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Conserved domains on  [gi|90111303|ref|NP_416109|]
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putative chloride:H(+) antiporter ClcB [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

voltage-gated ClC-type chloride channel ClcB( domain architecture ID 10792174)

voltage-gated ClC-type chloride channel ClcB acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
1-418 0e+00

putative voltage-gated ClC-type chloride channel ClcB; Provisional


:

Pssm-ID: 234963  Cd Length: 418  Bit Score: 681.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303    1 MFHRLLIATVVGILAAFAVAGFRHAMLLLEWLFLNNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTQQRPH 80
Cdd:PRK01610   1 MFRRLLIATVVGILAALAVAGFRHAMLLLEWLFLSNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLWGWQKFTQQRPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   81 APTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMAAAY 160
Cdd:PRK01610  81 APTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMASAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  161 RAPLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALLYNVQLSVTVQARDYALIISTGVLAGLCGPLLLT 240
Cdd:PRK01610 161 HAPLAGSLFIAEILFGTLMLASLGPVVISAVVALLTTNLLNGSDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLLLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  241 LMNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGG 320
Cdd:PRK01610 241 LMNASHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSVVQSFLTAPPLLMLIAGIFLCKLLAVLASSGSGAPGG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  321 VFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVI 400
Cdd:PRK01610 321 VFTPTLFVGLAIGMLYGRSLGLWLPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVI 400
                        410
                 ....*....|....*...
gi 90111303  401 SRTLHRDSIYRQHTAQHS 418
Cdd:PRK01610 401 SRTLRRDSIYRQHTAEHS 418
 
Name Accession Description Interval E-value
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
1-418 0e+00

putative voltage-gated ClC-type chloride channel ClcB; Provisional


Pssm-ID: 234963  Cd Length: 418  Bit Score: 681.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303    1 MFHRLLIATVVGILAAFAVAGFRHAMLLLEWLFLNNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTQQRPH 80
Cdd:PRK01610   1 MFRRLLIATVVGILAALAVAGFRHAMLLLEWLFLSNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLWGWQKFTQQRPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   81 APTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMAAAY 160
Cdd:PRK01610  81 APTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMASAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  161 RAPLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALLYNVQLSVTVQARDYALIISTGVLAGLCGPLLLT 240
Cdd:PRK01610 161 HAPLAGSLFIAEILFGTLMLASLGPVVISAVVALLTTNLLNGSDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLLLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  241 LMNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGG 320
Cdd:PRK01610 241 LMNASHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSVVQSFLTAPPLLMLIAGIFLCKLLAVLASSGSGAPGG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  321 VFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVI 400
Cdd:PRK01610 321 VFTPTLFVGLAIGMLYGRSLGLWLPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVI 400
                        410
                 ....*....|....*...
gi 90111303  401 SRTLHRDSIYRQHTAQHS 418
Cdd:PRK01610 401 SRTLRRDSIYRQHTAEHS 418
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
5-411 1.32e-81

H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 256.60  E-value: 1.32e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   5 LLIATVVGILAAFAVAGFRHAMLLLEWLFLNndsGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTqqRPHAPTD 84
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHLFLG---GLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEA--RGSGIPQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  85 YMEALQT-DGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF-TPRQEWKLWIACGAAAGMAAAYRA 162
Cdd:COG0038  83 VIEAIHLkGGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLrLSPEDRRILLAAGAAAGLAAAFNA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 163 PLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALlYNVQLSVTVQARDYALIISTGVLAGLCGPLLLTLM 242
Cdd:COG0038 163 PLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLLFGNGPL-FGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 243 NACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGGVF 322
Cdd:COG0038 242 LKVERLFKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGELSLLLLLLLLLLKLLATALTLGSGGPGGIF 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 323 TPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISR 402
Cdd:COG0038 322 APSLFIGALLGAAFGLLLNLLFPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLMIACVIAYLVSR 401

                ....*....
gi 90111303 403 TLHRDSIYR 411
Cdd:COG0038 402 LLFPRSIYT 410
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
12-398 9.58e-76

