|
Name |
Accession |
Description |
Interval |
E-value |
| EriC |
cd01031 |
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ... |
24-422 |
2.21e-176 |
|
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that mediate the extreme acid resistance response in eubacteria and archaea. This response allows bacteria to survive in the acidic environments by decarboxylation-linked proton utilization. As shown for Escherichia coli EriC, these channels can counterbalance the electric current produced by the outwardly directed virtual proton pump linked to amino acid decarboxylation. The EriC proteins belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge. In Escherichia coli EriC, a glutamate residue that protrudes into the pore is thought to participate in gating by binding to a Cl- ion site within the selectivity filter.
Pssm-ID: 238504 [Multi-domain] Cd Length: 402 Bit Score: 502.07 E-value: 2.21e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 24 VGLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPIYLIGLAICCILAAFFVGYLVKN-EPDIKGSGIPQVEGQLRGELSM 102
Cdd:cd01031 1 IGLLAGLVAVLFRLGIDKLGNLRLSLYDFAANNPPLLLVLPLISAVLGLLAGWLVKKfAPEAKGSGIPQVEGVLAGLLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 103 NWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFNAPIAGLLFVLEE 182
Cdd:cd01031 81 NWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSKWFKTSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 183 IHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLLALQKFYNRL-P 261
Cdd:cd01031 161 LRHSFSPLALLTALVASIAADFVSRLFFGLGPVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKSQDLYRKLkK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 262 LPAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPGGIFLPILTLGALIG 341
Cdd:cd01031 241 LPRELRVLLPGLLIGPLGLLLPEALGGGHGLILSLAGGNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 342 SFYGNIMVDFGMDPI-YIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAYIVNDLLGGNPIYESL 420
Cdd:cd01031 321 LLFGTILVQLGPIPIsAPATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMVVCLVAYLVADLLGGKPIYEAL 400
|
..
gi 1565315252 421 LE 422
Cdd:cd01031 401 LE 402
|
|
| ClcA |
COG0038 |
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism]; |
13-423 |
7.35e-117 |
|
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
Pssm-ID: 439808 [Multi-domain] Cd Length: 415 Bit Score: 350.98 E-value: 7.35e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 13 TQIYFILKGIFVGLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPIYLIGLAICCILAAFFVGYLVKN-EPDIKGSGIPQ 91
Cdd:COG0038 3 RLLRLLLLAVLVGILAGLAAVLFRLLLELATHLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRfAPEARGSGIPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 92 VEGQLRGELSMNWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFNA 171
Cdd:COG0038 83 VIEAIHLKGGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLSPEDRRILLAAGAAAGLAAAFNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 172 PIAGLLFVLEEIHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLL 251
Cdd:COG0038 163 PLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 252 ALQKFYNRLPLPAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPGGIFL 331
Cdd:COG0038 243 KVERLFKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGELSLLLLLLLLLLKLLATALTLGSGGPGGIFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 332 PILTLGALIGSFYGNIMVD-FGMDPIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAYIVNDL 410
Cdd:COG0038 323 PSLFIGALLGAAFGLLLNLlFPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLMIACVIAYLVSRL 402
|
410
....*....|...
gi 1565315252 411 LGGNPIYESLLER 423
Cdd:COG0038 403 LFPRSIYTAQLER 415
|
|
| Voltage_CLC |
pfam00654 |
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ... |
70-409 |
1.42e-102 |
|
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.
Pssm-ID: 425802 [Multi-domain] Cd Length: 344 Bit Score: 311.79 E-value: 1.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 70 AAFFVGYLVKN-EPDIKGSGIPQVEGQLRGELSMNWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQ-LFR 147
Cdd:pfam00654 1 GGLLAGWLVKRfAPEAAGSGIPEVKAALHGGRGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRrLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 148 SPSSEEKILISSGASSGLAAAFNAPIAGLLFVLEEIHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLK 227
Cdd:pfam00654 81 LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGNSPLFSVGEPGSLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 228 YYGSLVILGVLLGILGFIYQKVLLALQKFYNR-LPLPAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMI 306
Cdd:pfam00654 161 ELPLFILLGILCGLLGALFNRLLLKVQRLFRKlLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFNGNTSLSLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 307 IGLFVLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIMVDFGMD-PIYIKDFVVIAMAGYFTAIGKAPLTAIILVT 385
Cdd:pfam00654 241 LLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALLFPIgGLPPGAFALVGMAAFLAAVTRAPLTAIVIVF 320
|
330 340
....*....|....*....|....
