlCFSIIQPLLRNLPA---------ESDFAKILIVGIAL 583
Cdd:TIGR00785  85 GKRIAYKLVGKMGgTTLGLGYFLVFLETLLAPMWPSNTAR---AGGILLPIIKSLLPllgskpeksPRKIGKYLMLGIAY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   584 ASNVGGIASPISSPQNIVALQNMDPAAG----WGEWFAVSIPVSLLCIFSIWFLL-----SFGLLKDEHITLAKIR-STK 653
Cdd:TIGR00785 162 SASIGSSGFLTGSAPNALAAGILSKILGiqisWGDWFLAGLPLGIILLLLVPLLLyvlfpPELKLKDEVDLWAKEElEEM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   654 DTFTGVQWFISIVTIGTIVLWclerrfdeVFG-----DMGVIALVPIIVFFGTGLLTKEDF--NNFLWTVIVLAMGGVAL 726
Cdd:TIGR00785 242 GPMSFREKALLGIFLLALLLW--------IFGgslgiNASVVALLAVVLMLFLGIVTWKDIqkNKVAWNTLILFGGLIGL 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   727 GKVVSSSGLLELIALKIGNAVSSL-NTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGSRLADPhPRLFVLASGMM 805
Cdd:TIGR00785 314 AGGLKKSGFIKWFSEKLVGILDGLsPTIAVLVLVVLFYIILYFFASNTAHTAALVPIFFSVASAQGIP-LELLALALALS 392
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113202   806 CSLA-MALPTSGFPNMTAImmeneaGKRYLKVSDFLKAGIPATLISFVILLLIGTP 860
Cdd:TIGR00785 393 ASLMgFLTPYATPPNAIAY------GSGYVKIKDMWRVGAIIGIVGLIVLLLVGTL 442
CitMHS pfam03600
Citrate transporter;
443-801 5.98e-32

Citrate transporter;


Pssm-ID: 460985 [Multi-domain]  Cd Length: 342  Bit Score: 127.81  E-value: 5.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   443 LLWATEAIPLFVTSFLVPFMTVFLKILrdengsplsgkeSTKVIFSSMWNPTIVLLLGGFTIAAALSKYHIAKRLATSIL 522
Cdd:pfam03600   2 VLIITEKLPRDVVALLGAVLLVLLGVL------------TPEEALSGIDSPTILLLLGMMIIGAILERTGLFDRLALKLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   523 AHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLR--NLPaesdfAKILIVGIALASNVGGIASPISSPQNI 600
Cdd:pfam03600  70 RLAGGKPRRLLVALMLATALLSAFLSNDGTVLIMIPIVLALARrlGLP-----PSPLLIALAFAANIGGTATPIGDPPNI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   601 VALQNMDPAAGW---GEWFAVSIPVSLLCIFSIWFLLSFGLLKDEHITLAKIRSTKDTFTGVQWFISIVTIgtIVLWCLE 677
Cdd:pfam03600 145 IIASALGLSFGDfgfFMFPPVGVALLLVGLLPLLLIFRKLLPVRKEEEAELEELRKRAIKDKLLLAISALV--LALVILG 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   678 RRFDEVFGDMGVIALVpiivfFGTGLLTKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVsslNTFRVLL 757
Cdd:pfam03600 223 FLLLSVLALAGALLLL-----LTGVLDPEEALKAVDWSTLLFFAGLFILVGALEKTGLADALADALGGLS---GLLVALA 294
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 19113202   758 IFSALTLVVSSFISHIVAAMVVLPIVHEV--GSRLADPHPRLFVLA 801
Cdd:pfam03600 295 LILWLSALLSAFISNVPTAALMAPIIVGMapAAGLGDPDPLAWALA 340
SPX pfam03105
SPX domain; We have named this region the SPX domain after SYG1, Pho81 and XPR1. This 180 ...
1-296 8.63e-30

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: 121.13  E-value: 8.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202     1 MKFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAP------------------------------------ 44
Cdd:pfam03105   1 MKFGKELEENLVPEWRDAYLDYKQLKKLIKKIQRELESTPPSSSpsssdsgsaaspsdsttslplrdplsrsssldrafg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202    45 ------------------------------------------DEETRLLEHERRSPDDRFMFALDKELQGIVEFYAPKEK 82
Cdd:pfam03105  81 glvpsppssssssssdsssssnssssssssspsllrrlpsesDDSSESYETTPLDSEDEFFERLDSELNKVNKFYKEKEE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202    83 EIADQYGRIKGEFEtyeneymsqgNNINYptpeRLQKSSASRKSgrMARSQELPRITSSNREIYLNGQTSDGGyAAPAIS 162
Cdd:pfam03105 161 EFLERLEALNKQLE----------ALRDF----RIKLIRESKSD--LYRWREPFGLYSSDSSVFFSTSELDSG-NSSESS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   163 RAESTAIQPSEPHDVDTSKNGLSKKQHSEAQPEVQgnddeveeeddddddededededeDNNNNNRWLLIEQYPSDIVAY 242
Cdd:pfam03105 224 VDDEVEEELERNGWISPIKSKDKKKRPSEALDKVK------------------------TPDRTLKGFLDASRRDYLNRI 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   243 ENF------VSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDKTLGSSLRESYMKRV 296
Cdd:pfam03105 280 NKVnlrkakKKLKKAFIELYRGLELLKSYSELNRTAFRKILKKFDKVTSLNASKDYMKEV 339
ArsB COG1055
Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];
491-856 1.01e-29

Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];


Pssm-ID: 440675 [Multi-domain]  Cd Length: 415  Bit Score: 122.93  E-value: 1.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 491 WNpTIVLLLGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAE 570
Cdd:COG1055  53 WN-TILFLLGMMIIVAILDESGFFEWLAIKLARRAKGSPRRLLWLLGLLTALLSAFLDNDTTALLLTPVVLAIARRLGLN 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 571 sdfAKILIVGIALASNVGGIASPISSPQNIVALQNMDPaaGWGEWFAVSIPVSLLCIFSIWFLLSFGLLKDEHITLAKIR 650
Cdd:COG1055 132 ---PVPFLIAIVFAANIGGAATPIGNPTNIMIASAGGL--SFLDFLANLFPPSLVSLLVTLLVLYLLFRKELPAAPDLED 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 651 STKDTFTGVQWF-ISIVTIGTIVLWCLerrFDEVFG-DMGVIALVPIIVFFgtgLLTKEDFNNFL----WTVIVLAMGGV 724
Cdd:COG1055 207 DPKEAIKDRRLLrISLLVLALLLVGFV---LHSFLGlPPALIALLGAAVLL---LLARVDVREVLkkvdWSTLLFFIGLF 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 725 ALGKVVSSSGLLELIALKIgNAVSSLNTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGsrlADPHPRLFVLASGM 804
Cdd:COG1055 281 VVVGGLENTGLLDLLAELL-ASLTGGNLLLAALLILWLSAILSAVVDNVPLVAALLPLIPDLG---ATGNPEPLWLALAL 356
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113202 805 MCSLAmalptsgfPNMTAI-------MMENEAgKRYLKVS--DFLKAGIPATLISFVILLL 856
Cdd:COG1055 357 GATLG--------GNLTPIgsaanviVLGIAE-KKGIKISfgEFLKVGLPLTLLTLLIALL 408
Na_sulph_symp pfam00939
Sodium:sulfate symporter transmembrane region; There are also some members in this family that ...
407-866 2.38e-26

Sodium:sulfate symporter transmembrane region; There are also some members in this family that do not match the Prosite motif, and belong to the subfamily SODIT1.


Pssm-ID: 279307 [Multi-domain]  Cd Length: 472  Bit Score: 113.62  E-value: 2.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   407 IATLITIIVIFILLLSFPV---IDNREQNnCLALLVMVSLLWATEAIPLFVTSF----LVPFMTVFLKILRDENGspLSG 479
Cdd:pfam00939   4 WWKLLALLAVLLIILLLPApdgLPSKAWH-LFAIFIATIVGWILEPLPMAVIALfaisLSAILIGTLLAKALSWA--LSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   480 kestkviFSsmwNPTIVLLLGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVamFASMWISNVAAPVLCFSI 559
Cdd:pfam00939  81 -------FS---STTTWLVFGAFFISAAFEKTGLGRRIALVLVKKMGKRTLGLGYGLVFS--DLLLAPATPSNTARAGGI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   560 IQPLLRNLPA--ESDFAK--------ILIVGIALASNVGGIASPISSPQNIVALQNMDPAAG----WGEWFAVSIPVSLL 625
Cdd:pfam00939 149 VFPIIMSLPPafGSDPEKgserrigaYLMWTVYQSTSITSAMFLTAMAPNLLLLGLMNSILGvtitWASWFLAAIPPGVI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   626 CIFSIWFLLSFGLL-----KDEHITLAKIR-STKDTFTGVQWFISIVTIGTIVLWCLErrfDEVFGDMGVIALVPIIVFF 699
Cdd:pfam00939 229 LLLLAPLLLYVLYPpeiksVPDAKAIAKTElKELGPMTFREKALLGLFVLLLLLWIFG---GSLNIDATTVAIIGLALML 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   700 GTGLLTKEDF--NNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVSSLN----TFRVLLIFSALTLVVSSFISHI 773
Cdd:pfam00939 306 LLRILDWKDIvkNKGAWNTLIWLGGLIMLANGLERSGFIEWLGNTLSTSLSGFSpamaFIIILSLFYLSHYLFASATAHT 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   774 VAamvVLPIVHEVGSRLADPHPRLFVLASGMMCSLA-MALPTSGFPNMTAImmeneaGKRYLKVSDFLKAGIPATLISFV 852
Cdd:pfam00939 386 AA---MLPIFAAVAQAIPGAPPLLAALLLGFAISLGgFLTPYGTGPGPIYF------GSGYLKVKDWWRIGAILTIIGLL 456
                         490
                  ....*....|....
gi 19113202   853 ILLLIGTPIMRALG 866
Cdd:pfam00939 457 ILLLLGNWWWKPLG 470
SPX cd14447
Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX ...
2-92 3.75e-15