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: 240.54  E-value: 9.58e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  12 GILAAFAVAGFRHAMLLLEWLFLNNDSGSLvnAATNLSPWRRLLTPALGGLAAGLLLMgwqKFTQQRPHAPTDYMEAL-Q 90
Cdd:cd00400   1 GVLSGLGAVLFRLLIELLQNLLFGGLPGEL--AAGSLSPLYILLVPVIGGLLVGLLVR---LLGPARGHGIPEVIEAIaL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  91 TDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF-TPRQEWKLWIACGAAAGMAAAYRAPLAGSLF 169
Cdd:cd00400  76 GGGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLrLSRNDRRILVACGAAAGIAAAFNAPLAGALF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 170 IAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALlYNVQLSVTVQARDYALIISTGVLAGLCGPLLLTLMNACHRGF 249
Cdd:cd00400 156 AIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEPA-FGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 250 VSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGGVFTPTLFIG 329
Cdd:cd00400 235 RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLALAGELSLLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIG 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111303 330 LAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIAS 398
Cdd:cd00400 315 AALGAAFGLLLPALFPGLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLMLAVVIAY 383
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
83-402 2.26e-64

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: 209.71  E-value: 2.26e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303    83 TDYMEALQ-TDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF--TPRQEWKLWIACGAAAGMAAA 159
Cdd:pfam00654  22 PEVKAALHgGRGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLfrLSPRDRRILLAAGAAAGLAAA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   160 YRAPLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALlYNVQLSVTVQARDYALIISTGVLAGLCGPLLL 239
Cdd:pfam00654 102 FNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGNSPL-FSVGEPGSLSLLELPLFILLGILCGLLGALFN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   240 TLMNACHRGFVS-LKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAP 318
Cdd:pfam00654 181 RLLLKVQRLFRKlLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFNGNTSLSLLLLLLLLKFLATALSLGSGAP 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   319 GGVFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIAS 398
Cdd:pfam00654 261 GGIFAPSLAIGAALGRAFGLLLALLFPIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAY 340

                  ....
gi 90111303   399 VISR 402
Cdd:pfam00654 341 AVSR 344
 
Name Accession Description Interval E-value
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
1-418 0e+00

putative voltage-gated ClC-type chloride channel ClcB; Provisional


Pssm-ID: 234963  Cd Length: 418  Bit Score: 681.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303    1 MFHRLLIATVVGILAAFAVAGFRHAMLLLEWLFLNNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTQQRPH 80
Cdd:PRK01610   1 MFRRLLIATVVGILAALAVAGFRHAMLLLEWLFLSNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLWGWQKFTQQRPH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   81 APTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMAAAY 160
Cdd:PRK01610  81 APTDYMEALQTDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMASAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  161 RAPLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALLYNVQLSVTVQARDYALIISTGVLAGLCGPLLLT 240
Cdd:PRK01610 161 HAPLAGSLFIAEILFGTLMLASLGPVVISAVVALLTTNLLNGSDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLLLT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  241 LMNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGG 320
Cdd:PRK01610 241 LMNASHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSVVQSFLTAPPLLMLIAGIFLCKLLAVLASSGSGAPGG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  321 VFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVI 400
Cdd:PRK01610 321 VFTPTLFVGLAIGMLYGRSLGLWLPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVI 400
                        410
                 ....*....|....*...
gi 90111303  401 SRTLHRDSIYRQHTAQHS 418
Cdd:PRK01610 401 SRTLRRDSIYRQHTAEHS 418
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
5-410 1.21e-81

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 261.60  E-value: 1.21e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303    5 LLIATVVGILAAFAVAGFRHAMLLLEwLFLNNDSGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTQQRPHapTD 84
Cdd:PRK01862  25 LIWSAIVGIGGAFATTAFREGIELIQ-HLISGHSGSFVEMAKSLPWYVRVWLPAAGGFLAGCVLLLANRGARKGGK--TD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   85 YMEALQT-DGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQ--RFTPRQeWKLWIACGAAAGMAAAYR 161
Cdd:PRK01862 102 YMEAVALgDGVVPVRQSLWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRfaHFDPPR-LRLLVACGAAAGITSAYN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  162 APLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNliNHSDAL-LYNVQLSVTVQARDYALIISTGVLAGLCGPLLLT 240
Cdd:PRK01862 181 APIAGAFFVAEIVLGSIAMESFGPLVVASVVANIVMR--EFAGYQpPYEMPVFPAVTGWEVLLFVALGVLCGAAAPQFLR 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  241 LMNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGG 320
Cdd:PRK01862 259 LLDASKNQFKRLPVPLPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILHAPWTWQALVAVLVAKLIATAATAGSGAVGG 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  321 VFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVI 400
Cdd:PRK01862 339 VFTPTLFVGAVVGSLFGLAMHALWPGHTSAPFAYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFT 418
                        410
                 ....*....|
gi 90111303  401 SRTLHRDSIY 410
Cdd:PRK01862 419 ARALGTTSMY 428
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
5-411 1.32e-81