gi 1565315252 386 EMVGSLNHLMPLGLAALVAYIVND 409
Cdd:pfam00654 321 ELTGSLQLLLPLMLAVLIAYAVSR 344
|
|
| PRK05277 |
PRK05277 |
H(+)/Cl(-) exchange transporter ClcA; |
18-425 |
1.75e-86 |
|
H(+)/Cl(-) exchange transporter ClcA;
Pssm-ID: 235385 [Multi-domain] Cd Length: 438 Bit Score: 273.31 E-value: 1.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 18 ILKGIFVGLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPIYLIGLAICCILAAFFVGY-LVKN-EPDIKGSGIPQVEGQ 95
Cdd:PRK05277 1 LFMAAVVGTLTGLVGVAFELAVDWVQNQRLGLLASVADNGLLLWIVAFLISAVLAMIGYfLVRRfAPEAGGSGIPEIEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 96 LRGELSMNWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEK-ILISSGASSGLAAAFNAPIA 174
Cdd:PRK05277 81 LEGLRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVLDIFRLRSDEARhTLLAAGAAAGLAAAFNAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 175 GLLFVLEEIHHSF--SPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLLA 252
Cdd:PRK05277 161 GILFVIEEMRPQFrySLISIKAVFIGVIMATIVFRLFNGEQAVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 253 LQKFYNRLP---------LPAYFHGFVPFLlilpiGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGG 323
Cdd:PRK05277 241 TQDLFDRLHggnkkrwvlMGGAVGGLCGLL-----GLLAPAAVGGGFNLIPIALAGNFSIGMLLFIFVARFITTLLCFGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 324 GLPGGIFLPILTLGALIGSFYGNIMVDFGMD-PIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAAL 402
Cdd:PRK05277 316 GAPGGIFAPMLALGTLLGLAFGMVAAALFPQyHIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCL 395
|
410 420
....*....|....*....|...
gi 1565315252 403 VAYIVNDLLGGNPIYESLLERLL 425
Cdd:PRK05277 396 GATLLAQFLGGKPIYSALLERTL 418
|
|
| TrkA_C |
pfam02080 |
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of ... |
442-506 |
1.95e-07 |
|
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of this domain is unknown. It has been suggested that it may bind an unidentified ligand. The domain is predicted to adopt an all beta structure.
Pssm-ID: 460440 [Multi-domain] Cd Length: 70 Bit Score: 48.37 E-value: 1.95e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1565315252 442 FPVTAESSLDGLMVRDFNWPK--NMLLISIRRGNQEILTHGDTIMNVGDILVILTDEANLPRIKQEI 506
Cdd:pfam02080 4 VTVPENSPLVGKTLKELNLPErfGVRIVAIRRGGRLIIPSGDTVLEAGDRLLVIGTPDDLAALRELL 70
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
444-504 |
4.25e-05 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 45.88 E-value: 4.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1565315252 444 VTAESSLDGLMVRDFNWPKNMLLISIRRGNQEILTHGDTIMNVGD-ILVILTDEANLPRIKQ 504
Cdd:PRK09496 385 AHETSKVVGKPLKDLKLPKGVLIGAIVRGGEVIIPTGDTVIEPGDhVIVFVLDKKFVPDVEK 446
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
442-491 |
6.84e-04 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 41.59 E-value: 6.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1565315252 442 FPVTAESSLDGLMVRDFNWPK--NMLLISIRRGNQEILTHGDTIMNVGDILV 491
Cdd:COG0569 245 VTVPEGSPLVGKTLKELDLREryGVTVVAIKRGGEVIIPSGDTVLEAGDELI 296
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EriC |
cd01031 |
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ... |
24-422 |
2.21e-176 |
|
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that mediate the extreme acid resistance response in eubacteria and archaea. This response allows bacteria to survive in the acidic environments by decarboxylation-linked proton utilization. As shown for Escherichia coli EriC, these channels can counterbalance the electric current produced by the outwardly directed virtual proton pump linked to amino acid decarboxylation. The EriC proteins belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge. In Escherichia coli EriC, a glutamate residue that protrudes into the pore is thought to participate in gating by binding to a Cl- ion site within the selectivity filter.
Pssm-ID: 238504 [Multi-domain] Cd Length: 402 Bit Score: 502.07 E-value: 2.21e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 24 VGLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPIYLIGLAICCILAAFFVGYLVKN-EPDIKGSGIPQVEGQLRGELSM 102
Cdd:cd01031 1 IGLLAGLVAVLFRLGIDKLGNLRLSLYDFAANNPPLLLVLPLISAVLGLLAGWLVKKfAPEAKGSGIPQVEGVLAGLLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 103 NWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFNAPIAGLLFVLEE 182
Cdd:cd01031 81 NWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSKWFKTSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 183 IHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLLALQKFYNRL-P 261
Cdd:cd01031 161 LRHSFSPLALLTALVASIAADFVSRLFFGLGPVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKSQDLYRKLkK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 262 LPAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPGGIFLPILTLGALIG 341
Cdd:cd01031 241 LPRELRVLLPGLLIGPLGLLLPEALGGGHGLILSLAGGNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 342 SFYGNIMVDFGMDPI-YIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAYIVNDLLGGNPIYESL 420
Cdd:cd01031 321 LLFGTILVQLGPIPIsAPATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMVVCLVAYLVADLLGGKPIYEAL 400
|
..