Domain found in Syg1, Pho81, XPR1, and related proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). This domain is found at the amino terminus of a variety of proteins. In the yeast protein Syg1, the N-terminus directly binds to the G-protein beta subunit and inhibits transduction of the mating pheromone signal. Similarly, the N-terminus of the human XPR1 protein binds directly to the beta subunit of the G-protein heterotrimer leading to increased production of cAMP. These findings suggest that members of this family are involved in G-protein associated signal transduction. The N-termini of several proteins involved in the regulation of phosphate transport, including the putative phosphate level sensors Pho81 from Saccharomyces cerevisiae and NUC-2 from Neurospora crassa, are also members of this family. The SPX domain of S. cerevisiae low-affinity phosphate transporters Pho87 and Pho90 auto-regulates uptake and prevents efflux. This SPX dependent inhibition is mediated by the physical interaction with Spl2. NUC-2 contains several ankyrin repeats. Several members of this family are annotated as XPR1 proteins: the xenotropic and polytropic retrovirus receptor confers susceptibility to infection with xenotropic and polytropic murine leukaemia viruses (MLV). Infection by these retroviruses can inhibit XPR1-mediated cAMP signaling and result in cell toxicity and death. The similarity between Syg1, phosphate regulators and XPR1 sequences has been previously noted, as has the additional similarity to several predicted proteins, of unknown function, from Drosophila melanogaster, Arabidopsis thaliana, Caenorhabditis elegans, Schizosaccharomyces pombe, S. cerevisiae, and many other diverse organisms.


Pssm-ID: 269894 [Multi-domain]  Cd Length: 143  Bit Score: 73.37  E-value: 3.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDEEtrLLEHERRSPDDRFMFALDKELQGIVEFYAPKE 81
Cdd:cd14447   1 KFGKRLREEAVPEWRDKYVDYKALKKLIKNLVASADEASNSSEALE--LSESGGEEFESEFFEALDAELEKVNEFYQELL 78
                        90
                ....*....|.
gi 19113202  82 KEIADQYGRIK 92
Cdd:cd14447  79 EELQELLKRLE 89
ArsB_NhaD_permease cd00625
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
671-857 3.24e-14

Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, antimonite, sulfate and organic anions across biological membranes in all three kingdoms of life. A typical anion permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump.


Pssm-ID: 238344 [Multi-domain]  Cd Length: 396  Bit Score: 75.36  E-value: 3.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 671 IVLWCLERRfdevfgDMGVIALVPIIVFFGTGLLTKED-FNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIgnAVSS 749
Cdd:cd00625   1 YVLIRPEKL------PRAVVALLGAVLLVLLGVVSPKEaLSAIDWETILLLFGMMILSAALEETGLFDRLAAKL--ARAS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 750 LNTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGSRLADPHPRLFVLASGMMCSLA-MALPTSGFPNMTAimmene 828
Cdd:cd00625  73 KGSRRLLLLLMLLTAALSAFFSNDATAVLLTPIVLALLRKLGLSPPVPLLLALAFAANIGgAATPIGNPPNLII------ 146
                       170       180
                ....*....|....*....|....*....
gi 19113202 829 AGKRYLKVSDFLKAGIPATLISFVILLLI 857
Cdd:cd00625 147 ASLSGLGFLDFLAFMAPPALGLLLLLLGL 175
P_permease cd01116
Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible ...
478-853 5.02e-13

Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible for classic phenotype of oculocutaneous albinism type 2 (OCA2). Although the precise function of the P protein is unknown, it was predicted to regulate the intraorganelle pH, together with the ATP-driven proton pump. It shows significant sequence similarity to the Na+/H+ antiporter NhaD from Vibrio parahaemolyticus. Both proteins belong to ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease contains 8-13 transmembrane domains.