H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 256.60  E-value: 1.32e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   5 LLIATVVGILAAFAVAGFRHAMLLLEWLFLNndsGSLVNAATNLSPWRRLLTPALGGLAAGLLLMGWQKFTqqRPHAPTD 84
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHLFLG---GLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEA--RGSGIPQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  85 YMEALQT-DGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF-TPRQEWKLWIACGAAAGMAAAYRA 162
Cdd:COG0038  83 VIEAIHLkGGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLrLSPEDRRILLAAGAAAGLAAAFNA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 163 PLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALlYNVQLSVTVQARDYALIISTGVLAGLCGPLLLTLM 242
Cdd:COG0038 163 PLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLLFGNGPL-FGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 243 NACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGGVF 322
Cdd:COG0038 242 LKVERLFKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGELSLLLLLLLLLLKLLATALTLGSGGPGGIF 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 323 TPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISR 402
Cdd:COG0038 322 APSLFIGALLGAAFGLLLNLLFPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLMIACVIAYLVSR 401

                ....*....
gi 90111303 403 TLHRDSIYR 411
Cdd:COG0038 402 LLFPRSIYT 410
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
12-398 9.58e-76

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: 240.54  E-value: 9.58e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  12 GILAAFAVAGFRHAMLLLEWLFLNNDSGSLvnAATNLSPWRRLLTPALGGLAAGLLLMgwqKFTQQRPHAPTDYMEAL-Q 90
Cdd:cd00400   1 GVLSGLGAVLFRLLIELLQNLLFGGLPGEL--AAGSLSPLYILLVPVIGGLLVGLLVR---LLGPARGHGIPEVIEAIaL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  91 TDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF-TPRQEWKLWIACGAAAGMAAAYRAPLAGSLF 169
Cdd:cd00400  76 GGGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLrLSRNDRRILVACGAAAGIAAAFNAPLAGALF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 170 IAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALlYNVQLSVTVQARDYALIISTGVLAGLCGPLLLTLMNACHRGF 249
Cdd:cd00400 156 AIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEPA-FGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 250 VSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGGVFTPTLFIG 329
Cdd:cd00400 235 RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLALAGELSLLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIG 314
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90111303 330 LAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIAS 398
Cdd:cd00400 315 AALGAAFGLLLPALFPGLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLMLAVVIAY 383
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
83-402 2.26e-64

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: 209.71  E-value: 2.26e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303    83 TDYMEALQ-TDGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF--TPRQEWKLWIACGAAAGMAAA 159
Cdd:pfam00654  22 PEVKAALHgGRGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLfrLSPRDRRILLAAGAAAGLAAA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   160 YRAPLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALlYNVQLSVTVQARDYALIISTGVLAGLCGPLLL 239
Cdd:pfam00654 102 FNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGNSPL-FSVGEPGSLSLLELPLFILLGILCGLLGALFN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   240 TLMNACHRGFVS-LKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAP 318
Cdd:pfam00654 181 RLLLKVQRLFRKlLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFNGNTSLSLLLLLLLLKFLATALSLGSGAP 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303   319 GGVFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIAS 398
Cdd:pfam00654 261 GGIFAPSLAIGAALGRAFGLLLALLFPIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAY 340

                  ....
gi 90111303   399 VISR 402
Cdd:pfam00654 341 AVSR 344
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
101-410 8.95e-38