gi 1565315252 421 LE 422
Cdd:cd01031 401 LE 402
|
|
| ClcA |
COG0038 |
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism]; |
13-423 |
7.35e-117 |
|
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
Pssm-ID: 439808 [Multi-domain] Cd Length: 415 Bit Score: 350.98 E-value: 7.35e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 13 TQIYFILKGIFVGLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPIYLIGLAICCILAAFFVGYLVKN-EPDIKGSGIPQ 91
Cdd:COG0038 3 RLLRLLLLAVLVGILAGLAAVLFRLLLELATHLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRfAPEARGSGIPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 92 VEGQLRGELSMNWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFNA 171
Cdd:COG0038 83 VIEAIHLKGGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLSPEDRRILLAAGAAAGLAAAFNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 172 PIAGLLFVLEEIHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLL 251
Cdd:COG0038 163 PLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 252 ALQKFYNRLPLPAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPGGIFL 331
Cdd:COG0038 243 KVERLFKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGELSLLLLLLLLLLKLLATALTLGSGGPGGIFA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 332 PILTLGALIGSFYGNIMVD-FGMDPIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAYIVNDL 410
Cdd:COG0038 323 PSLFIGALLGAAFGLLLNLlFPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLMIACVIAYLVSRL 402
|
410
....*....|...
gi 1565315252 411 LGGNPIYESLLER 423
Cdd:COG0038 403 LFPRSIYTAQLER 415
|
|
| Voltage_CLC |
pfam00654 |
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ... |
70-409 |
1.42e-102 |
|
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.
Pssm-ID: 425802 [Multi-domain] Cd Length: 344 Bit Score: 311.79 E-value: 1.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 70 AAFFVGYLVKN-EPDIKGSGIPQVEGQLRGELSMNWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQ-LFR 147
Cdd:pfam00654 1 GGLLAGWLVKRfAPEAAGSGIPEVKAALHGGRGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRrLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 148 SPSSEEKILISSGASSGLAAAFNAPIAGLLFVLEEIHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLK 227
Cdd:pfam00654 81 LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGNSPLFSVGEPGSLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 228 YYGSLVILGVLLGILGFIYQKVLLALQKFYNR-LPLPAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMI 306
Cdd:pfam00654 161 ELPLFILLGILCGLLGALFNRLLLKVQRLFRKlLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFNGNTSLSLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 307 IGLFVLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIMVDFGMD-PIYIKDFVVIAMAGYFTAIGKAPLTAIILVT 385
Cdd:pfam00654 241 LLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALLFPIgGLPPGAFALVGMAAFLAAVTRAPLTAIVIVF 320
|
330 340
....*....|....*....|....
gi 1565315252 386 EMVGSLNHLMPLGLAALVAYIVND 409
Cdd:pfam00654 321 ELTGSLQLLLPLMLAVLIAYAVSR 344
|
|
| PRK05277 |
PRK05277 |
H(+)/Cl(-) exchange transporter ClcA; |
18-425 |
1.75e-86 |
|
H(+)/Cl(-) exchange transporter ClcA;
Pssm-ID: 235385 [Multi-domain] Cd Length: 438 Bit Score: 273.31 E-value: 1.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 18 ILKGIFVGLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPIYLIGLAICCILAAFFVGY-LVKN-EPDIKGSGIPQVEGQ 95
Cdd:PRK05277 1 LFMAAVVGTLTGLVGVAFELAVDWVQNQRLGLLASVADNGLLLWIVAFLISAVLAMIGYfLVRRfAPEAGGSGIPEIEGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 96 LRGELSMNWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEK-ILISSGASSGLAAAFNAPIA 174
Cdd:PRK05277 81 LEGLRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVLDIFRLRSDEARhTLLAAGAAAGLAAAFNAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 175 GLLFVLEEIHHSF--SPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLLA 252
Cdd:PRK05277 161 GILFVIEEMRPQFrySLISIKAVFIGVIMATIVFRLFNGEQAVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 253 LQKFYNRLP---------LPAYFHGFVPFLlilpiGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGG 323
Cdd:PRK05277 241 TQDLFDRLHggnkkrwvlMGGAVGGLCGLL-----GLLAPAAVGGGFNLIPIALAGNFSIGMLLFIFVARFITTLLCFGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 324 GLPGGIFLPILTLGALIGSFYGNIMVDFGMD-PIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAAL 402
Cdd:PRK05277 316 GAPGGIFAPMLALGTLLGLAFGMVAAALFPQyHIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCL 395
|
410 420
....*....|....*....|...
gi 1565315252 403 VAYIVNDLLGGNPIYESLLERLL 425
Cdd:PRK05277 396 GATLLAQFLGGKPIYSALLERTL 418
|
|
| Voltage_gated_ClC |
cd00400 |
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ... |
25-405 |
2.68e-66 |
|
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function.