Pssm-ID: 238536 [Multi-domain]  Cd Length: 413  Bit Score: 71.90  E-value: 5.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 478 SGKESTKVIFSSMWNPTIVLLLGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCF 557
Cdd:cd01116  33 TLSPDLETIVSWVDWETLALLLGMMIIVSILSETGVFEYLAIWAVKISKGRPWRLLLLLGLLTAFLSAFLDNVTTVLLMV 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 558 SIIQPLLRNLPAesdFAKILIVGIALASNVGGIASPISSPQNIVALQNMDpaAGWGEWFAVSIPVSLLCIFSIwFLLSFG 637
Cdd:cd01116 113 PVTIRLCEVLGL---NPVPVLISEVIAANIGGAATLIGDPPNIMIGSAAG--LTFNDFLLHMLPSVVLALVVT-FILLYF 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 638 LLKDEHITLAKIRSTKDTFT--------GVQWFISIVTIGTIVLWCLErrfDEVFGDMGVIALVPIIVFFGTGLltKEDF 709
Cdd:cd01116 187 LYRNILKAREEDVLALAELEpkypikdkVLLLKSLTILTLVIIGFVLH---SPLGVSLGWIALLGALLLLLLAD--KLDF 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 710 NNFL----WTVIVLAMGGVALGKVVSSSGLLELIALKIGNAVSSLNTFRVLLI--FSALtlvVSSFISHIVAAMVVLPIV 783
Cdd:cd01116 262 EDVLsrveWDTLLFFAGLFVLVGGLEELGIIEWIAELLVGVILGRIAVAVILIlwISAL---LSAFIDNIPVTATMIPIV 338
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113202 784 HEVGSRL-ADPHPRLFVLASGmmCSLAMALPTSGFP-NMTAIMMENEAGkryLKVS--DFLKAGIPATLISFVI 853
Cdd:cd01116 339 KDLASQLgIPLLPLWWALALG--ACLGGNGTLIGASaNVVAAGIAEQHG---YKISfwEFLKVGFPIMLVSLIL 407
YbiR_permease cd01117
Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to ...
492-857 1.94e-12

Putative anion permease YbiR. Based on sequence similarity, YbiR proteins are predicted to function as anion translocating permeases in eubacteria, archaea and plants. They belong to ArsB/NhaD superfamily of permeases that have been shown to translocate sodium, sulfate, arsenite and organic anions. A typical ArsB/NhaD permease is composed of 8-13 transmembrane domains.


Pssm-ID: 238537 [Multi-domain]  Cd Length: 384  Bit Score: 70.00  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 492 NPTIVLLLGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNvaaPVLCFSIIqPL------LR 565
Cdd:cd01117  40 DLDTIILLFGLMVVSAALELSGFFDALGSRILVKAGSPRRLLFLLVLLSGILSALLTN---DTACLVFT-PIvlelarVA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 566 NLPAesdfaKILIVGIALASNVGGIASPISSPQNIV--ALQNMDpaagWGEWFAVSIPVSLLCIFSIWFLLSF---GLLK 640
Cdd:cd01117 116 GLPP-----IPLLLALATAANIGSAATPIGNPQNLLiaSESGIS----FPFFLAAMAPLALLGLLLLLILLLVlfpGELK 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 641 DEHITLAKIRSTKDTFTGVqWFISIVTIGTIVLWCLERRFDEVFgdmgVIALVPIIVFFGTGLLTKEDFNNFLWTVIVLA 720
Cdd:cd01117 187 GLPLDKATKEEGVGARKLA-VKLLVLILLLLVAFLALLGVIPLW----TAALVAAVLLLLTRLKPRRVLKKVDWGLLLFF 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 721 MGGVALGKVVSSSGLLELIALkignavsSLNTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEvgsrlADPHPRLfvl 800
Cdd:cd01117 262 AGLFILVGGFAQGLPLEGLSR-------LLPLLDSVLSLFLVSIGLSQLISNVPAVLLLLPFLPS-----ADEKDWL--- 326
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113202 801 asgmmcSLAMALPTSGFPNMTA-----IMMENEAGKRY-LKVSDFLKAGIPATLISFVILLLI 857
Cdd:cd01117 327 ------LLAAGSTIAGNLTLLGsaanlIVAEAAERRGVrLSFGEFLKYGVPLTLLTAAIGILW 383
SPX_GDE1_like cd14484
SPX domain of Gde1 and similar proteins; This region has been named the SPX domain after (Syg1, ...
2-92 2.47e-11