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: 141.14  E-value: 8.95e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF-TPRQEWKLWIACGAAAGMAAAYRAPLAGSLFIAEVLFGTMM 179
Cdd:cd01031  87 PVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSKWFkTSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFS 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 180 LASLGPVIISAVVALLVSNLINHSDALLYnVQLSVTVQARDYALIISTGVLAGLCGPL----LLTLMNACHRGfvsLKLA 255
Cdd:cd01031 167 PLALLTALVASIAADFVSRLFFGLGPVLS-IPPLPALPLKSYWLLLLLGIIAGLLGYLfnrsLLKSQDLYRKL---KKLP 242
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 256 PPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGGVFTPTLFIGLAIGML 335
Cdd:cd01031 243 RELRVLLPGLLIGPLGLLLPEALGGGHGLILSLAGGNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLGLL 322
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90111303 336 YGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLHRDSIY 410
Cdd:cd01031 323 FGTILVQLGPIPISAPATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMVVCLVAYLVADLLGGKPIY 397
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
12-402 7.54e-30

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: 118.94  E-value: 7.54e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  12 GILAAFAVAGFRHAMLLLEWLFLNNDSGSLVNAATNLSPWRRLLTPALGGLAAGlllMGWQkFTQQRPHAPTDYMEALQT 91
Cdd:cd01033   1 GVGAGLGGGLLTLLLHGVQHLAFGYSEGSFLTGVAAVSPIRRALSLTVGGLIAG---LGWY-LLRRKGKKLVSIKQAVRG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  92 DGQFDYAASLVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF--TPRQEwKLWIACGAAAGMAAAYRAPLAGSLF 169
Cdd:cd01033  77 KKRMPFWETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWLglTVADR-RLLVACAAGAGLAAVYNVPLAGALF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 170 IAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALLYNVQLSVTVQardyaliisTGVLAGLCGPLLLTLMNACHRGF 249
Cdd:cd01033 156 ALEILLRTISLRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTP---------LLIWALLAGPVLGVVAAGFRRLS 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 250 VSLKLAPP------WQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSGAPGGVFT 323
Cdd:cd01033 227 QAARAKRPkgkrilWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSLLLILLVLKIVATLLALRAGAYGGLLT 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 324 PTLFIGLAIGMLYGRSLGLWFPdGEEITLLLgLTGMATLLAATTHAPIMSTLMICEMTG-EYQLLPGLLIACVIASVISR 402
Cdd:cd01033 307 PSLALGALLGALLGIVWNALLP-PLSIAAFA-LIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGAVAVSR 384
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
163-412 6.10e-27

H(+)/Cl(-) exchange transporter ClcA;


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 111.52  E-value: 6.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  163 PLAGSLFIAEVLFGTMM--LASLGPVIISAVVALLVSNLINHSDALLYNVQLSVtVQARDYALIISTGVLAGLCGP---- 236
Cdd:PRK05277 158 PLAGILFVIEEMRPQFRysLISIKAVFIGVIMATIVFRLFNGEQAVIEVGKFSA-PPLNTLWLFLLLGIIFGIFGVlfnk 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  237 LLLTLMNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIIAGIFLCKLCAVLASSGSG 316
Cdd:PRK05277 237 LLLRTQDLFDRLHGGNKKRWVLMGGAVGGLCGLLGLLAPAAVGGGFNLIPIALAGNFSIGMLLFIFVARFITTLLCFGSG 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303  317 APGGVFTPTLFIGLAIGMLYGRSLGLWFPDGEEITLLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVI 396
Cdd:PRK05277 317 APGGIFAPMLALGTLLGLAFGMVAAALFPQYHIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCLG 396
                        250
                 ....*....|....*.
gi 90111303  397 ASVISRTLHRDSIYRQ 412
Cdd:PRK05277 397 ATLLAQFLGGKPIYSA 412
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
163-411 6.16e-21