Pssm-ID: 238233 [Multi-domain] Cd Length: 383 Bit Score: 218.97 E-value: 2.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 25 GLLTGIVVSLFRLSIEKLSDLV--RSIYEMSREQPIYLIGLAICCIlAAFFVGYLVKNEPDIKGSGIPQVEGQLRGELSM 102
Cdd:cd00400 1 GVLSGLGAVLFRLLIELLQNLLfgGLPGELAAGSLSPLYILLVPVI-GGLLVGLLVRLLGPARGHGIPEVIEAIALGGGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 103 NWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFNAPIAGLLFVLEE 182
Cdd:cd00400 80 LPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAAGIAAAFNAPLAGALFAIEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 183 IHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLLALQKFYNRLPL 262
Cdd:cd00400 160 LLGEYSVASLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFRRLPI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 263 PAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPGGIFLPILTLGALIGS 342
Cdd:cd00400 240 PPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLALAGELSLLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGA 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1565315252 343 FYGNIMVDFGMD-PIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAY 405
Cdd:cd00400 320 AFGLLLPALFPGlVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLMLAVVIAY 383
|
|
| PRK01862 |
PRK01862 |
voltage-gated chloride channel ClcB; |
21-423 |
6.96e-40 |
|
voltage-gated chloride channel ClcB;
Pssm-ID: 234987 [Multi-domain] Cd Length: 574 Bit Score: 152.21 E-value: 6.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 21 GIFVGLLTGIVVSLFRLSIEKLSDLVR----SIYEMSREQPIYL-IGL-AICCILAAFFVgyLVKNEPDIKGSGIPQVEG 94
Cdd:PRK01862 28 SAIVGIGGAFATTAFREGIELIQHLISghsgSFVEMAKSLPWYVrVWLpAAGGFLAGCVL--LLANRGARKGGKTDYMEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 95 QLRGELSMNWFSVLWKKfIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFNAPIA 174
Cdd:PRK01862 106 VALGDGVVPVRQSLWRS-ASSLLTIGSGGSIGREGPMVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGITSAYNAPIA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 175 GLLFVLEEI-----HHSFSPLvwltsFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKV 249
Cdd:PRK01862 185 GAFFVAEIVlgsiaMESFGPL-----VVASVVANIVMREFAGYQPPYEMPVFPAVTGWEVLLFVALGVLCGAAAPQFLRL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 250 LLALQKFYNRLPLPAYFHGFVPFLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPGGI 329
Cdd:PRK01862 260 LDASKNQFKRLPVPLPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILHAPWTWQALVAVLVAKLIATAATAGSGAVGGV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 330 FLPILTLGALIGSFYGNIMvdFGMDPIYIKDFVVIAMAG---YFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAYI 406
Cdd:PRK01862 340 FTPTLFVGAVVGSLFGLAM--HALWPGHTSAPFAYAMVGmgaFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYF 417
|
410
....*....|....*..
gi 1565315252 407 VNDLLGGNPIYESLLER 423
Cdd:PRK01862 418 TARALGTTSMYEITLRR 434
|
|
| EriC_like |
cd01034 |
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ... |
82-417 |
1.17e-39 |
|
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, are putative halogen ion (Cl-, Br- and I-) transport proteins found in eubacteria. They belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge.
Pssm-ID: 238506 [Multi-domain] Cd Length: 390 Bit Score: 148.14 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 82 PDIKGSGIPQV-------EGQLRGELSMNWFSVLwkKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSS-EE 153
Cdd:cd01034 49 PGAAGSGIPQViaalelpSAAARRRLLSLRTAVG--KILLTLLGLLGGASVGREGPSVQIGAAVMLAIGRRLPKWGGlSE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 154 KILISSGASSGLAAAFNAPIAGLLFVLEEIHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLV 233
Cdd:cd01034 127 RGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRFSGLVLLAVIAAGLVSLAVLGNYPYFGVAAVALPLGEAWLLVL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 234 ILGVLLGILGFIYQKVLLALQKF---------YNRLPLPAYFHGFVPFLLILPIGYLWPSTlGGGNQIVLAFGHASLPIi 304
Cdd:cd01034 207 VCGVVGGLAGGLFARLLVALSSGlpgwvrrfrRRRPVLFAALCGLALALIGLVSGGLTFGT-GYLQARAALEGGGGLPL- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 305 miiGLFVLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIMvdfgmDPIYIKDFVVIAMAGYFTAIGKAPLTAIILV 384
Cdd:cd01034 285 ---WFGLLKFLATLLSYWSGIPGGLFAPSLAVGAGLGSLLAALL-----GSVSQGALVLLGMAAFLAGVTQAPLTAFVIV 356
|
330 340 350
....*....|....*....|....*....|...
gi 1565315252 385 TEMVGSLNHLMPLGLAALVAYIVNDLLGGNPIY 417
Cdd:cd01034 357 MEMTGDQQMLLPLLAAALLASGVSRLVCPEPLY 389
|
|
| ClC_6_like |
cd03685 |
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ... |
22-422 |
3.04e-36 |
|
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. Proteins in this family are ubiquitous in eukarotes and their functions are unclear. They are expressed in intracellular organelles membranes. This family belongs to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. ClC chloride ion channel superfamily perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, and transepithelial transport in animals.