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: 62.16  E-value: 2.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEHEQitlqqgAPDEETRLLEherrspddrFMFALDKELQGIVEFYAPKE 81
Cdd:cd14484   1 KFGKNLPRNQVPEWSSSYINYKGLKKLIKAIAEQQ------KEGVKVDLAE---------FFFALDRNLEDVDTFYNKKF 65
                        90
                ....*....|....*...
gi 19113202  82 KEIA-------DQYGRIK 92
Cdd:cd14484  66 AEYSrrlklllDRYGFSP 83
ArsB COG1055
Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];
659-857 4.08e-10

Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];


Pssm-ID: 440675 [Multi-domain]  Cd Length: 415  Bit Score: 62.84  E-value: 4.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 659 VQWFISIVTIGTIVLWCLERRFdevfGDMGVIALVPIIVFFGTGLLTKED-FNNFLWTVIVLAMGGVALGKVVSSSGLLE 737
Cdd:COG1055   1 MMILALAIFVLTYLLIILEPRG----LNRAVAALLGAALLLLLGVVSLEDaLEAIDWNTILFLLGMMIIVAILDESGFFE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 738 LIALKIGNAVSSlNTFRVLLIFSALTLVVSSFISHIVAAMVVLPIVHEVGSRLADPhPRLFVLASGMMCSLA-MALPTSG 816
Cdd:COG1055  77 WLAIKLARRAKG-SPRRLLWLLGLLTALLSAFLDNDTTALLLTPVVLAIARRLGLN-PVPFLIAIVFAANIGgAATPIGN 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19113202 817 FPNmtaIMMENEAGkryLKVSDFLKAGIPATLISFVILLLI 857
Cdd:COG1055 155 PTN---IMIASAGG---LSFLDFLANLFPPSLVSLLVTLLV 189
ArsB_NhaD_permease cd00625
Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, ...
434-634 4.25e-10

Anion permease ArsB/NhaD. These permeases have been shown to translocate sodium, arsenate, antimonite, sulfate and organic anions across biological membranes in all three kingdoms of life. A typical anion permease contains 8-13 transmembrane helices and can function either independently as a chemiosmotic transporter or as a channel-forming subunit of an ATP-driven anion pump.


Pssm-ID: 238344 [Multi-domain]  Cd Length: 396  Bit Score: 62.65  E-value: 4.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 434 CLALLVMVSLLWATEAIPLFVTSFLVPFMTVFLKILRDENgsplsgkestkVIFSSMWNpTIVLLLGGFTIAAALSKYHI 513
Cdd:cd00625 213 LLLLLLFVLLFFFLIPLGLIALLGALLLLLLLVRGLDPEE-----------VLKSVDWG-TLLFFAGLFVLVGALESTGL 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 514 AKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAApvlcFSIIQPLLrnlpAESDFAKILIVGIALASNVGGIASP 593
Cdd:cd00625 281 LEWLAELLVALVGLPPLAALLLIGLLSALLSNFISNVPT----VALLLPIA----ASLAPPEPAWLALALGSTLGGNLTL 352
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19113202 594 ISSPQNIVALQ---NMDPAAGWGEWFAVSIPVSLLCIFSIWFLL 634
Cdd:cd00625 353 IGSLANLIPLGaaeNAGVGISFGEFLKVGLPLTLLSLVVSLLYL 396
SPX_XPR1_like cd14477
SPX domain of the xenotropic and polytropic retrovirus receptor 1 (XPR1) and related proteins; ...
2-145 4.62e-10

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: 59.22  E-value: 4.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKLIYsleheqiTLQQGAPDEETRLLEHERR---SPDDRFMFALDKELQGIVEFYA 78
Cdd:cd14477   1 KFGEHLSAHITPEWRKQYINYEELKAMLY-------AAVEQAPSPEVTDEDVVKRyfaKFEEEFFQECDKELAKVNTFFS 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113202  79 PKEKEIADQYGRIKGEFETYENEymsqgnninyptperlQKSSASRKSGRMARSQELPRITSSNREI 145
Cdd:cd14477  74 EKLAEAQRKFATLKNELLSSLEA----------------QGESGAASSLIRRVFALLRKERVKPRKL 124
CitT COG0471
Di- and tricarboxylate antiporter [Carbohydrate transport and metabolism];
435-636 1.56e-08

Di- and tricarboxylate antiporter [Carbohydrate transport and metabolism];