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: 93.83  E-value: 6.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 163 PLAGSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLINHSDALLYNVQLSVTVQArDYALIISTGVLAGLCGPLLLTLM 242
Cdd:cd01034 145 PLAGIVFAIEELSRDFELRFSGLVLLAVIAAGLVSLAVLGNYPYFGVAAVALPLGE-AWLLVLVCGVVGGLAGGLFARLL 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 243 NACHRGFVSLKLAP----PWQLALG-GLIVGLLSLFTP-AVWGNGYSTVQSFLTAPPLLmiIAGIFLCKLCAVLASSGSG 316
Cdd:cd01034 224 VALSSGLPGWVRRFrrrrPVLFAALcGLALALIGLVSGgLTFGTGYLQARAALEGGGGL--PLWFGLLKFLATLLSYWSG 301
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 317 APGGVFTPTLfiglAIGMLYGRSLGLWFPDGEEITLLLglTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVI 396
Cdd:cd01034 302 IPGGLFAPSL----AVGAGLGSLLAALLGSVSQGALVL--LGMAAFLAGVTQAPLTAFVIVMEMTGDQQMLLPLLAAALL 375
                       250
                ....*....|....*
gi 90111303 397 ASVISRTLHRDSIYR 411
Cdd:cd01034 376 ASGVSRLVCPEPLYH 390
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
163-411 1.19e-12

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: 68.76  E-value: 1.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 163 PLAGSLFIAEVLF-GTMMLASLGPVIISAVVALLVSNLINHsDALLYNVQLSVTVQARDYALIISTGVLAGLCGPLLLTL 241
Cdd:cd03682 142 PLAGAIFALEVLVlGRLRYSALIPCLVAAIVADWVSHALGL-EHTHYHIVFIPTLDPLLFVKVILAGIIFGLAGRLFAEL 220
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 242 MNACHRGFVSLKLAPPWQLALGGLIVGLLSLFTPAVWGNGYST---VQSFLTAPpllmIIAGIFLCKLCAVLASSGSGAP 318
Cdd:cd03682 221 LHFLKKLLKKRIKNPYLRPFVGGLLIILLVYLLGSRRYLGLGTpliEDSFFGGT----VYPYDWLLKLIFTVITLGAGFK 296
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 319 GGVFTPTLFIGLAIGMLYGRSLGLwfpdgeEITLLLGLtGMATLLAATTHAPIMSTLMICEMTGeYQLLPGLLIACVIAS 398
Cdd:cd03682 297 GGEVTPLFFIGATLGNALAPILGL------PVSLLAAL-GFVAVFAGATNTPLACIIMGIELFG-AENAPYFFIACLVAY 368
                       250
                ....*....|...
gi 90111303 399 VISrtlHRDSIYR 411
Cdd:cd03682 369 LFS---GHTGIYG 378
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
318-410 2.26e-08

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: 55.72  E-value: 2.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 318 PGGVFTPTLFIGLAIGMLYGRSLGLWFPDGEEITL-------LLGLTGMATLLAATTHApIMSTLMICEMTGEYQLLPGL 390
Cdd:cd03683 315 PAGIFMPVFVIGAALGRLVGEIMAVLFPEGIRGGIsnpigpgGYAVVGAAAFSGAVTHT-VSVAVIIFELTGQISHLLPV 393
                        90       100
                ....*....|....*....|
gi 90111303 391 LIACVIASVISRTLHRdSIY 410
Cdd:cd03683 394 LIAVLISNAVAQFLQP-SIY 412
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
101-397 1.99e-05

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: 46.57  E-value: 1.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFT---------------PRQEWKLwIACGAAAGMAAAYRAPLA 165
Cdd:cd01036  89 IAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSrtlgchvhlfqlfrnPRDRRDF-LVAGAAAGVASAFGAPIG 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 166 GSLFIAEVLFGTMMLASLGPVIISAVVALLVSNLIN---------HSDALLYNVQLSVTVQARDYALIISTGVLAGLCGP 236
Cdd:cd01036 168 GLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNsfnsgfellDRSSAMFLSLTVFELHVPLNLYEFIPTVVIGVICG 247
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 237 LLLTLMNACHRGFVSlklappWQLALGGLIVGLLSLFTPAVWGNGYSTVQSFLTAPPLLMIiagiflcKLCAVLASSGSG 316
Cdd:cd01036 248 LLAALFVRLSIIFLR------WRRRLLFRKTARYRVLEPVLFTLIYSTIHYAPTLLLFLLI-------YFWMSALAFGIA 314
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111303 317 APGGVFTPTLFIGLAIGMLYGRSLGLWFPDG---EEITL-----LLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLP 388
Cdd:cd01036 315 VPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGigaESATLwadpgVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLL 394

                ....*....
gi 90111303 389 GLLIACVIA 397
Cdd:cd01036 395 PLMVAILIA 403
 
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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