Pssm-ID: 239657 [Multi-domain] Cd Length: 466 Bit Score: 140.10 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 22 IFVGLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPIYLIGL---AICCILAAFFVGYLVKN-EPDIKGSGIPQVEGQLR 97
Cdd:cd03685 37 LLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIEKGRLFTAFlvyLGLNLVLVLVAALLVAYiAPTAAGSGIPEVKGYLN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 98 G--ELSMNWFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQ--------------LFRSpSSEEKILISSGA 161
Cdd:cd03685 117 GvkIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIAAGLSQggstslrldfrwfrYFRN-DRDKRDFVTCGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 162 SSGLAAAFNAPIAGLLFVLEEIhHSF--SPLVWLTSFASAI---TANFVSLYFFGL------RPVLYLGDLPSLPLKYY- 229
Cdd:cd03685 196 AAGVAAAFGAPVGGVLFSLEEV-ASFwnQALTWRTFFSSMIvtfTLNFFLSGCNSGkcglfgPGGLIMFDGSSTKYLYTy 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 230 ---GSLVILGVLLGILGFIYQKVLLALQKFYNRlplpaYFHGFVPFLLILpigylwpstlgggnQIVLAFGHASLPIIMI 306
Cdd:cd03685 275 felIPFMLIGVIGGLLGALFNHLNHKVTRFRKR-----INHKGKLLKVLE--------------ALLVSLVTSVVAFPQT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 307 IGLF-VLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIMVD-FGMDPIYIKDFVVIAMAGYFTAIGKAPLTAIILV 384
Cdd:cd03685 336 LLIFfVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSyFGFTSIDPGLYALLGAAAFLGGVMRMTVSLTVIL 415
|
410 420 430
....*....|....*....|....*....|....*...
gi 1565315252 385 TEMVGSLNHLMPLGLAALVAYIVNDLLgGNPIYESLLE 422
Cdd:cd03685 416 LELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQ 452
|
|
| ClC_euk |
cd01036 |
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ... |
25-418 |
2.04e-33 |
|
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) channel proteins that perform a variety of functions including cell volume regulation, membrane potential stabilization, charge compensation necessary for the acidification of intracellular organelles, signal transduction and transepithelial transport. They are also involved in many pathophysiological processes and are responsible for a number of human diseases. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. Some proteins possess long C-terminal cytoplasmic regions containing two CBS (cystathionine beta synthase) domains of putative regulatory function.
Pssm-ID: 238507 [Multi-domain] Cd Length: 416 Bit Score: 131.31 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 25 GLLTGIVVSLFRLSIEKLSDLVRSIYEMSREQPI--YLIGLAICCILAAFFVGYLVKNEPDIKGSGIPQVEGQLRG---E 99
Cdd:cd01036 1 GLLMGLVAVVLDYAVESSLDAGQWLLRRIPGSYLlgYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGvhlP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 100 LSMNwFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQ--------------LFRSPSsEEKILISSGASSGL 165
Cdd:cd01036 81 MYLS-IRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQgrsrtlgchvhlfqLFRNPR-DRRDFLVAGAAAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 166 AAAFNAPIAGLLFVLEEIHHSFS-PLVWLTSFASAITANFVSLYF-------------FGLRPVLYLGDLPSLPLKYYGS 231
Cdd:cd01036 159 ASAFGAPIGGLLFVLEEVSTFFPvRLAWRVFFAALVSAFVIQIYNsfnsgfelldrssAMFLSLTVFELHVPLNLYEFIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 232 LVILGVLLGILGFIYQKVLLALQKFYNRLPLPayFHGFVPFLLilpigylwpstlgggnQIVLAFGHASLPIIMIIGLF- 310
Cdd:cd01036 239 TVVIGVICGLLAALFVRLSIIFLRWRRRLLFR--KTARYRVLE----------------PVLFTLIYSTIHYAPTLLLFl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 311 VLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIMVDFGMDPIYIKDFVVIAMAGYFTAIGKAPLTA---------I 381
Cdd:cd01036 301 LIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIGAESATLWADPGVYALIGAAAFLGgttrltfsiC 380
|
410 420 430
....*....|....*....|....*....|....*..
gi 1565315252 382 ILVTEMVGSLNHLMPLGLAALVAYIVNDLLgGNPIYE 418
Cdd:cd01036 381 VIMMELTGDLHHLLPLMVAILIAKAVADAF-CESLYH 416
|
|
| ClC_3_like |
cd03684 |
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ... |
25-422 |
3.93e-30 |
|
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 was initially cloned from rat kidney. Expression of ClC-3 produces outwardly-rectifying Cl currents that are inhibited by protein kinase C activation. It has been suggested that ClC-3 may be a ubiquitous swelling-activated Cl channel that has very similar characteristics to those of native volume-regulated Cl currents. The function of ClC-4 is unclear. Studies of human ClC-4 have revealed that it gives rise to Cl currents that rapidly activate at positive voltages, and are sensitive to extracellular pH, with currents decreasing when pH falls below 6.5. ClC-4 is broadly distributed, especially in brain and heart. ClC-5 is predominantly expressed in the kidney, but can be found in the brain and liver. Mutations in the ClC-5 gene cause certain hereditary diseases, including Dent's disease, an X-chromosome linked syndrome characterised by proteinuria, hypercalciuria, and kidney stones (nephrolithiasis), leading to progressive renal failure. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl- and I-) channel proteins, that perform a variety of functions including cell volume regulation, the membrane potential stabilization, transepithelial chloride transport and charge compensation necessary for the acidification of intracellular organelles.