Pssm-ID: 440239 [Multi-domain]  Cd Length: 369  Bit Score: 57.47  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 435 LALLVMVSLLWATEA---IPLFVTSFLVPFMTVFLKILrdengsplSGKESTKVIfssMWNpTIVLLLGGFTIAAALSKY 511
Cdd:COG0471 178 LAIFALTVLLWITGSlhgIPIAVVALLGAVLLLLTGVL--------TWKDAYKSI---PWG-VLLLFGGGLALGAALEKT 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 512 HIAKRLATSILAHAGRK-PRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLLRNLPAEsdfAKILIVGIALASNvGGI 590
Cdd:COG0471 246 GLAAWLADALLPLLGGLsPLLLLLLLALLTLLLTEFASNTATAALLLPIAISLAQALGVN---PLPLALAVAFAAS-CAF 321
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 19113202 591 ASPISSPQNIVALqnmdpAAGW---GEWFAVSIPVSLLCIFSIWFLLSF 636
Cdd:COG0471 322 LLPVGTPPNAIVY-----GSGYykfKDFLKVGLPLNLIGLVVLLLLGPL 365
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
243-282 5.63e-08

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: 52.54  E-value: 5.63e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 19113202 243 ENFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDK 282
Cdd:cd14480  96 EDFKELEEELDDILADVHDLAKFTRLNYTGFLKIVKKHDK 135
SPX_SYG1_like cd14475
SPX domain of the yeast plasma protein Syg1 and related proteins; This region has been named ...
2-133 8.73e-08

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: 51.80  E-value: 8.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKLIYSLEheqitlqqgapdeetrlleherrspddrFMFALDKELQGIVEFYAPKE 81
Cdd:cd14475   1 KFAKYLEENLVPEWRKKYLDYKGGKKKIKARE----------------------------FFEFLDSELDKVESFYKEKE 52
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 19113202  82 KEIADQYGRIKGEFETYENEYMSQGNNINYPTPERLQKSSASRKSGRMARSQ 133
Cdd:cd14475  53 DEARERLDLLRDQLHELRDHRIQEADDGRRDYSRRPEQNAHDPVSYRSARRK 104
ArsB COG1055
Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];
477-639 1.03e-07

Na+/H+ antiporter NhaD or related arsenite permease [Inorganic ion transport and metabolism];


Pssm-ID: 440675 [Multi-domain]  Cd Length: 415  Bit Score: 55.13  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 477 LSGKESTKVIFSSMWNPTIVLLLGGFTIAAALSKYHIAKRLATSILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLC 556
Cdd:COG1055 255 LLARVDVREVLKKVDWSTLLFFIGLFVVVGGLENTGLLDLLAELLASLTGGNLLLAALLILWLSAILSAVVDNVPLVAAL 334
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 557 FSIIQPLlrnlpAESDFAKILIVGIALASNVGGIASPISSPQNIVALQNMDPAA---GWGEWFAVSIPVSLLCIFSIWFL 633
Cdd:COG1055 335 LPLIPDL-----GATGNPEPLWLALALGATLGGNLTPIGSAANVIVLGIAEKKGikiSFGEFLKVGLPLTLLTLLIALLY 409

                ....*.
gi 19113202 634 LSFGLL 639
Cdd:COG1055 410 LLLLYF 415
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
2-83 3.24e-07

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: 50.33  E-value: 3.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKL---IYSLEHEQITLQQGAPDEETrllEHERrspddRFMFALDKELQGIVEFYA 78
Cdd:cd14476   1 KFGKEFESQMVPEWQEAYVDYKQLKKDlkrIQKFRDEYETTFLEAAEEGG---EYEL-----VFFRRLDDELNKVNKFYR 72

                ....*
gi 19113202  79 PKEKE 83
Cdd:cd14476  73 SKVEE 77
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
2-83 6.01e-07

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: 49.94  E-value: 6.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAV--PEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDEETRLLEHERRSPD---------DRFMFALDKEL 70
Cdd:cd14483   1 KFGKYIQARQLelPEYSAYFLDYKALKKLIKSLAAPRVAAAAALLAGGRPLSPDGTDESDaqtslqankAAFFFKLEREL 80
                        90
                ....*....|...
gi 19113202  71 QGIVEFYAPKEKE 83
Cdd:cd14483  81 EKVNAFYLQKEAE 93
SPX_VTC2_like cd14480
SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been ...
2-118 1.17e-05

SPX domain of the vacuolar transport chaperone Vtc2 and similar proteins; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The domain is found at the amino terminus of a variety of proteins. Vtc2 is part of the Saccharomyces cerevisiae membrane-integral VTC complex, together with Vtc1, Vtc3, and Vtc4. It contains an N-terminal SPX domain next to a central polyphosphate polymerase domain and a C-terminal domain of unknown function.