Pssm-ID: 239656 Cd Length: 445 Bit Score: 122.33 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 25 GLLTGIVVSLFRLSIEKLSDLVRSIYEMsreqPIYLIGlaicCILAAFFVGYLVKN-EPDIKGSGIPQVEGQL-----RG 98
Cdd:cd03684 1 GIAIGLIAGLIDIIASWLSDLKEGYCNY----IIYVLL----ALLFAFIAVLLVKVvAPYAAGSGIPEIKTILsgfiiRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 99 ELSmnwFSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLF---RSPSSEEKILISSGASSGLAAAFNAPIAG 175
Cdd:cd03684 73 FLG---KWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFpkyRRNEAKRREILSAAAAAGVAVAFGAPIGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 176 LLFVLEEIHHSFSPLVWLTSFASAITANFV--SLYFFG-----LRPVLYLGDLPSLPLKYYgslVILGVLLGILGFIYQK 248
Cdd:cd03684 150 VLFSLEEVSYYFPLKTLWRSFFCALVAAFTlkSLNPFGtgrlvLFEVEYDRDWHYFELIPF---ILLGIFGGLYGAFFIK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 249 VLLALQKFYNRLPLPAYFHGFVPFLLILP--IGYLWPSTLGGGNQIV-LAFG------------------HASLPIIMII 307
Cdd:cd03684 227 ANIKWARFRKKSLLKRYPVLEVLLVALITalISFPNPYTRLDMTELLeLLFNecepgddnslccyrdppaGDGVYKALWS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 308 GLF--VLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIM---------------VDFGMDPIYIKDFVVIAMAGYF 370
Cdd:cd03684 307 LLLalIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGILVeqlaysypdsiffacCTAGPSCITPGLYAMVGAAAFL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1565315252 371 TAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAYIVNDLLGGNPIYESLLE 422
Cdd:cd03684 387 GGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWVADAIGKEGIYDAHIH 438
|
|
| ClC_like |
cd01033 |
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ... |
18-407 |
1.13e-29 |
|
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) transporters found in eubacteria. They belong to the ClC superfamily of halogen ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge.
Pssm-ID: 238505 [Multi-domain] Cd Length: 388 Bit Score: 120.09 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 18 ILKGIFVGLLT----GIVVSLFRLSIEKLSDLVRSIYEMSReqpiyLIGLAICCILAAFFVGYLVKnepdiKGSGIPQVE 93
Cdd:cd01033 2 VGAGLGGGLLTlllhGVQHLAFGYSEGSFLTGVAAVSPIRR-----ALSLTVGGLIAGLGWYLLRR-----KGKKLVSIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 94 GQLRGELSMNwfsvLWKKFIGGVL---SVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFN 170
Cdd:cd01033 72 QAVRGKKRMP----FWETIIHAVLqivTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVADRRLLVACAAGAGLAAVYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 171 APIAGLLFVLEEIHHSFSPLVWLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLkyygsLVILGVLLG-ILGFIYQKV 249
Cdd:cd01033 148 VPLAGALFALEILLRTISLRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTP-----LLIWALLAGpVLGVVAAGF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 250 LLALQKFYNRLPLPAYFHGFVP--FLLILPIGYLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPG 327
Cdd:cd01033 223 RRLSQAARAKRPKGKRILWQMPlaFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSLLLILLVLKIVATLLALRAGAYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 328 GIFLPILTLGALIGSFYGnIMVDFGMDPIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVG-SLNHLMPLGLAALVAYI 406
Cdd:cd01033 303 GLLTPSLALGALLGALLG-IVWNALLPPLSIAAFALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGAVA 381
|
.
gi 1565315252 407 V 407
Cdd:cd01033 382 V 382
|
|
| ClC_1_like |
cd03683 |
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ... |
24-421 |
2.91e-26 |
|
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ClC-1 is expressed in skeletal muscle and its mutation leads to both recessively and dominantly-inherited forms of muscle stiffness or myotonia. ClC-K is exclusively expressed in kidney. Similarly, mutation of ClC-K leads to nephrogenic diabetes insipidus in mice and Bartter's syndrome in human. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl-, Br- and I-) channel proteins, that perform a variety of functions including cell volume regulation, regulation of intracelluar chloride concentration, membrane potential stabilization, charge compensation necessary for the acidification of intracellular organelles and transepithelial chloride transport.
Pssm-ID: 239655 [Multi-domain] Cd Length: 426 Bit Score: 110.80 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 24 VGLLTGIVVSLFRLSIEKLSD----LVRSIYEMSREQPIYLIGLAICCILAAFFVGYLVKnePDIKGSGIPQVEGQLRGE 99
Cdd:cd03683 8 LGILMALISIAMDFAVEKLLNarrwLYSLLTGNSLLQYLVWVAYPVALVLFSALFCKYIS--PQAVGSGIPEMKTILRGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 100 LSMNW--FSVLWKKFIGGVLSVGAGLFLGREGPSIQLGASIGQ------GAGQLFRSPSSEEKILISSGASSGLAAAFNA 171
Cdd:cd03683 86 VLPEYltFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAAllskltTFFSGIYENESRRMEMLAAACAVGVACTFGA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 172 PIAGLLFVLEEIHHSFSPL-VWLTSFASAITAN--FVSLYFFGLRPVLYLG-----------DLPSLPLkyygsLVILGV 237
Cdd:cd03683 166 PIGGVLFSIEVTSTYFAVRnYWRGFFAATCGAFtfRLLAVFFSDQETITALfkttffvdfpfDVQELPI-----FALLGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 238 LLGILG----FIYQKVLLALQkfYNRLplpayfhgFVPFLLILPIGYLwpstlgggnqIVLAFGHASL--PIIMIIGLFV 311
Cdd:cd03683 241 ICGLLGalfvFLHRKIVRFRR--KNRL--------FSKFLKRSPLLYP----------AIVALLTAVLtfPFLTLFLFIV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 312 LRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIMVDFGMDPIYIKDFVVIAMAGYfTAIGKAPLTAII--------L 383
Cdd:cd03683 301 VKFVLTALAITLPVPAGIFMPVFVIGAALGRLVGEIMAVLFPEGIRGGISNPIGPGGY-AVVGAAAFSGAVthtvsvavI 379
|
410 420 430
....*....|....*....|....*....|....*...
gi 1565315252 384 VTEMVGSLNHLMPLGLAALVAYIVNDLLgGNPIYESLL 421
Cdd:cd03683 380 IFELTGQISHLLPVLIAVLISNAVAQFL-QPSIYDSII 416
|
|
| PRK01610 |
PRK01610 |
putative voltage-gated ClC-type chloride channel ClcB; Provisional |
111-419 |
5.85e-24 |
|
putative voltage-gated ClC-type chloride channel ClcB; Provisional
Pssm-ID: 234963 Cd Length: 418 Bit Score: 104.09 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 111 KFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFrSPSSEEKILISSGASSGLAAAFNAPIAGLLFVLEEIH-----H 185
Cdd:PRK01610 103 KSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF-TPRQEWKLWIACGAAAGMASAYHAPLAGSLFIAEILFgtlmlA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 186 SFSPLVwltsfASAITANFVSLYFFGLRPVLYLGDL-PSLPLKYYGSLVILGVLLGILGFIYQKVLLALQKFYNRL---- 260
Cdd:PRK01610 182 SLGPVV-----ISAVVALLTTNLLNGSDALLYNVQLsVTVQARDYALIISTGLLAGLCGPLLLTLMNASHRGFVSLklap 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 261 PLPAYFHGFVPFLLILpigyLWPSTLGGGNQIVLAFGHASLPIIMIIGLFVLRFVFSMISYGGGLPGGIFLPILTLGALI 340
Cdd:PRK01610 257 PWQLALGGLIVGLLSL----FTPAVWGNGYSVVQSFLTAPPLLMLIAGIFLCKLLAVLASSGSGAPGGVFTPTLFVGLAI 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 341 GSFYGNIMVDFGMDPIYIKDFVVIA-MAGYFTAIGKAPLTAIILVTEMVGSLNHLMPLGLAALVAYIVNDLLGGNPIYES 419
Cdd:PRK01610 333 GMLYGRSLGLWLPDGEEITLLLGLTgMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLRRDSIYRQ 412
|
|
| ClC_sycA_like |
cd03682 |
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ... |
21-408 |
4.19e-22 |
|
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it facilitates acid resistance in acidic soil. Mutation of this gene (sycA) in Rhizobium tropici CIAT899 causes serious deficiencies in nodule development, nodulation competitiveness, and N2 fixation on Phaseolus vulgaris plants, due to its reduced ability for acid resistance. This family is part of the ClC chloride channel superfamiy. These proteins catalyse the selective flow of Cl- ions across cell membranes and Cl-/H+ exchange transport. These proteins share two characteristics that are apparently inherent to the entire ClC chloride channel superfamily: a unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge.
Pssm-ID: 239654 [Multi-domain] Cd Length: 378 Bit Score: 98.03 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 21 GIFVGLLTGIVVSLFRLSIEKLSDLvrsiyemsREQPIYLIGLaicCILAAFFVGYLVKN--EPDIKGSGIPQVEGQLRG 98
Cdd:cd03682 2 ALLIGLLVGSASALFLWSLDWATEF--------REAHPWLLPF---LPLAGLLIGYLYQKfgKNSEKGNNLIIEEIHGPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 99 E---LSMNWFSvlwkkFIGGVLSVGAGLFLGREGPSIQLGASIGQGAGQLFRSPSSEEKILISSGASSGLAAAFNAPIAG 175
Cdd:cd03682 71 EgipLRMAPLV-----LFGTVLTHLFGGSAGREGTAVQMGGSLADAFGRVFKLPEEDRRILLIAGIAAGFAAVFGTPLAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 176 LLFVLEEI---HHSFSPLvwLTSFASAITANFVSLYFFGLRPVLYLGDLPSLPLKYYGSLVILGVLLGILGFIYQKVLLA 252
Cdd:cd03682 146 AIFALEVLvlgRLRYSAL--IPCLVAAIVADWVSHALGLEHTHYHIVFIPTLDPLLFVKVILAGIIFGLAGRLFAELLHF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 253 LQKFYNRLPLPAYFHGFVPFLLILPIGYLWPST--LG-GGNQIVLAFGHASLPIIMiiglFVLRFVFSMISYGGGLPGGI 329
Cdd:cd03682 224 LKKLLKKRIKNPYLRPFVGGLLIILLVYLLGSRryLGlGTPLIEDSFFGGTVYPYD----WLLKLIFTVITLGAGFKGGE 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1565315252 330 FLPILTLGALIGSFYGNIMvdfgmdPIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVGSLNhLMPLGLAALVAYIVN 408
Cdd:cd03682 300 VTPLFFIGATLGNALAPIL------GLPVSLLAALGFVAVFAGATNTPLACIIMGIELFGAEN-APYFFIACLVAYLFS 371
|
|
| TrkA_C |
pfam02080 |
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of ... |
442-506 |
1.95e-07 |
|
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of this domain is unknown. It has been suggested that it may bind an unidentified ligand. The domain is predicted to adopt an all beta structure.