Pssm-ID: 269901 [Multi-domain]  Cd Length: 135  Bit Score: 45.61  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQFNAVPEWSESYIAYSNLKKLiysLEHEQITLQQGAPDEETRLLEherrspddrfmfALDKELQGIVEFYAPKE 81
Cdd:cd14480   1 KFGKTLKSSIYPPWKDYYIDYDKLKKL---LKERETDRGWWTEDDERFFVE------------LLEVELEKVYTFQKEKY 65
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 19113202  82 KEIADqygRIKGEFETYENEYMSQGNNINYPTPERLQ 118
Cdd:cd14480  66 SELRR---RIDACEKKVKELVSNLDSSEDDPSEEDFK 99
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
262-282 2.44e-05

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: 44.95  E-value: 2.44e-05
                        10        20
                ....*....|....*....|.
gi 19113202 262 LISYVHLNYTGFSKILKKYDK 282
Cdd:cd14481 128 LENYSSLNYTGLVKILKKYDK 148
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
1-87 2.47e-05

SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; This region has been named the SPX domain after (Syg1, Pho81 and XPR1). The SPX domain is found at the amino terminus of a variety of proteins. This family, mostly found in plants, contains a C-terminal MFS domain (major facilitator superfamily), suggesting a function as a secondary transporter. The function of this N-terminal region is unclear, although it might be involved in regulating transport.


Pssm-ID: 269900 [Multi-domain]  Cd Length: 140  Bit Score: 44.97  E-value: 2.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   1 MKFSHSLQFNAVPEWSESYIAYSNLKKLIyslehEQITLQQgapDEETRllehERRSPDDRFMFALDKELQGIVEFYAPK 80
Cdd:cd14479   1 VNFGKKLKEDQIPEWEGYYINYKLLKKKV-----KQYVQQT---QDGGQ----DRRDVLKDFSKLLDDQIEKIVLFLLEQ 68

                ....*..
gi 19113202  81 EKEIADQ 87
Cdd:cd14479  69 QGLLASR 75
SPX_PHO81_NUC-2_like cd14483
SPX domain of Pho81, NUC-2, and similar proteins; This region has been named the SPX domain ...
244-283 1.32e-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: 43.39  E-value: 1.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 19113202 244 NFVSLKRKLTQLYVSIHDLISYVHLNYTGFSKILKKYDKT 283
Cdd:cd14483 121 SFVTLEEGFRQFERDLNKLQQFVELNATGFSKILKKWDKR 160
SPX-MFS_plant cd14479
SPX domain of proteins found in plants and stramenopiles; most have a C-terminal MFS domain; ...
261-285 1.43e-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: 42.66  E-value: 1.43e-04
                        10        20
                ....*....|....*....|....*
gi 19113202 261 DLISYVHLNYTGFSKILKKYDKTLG 285
Cdd:cd14479 111 KLLKFVELNATGLRKILKKFDKRFG 135
P_permease cd01116
Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible ...
687-857 1.53e-04

Permease P (pink-eyed dilution). Mutations in the human melanosomal P gene were responsible for classic phenotype of oculocutaneous albinism type 2 (OCA2). Although the precise function of the P protein is unknown, it was predicted to regulate the intraorganelle pH, together with the ATP-driven proton pump. It shows significant sequence similarity to the Na+/H+ antiporter NhaD from Vibrio parahaemolyticus. Both proteins belong to ArsB/NhaD superfamily of permeases that translocate sodium, arsenate, sulfate, and organic anions across biological membranes in all three kingdoms of life. A typical ArsB/NhaD permease contains 8-13 transmembrane domains.


Pssm-ID: 238536 [Multi-domain]  Cd Length: 413  Bit Score: 44.94  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 687 MGVIALVPIIVFFGTGLLtKEDFNNFLWTVIVLAMGGVALGKVVSSSGLLELIALKIGNaVSSLNTFRVLLIFSALTLVV 766
Cdd:cd01116  21 AGALWLVILGLATLSPDL-ETIVSWVDWETLALLLGMMIIVSILSETGVFEYLAIWAVK-ISKGRPWRLLLLLGLLTAFL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 767 SSFISHIVAAMVVLPIVHEVGSRLA-DPHPRLF--VLASGMMcslAMALPTSGFPNmtaIMMENEAGkryLKVSDFLKAG 843
Cdd:cd01116  99 SAFLDNVTTVLLMVPVTIRLCEVLGlNPVPVLIseVIAANIG---GAATLIGDPPN---IMIGSAAG---LTFNDFLLHM 169
                       170
                ....*....|....
gi 19113202 844 IPATLISFVILLLI 857
Cdd:cd01116 170 LPSVVLALVVTFIL 183
SPX_AtSPX1_like cd14481
SPX domain of the plant protein SPX1 and similar proteins; This region has been named the SPX ...
2-104 4.10e-04

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: 41.48  E-value: 4.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202   2 KFSHSLQF---NAVPEWSESYIAYSNLKKLIYSLEHEQITLQQGAPDEETRLLEHERRSPDDRFMFALDKELQGIVEFYA 78
Cdd:cd14481   1 KFGKSLKRqieETLPEWRDKFLSYKELKKLLKLISPGNADKPNSKRDRRGGGAARAMTKEEADFVRLLNAELDKFNAFFV 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 19113202  79 PKE-------KEIADQYGRIKGEFETYENEYMS 104
Cdd:cd14481  81 EKEeeyvirlKELQDRVAEAKETPRDSNEELMR 113
PLN00137 PLN00137
NHAD transporter family protein; Provisional
495-594 1.25e-03

NHAD transporter family protein; Provisional


Pssm-ID: 215071  Cd Length: 424  Bit Score: 42.37  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  495 IVLLLGGFTIAAALSKYHIAKRLATSILAhagRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSiiqpLLRNLPAESDFA 574
Cdd:PLN00137  69 VFFLLGAMTIVEIVDAHQGFKLVTDSITT---RSPRTLLWVVGFITFFLSSILDNLTTTIVMVS----LLRKLVPPSEYR 141
                         90       100
                 ....*....|....*....|
gi 19113202  575 KILIVGIALASNVGGIASPI 594
Cdd:PLN00137 142 KLLGAVVVVAANAGGAWTPI 161
PLN00136 PLN00136
silicon transporter; Provisional
487-601 4.82e-03

silicon transporter; Provisional


Pssm-ID: 215070 [Multi-domain]  Cd Length: 482  Bit Score: 40.36  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202  487 FSSMWNPTIVLLLGGFTIAAALSKYHIAKRLATsILAHAGRKPRSVLLTNMFVAMFASMWISNVAAPVLCFSIIQPLL-- 564
Cdd:PLN00136  58 YASIDLPILGLLFATMVVGSYLKNAGMFKHLGR-LLAWRSQGGRDLLCRVCVVTALASALFTNDTCCVVLTEFVLELAae 136
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19113202  565 RNLPAesdfaKILIVGIALASNVGGIASPISSPQNIV 601
Cdd:PLN00136 137 RNLPA-----KPFLLALASSANIGSSATPIGNPQNLV 168
GntT COG2610
H+/gluconate symporter GntT or related permease, GntP/DsdX family [Carbohydrate transport and ...
495-817 6.16e-03

H+/gluconate symporter GntT or related permease, GntP/DsdX family [Carbohydrate transport and metabolism];


Pssm-ID: 442022 [Multi-domain]  Cd Length: 440  Bit Score: 40.10  E-value: 6.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 495 IVLLLGGfTIAAALSKYHIAKRLATSILAHAGRKpRSVLltnmfvAMFASMWIsnVAAPVLC---FSIIQPLLRNLPAES 571
Cdd:COG2610  64 LVIGLGA-MLGKLLEDSGAAERIADTIIKKFGEK-RAPL------ALVLAGFI--LGIPVFFdvgFVILAPLAFSLARRA 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 572 DFAKILIVG-IALASNVG-GIASPISSPQNIVALQNMDPAAGWGEWFAVSIPVSLLC-IFSIWFLLSFGLLKDEHITLAK 648
Cdd:COG2610 134 GISKLLIGLaLAAGLSTThMLVPPTPGPLAAAGILGADLGAVILLGLIVAIPALIVGyLYAKWLGKKAPVPAPEGLAGEE 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 649 IRSTKDTFTGVQWFISIVTIGT-IVLWCLERRFDEVFGDMGVIALV-----PII-----VFFGTGLL----TKEDFNNFL 713
Cdd:COG2610 214 DEEEEDDEELPSFGLALLPILLpIVLILLGTIADLLPKDSALVQVLafigdPIIalligVLVAILLLrrglSREELMKIL 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113202 714 WT------VIVLAMG-GVALGKVVSSSGllelIALKIGNAVSSLNTFRVLLIFsaltlVVSSFI-----SHIVAAMVVLP 781
Cdd:COG2610 294 NEglkpagLILLITGaGGAFGAVLAASG----IGDAIADALSGLGLPPLLLAF-----LIAALLrgatgSATVAMITAAG 364
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 19113202 782 IVHEVGSRLaDPHPRLFVLASGMMCSLAMALPTSGF 817
Cdd:COG2610 365 ILAPLLLAL-GVSPELLVLAIGAGSGGLSHVNDSGF 399
SPX_PHO1_like cd14476
SPX domain of the plant protein PHOSPHATE1 (PHO1); This region has been named the SPX domain ...
245-285 8.27e-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: 37.62  E-value: 8.27e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 19113202 245 FVSLKRKLT--QLYVSIHDLISYVHLNYTGFSKILKKYDKTLG 285
Cdd:cd14476  92 LIAFRVKVEnpQFYRKLRLLKSYSFLNMLAFSKILKKYDKVTS 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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