Pssm-ID: 460440 [Multi-domain] Cd Length: 70 Bit Score: 48.37 E-value: 1.95e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1565315252 442 FPVTAESSLDGLMVRDFNWPK--NMLLISIRRGNQEILTHGDTIMNVGDILVILTDEANLPRIKQEI 506
Cdd:pfam02080 4 VTVPENSPLVGKTLKELNLPErfGVRIVAIRRGGRLIIPSGDTVLEAGDRLLVIGTPDDLAALRELL 70
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
444-504 |
4.25e-05 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 45.88 E-value: 4.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1565315252 444 VTAESSLDGLMVRDFNWPKNMLLISIRRGNQEILTHGDTIMNVGD-ILVILTDEANLPRIKQ 504
Cdd:PRK09496 385 AHETSKVVGKPLKDLKLPKGVLIGAIVRGGEVIIPTGDTVIEPGDhVIVFVLDKKFVPDVEK 446
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
442-506 |
8.52e-05 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 45.11 E-value: 8.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1565315252 442 FPVTAESSLDGLMVRDFN---WPKNMLLISIRRGNQEILTHGDTIMNVGDILVILTDEANLPRIKQEI 506
Cdd:PRK09496 157 VKVYEGSPLVGKPLSDLRehfPDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYFIGAREHIRAVMSEF 224
|
|
| Voltage_gated_ClC |
cd00400 |
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ... |
311-415 |
2.17e-04 |
|
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function.
Pssm-ID: 238233 [Multi-domain] Cd Length: 383 Bit Score: 43.71 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 311 VLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNImvdFGMDPIYIKDFVVIAMAGYFTAIGKAPLTAIILVTEMVG- 389
Cdd:cd00400 86 LVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRR---LRLSRNDRRILVACGAAAGIAAAFNAPLAGALFAIEVLLg 162
|
90 100
....*....|....*....|....*...
gi 1565315252 390 --SLNHLMPLGLAALVAYIVNDLLGGNP 415
Cdd:cd00400 163 eySVASLIPVLLASVAAALVSRLLFGAE 190
|
|
| PRK05326 |
PRK05326 |
potassium/proton antiporter; |
440-508 |
3.78e-04 |
|
potassium/proton antiporter;
Pssm-ID: 235410 [Multi-domain] Cd Length: 562 Bit Score: 43.27 E-value: 3.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1565315252 440 FDFPVTAESSLDGLMVRDFNWPKNMLLISIRRGNQEILTHGDTIMNVGDILVILTDEANLPRIKQEIEA 508
Cdd:PRK05326 417 LEYRVPAGSWLVGKALRDLRLPRGALIALIIRDGKLLVPTGSTRLKAGDVLLVLGPERDLPALERLFSQ 485
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
442-491 |
6.84e-04 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 41.59 E-value: 6.84e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1565315252 442 FPVTAESSLDGLMVRDFNWPK--NMLLISIRRGNQEILTHGDTIMNVGDILV 491
Cdd:COG0569 245 VTVPEGSPLVGKTLKELDLREryGVTVVAIKRGGEVIIPSGDTVLEAGDELI 296
|
|
| Voltage_CLC |
pfam00654 |
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ... |
288-417 |
8.08e-04 |
|
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.
Pssm-ID: 425802 [Multi-domain] Cd Length: 344 Bit Score: 41.76 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1565315252 288 GGNQIVLAFGHASLPIIMI-IGLFVLRFVFSMISYGGGLPGGIFLPILTLGALIGSFYGNIMvdFGMDPIYIKDFVVIAM 366
Cdd:pfam00654 17 AGSGIPEVKAALHGGRGPLpLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL--FRLSPRDRRILLAAGA 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1565315252 367 AGYFTAIGKAPLTAIILVTEMVG---SLNHLMPLGLAALVAYIVNDLLGGNPIY 417
Cdd:pfam00654 95 AAGLAAAFNAPLAGVLFALEELSrsfSLRALIPVLLASVVAALVSRLIFGNSPL 148
|
|
| |
