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Conserved domains on  [gi|1723628119|ref|WP_146751070|]
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chloride channel protein, partial [Enterococcus malodoratus]

Protein Classification

chloride channel protein( domain architecture ID 10087035)

ClC family voltage-gated chloride channel protein catalyzes the selective flow of Cl(-) ions across the cellular membrane

CATH:  1.10.3080.10
Gene Ontology:  GO:0006821|GO:0005247
PubMed:  11182894
SCOP:  4003598

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 13-176 9.13e-24

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: 99.56  E-value: 9.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  13 MESSFTWQGLLLVIPMILLGALFGKLFLVLQDRGEKLNQRIRNPLPL-AIFAGIILGVLGIISPYFLFSGEHNLLSFTRQ 91
Cdd:cd00400   197 LYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFRRLPIPPWLrPALGGLLLGLLGLFLPQVLGSGYGAILLALAG 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  92 AETmnFFILLLIGFGKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLLPY-------SPGLLVAVFTASACAVILKQ 164
Cdd:cd00400   277 ELS--LLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPAlfpglvaSPGAYALVGMAALLAAVLRA 354

                         170
                  ....*....|..
gi 1723628119 165 PFATACLFLLLF 176
Cdd:cd00400   355 PLTAILLVLELT 366
 
Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 13-176 9.13e-24

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: 99.56  E-value: 9.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  13 MESSFTWQGLLLVIPMILLGALFGKLFLVLQDRGEKLNQRIRNPLPL-AIFAGIILGVLGIISPYFLFSGEHNLLSFTRQ 91
Cdd:cd00400   197 LYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFRRLPIPPWLrPALGGLLLGLLGLFLPQVLGSGYGAILLALAG 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  92 AETmnFFILLLIGFGKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLLPY-------SPGLLVAVFTASACAVILKQ 164
Cdd:cd00400   277 ELS--LLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPAlfpglvaSPGAYALVGMAALLAAVLRA 354

                         170
                  ....*....|..
gi 1723628119 165 PFATACLFLLLF 176
Cdd:cd00400   355 PLTAILLVLELT 366
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
15-181 1.75e-18

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 84.80  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  15 SSFTWQGLLLVIPMILLGALFGKLFLVLQDRGEKLNQRIRNPLPL-AIFAGIILGVLGIISPYFLFSGEHNLLSFTrqAE 93
Cdd:COG0038   213 PALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRLKLPPWLrPAIGGLLVGLLGLFLPQVLGSGYGLIEALL--NG 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  94 TMNFFILLLIGFGKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLLPY-------SPGLLVAVFTASACAVILKQPF 166
Cdd:COG0038   291 ELSLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLlfpglglSPGLFALVGMAAVFAAVTRAPL 370

                         170
                  ....*....|....*
gi 1723628119 167 ATaclFLLLFpvELF 181
Cdd:COG0038   371 TA---ILLVL--EMT 380
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 16-174 1.89e-17

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: 81.44  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  16 SFTWQGLLLVIPMILLGALFGKLFLVLQDRGEKL--NQRIRNPLPLAIFAGIILGVLGIISPYFLFSGEHNLLSFTrqAE 93
Cdd:pfam00654 156 SLSLLELPLFILLGILCGLLGALFNRLLLKVQRLfrKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF--NG 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  94 TMNFFILLLIGFGKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLLPY-------SPGLLVAVFTASACAVILKQPF 166
Cdd:pfam00654 234 NTSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALlfpigglPPGAFALVGMAAFLAAVTRAPL 313


                  ....*...
gi 1723628119 167 aTACLFLL 174
Cdd:pfam00654 314 -TAIVIVF 320
PRK03655 PRK03655
putative ion channel protein; Provisional
 45-188 2.15e-08

putative ion channel protein; Provisional


Pssm-ID: 235148  Cd Length: 414  Bit Score: 54.73  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  45 RGEKLNQRIRNPLPLAIFAGIILGVLGIIS-PYFLFSG--EHNLLSFTRQAETMNFFILLLIgfgKLAITMICLACNWRG 121
Cdd:PRK03655  246 RLHALMHRLKNPVLVLGIGGFILGILGVIGgPLTLFKGldEMQQMAANQAFSASDYFLLAVV---KLAALVVAAASGFRG 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119 122 GTIFPMIFSSIAVALAFANLLPYSP----------GLLVAV--------FTAsacAVILKQPfataCLFLLLFPVELFLW 183
Cdd:PRK03655  323 GRIFPAVFVGVALGLMLHAHVPAVPaaitvscailGIVLVVtrdgwlslFMA---AVVVPDT----TLLPLLCIVMLPAW 395


                  ....*
gi 1723628119 184 IWLAG 188
Cdd:PRK03655  396 LLLAG 400
 
Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 13-176 9.13e-24

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: 99.56  E-value: 9.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  13 MESSFTWQGLLLVIPMILLGALFGKLFLVLQDRGEKLNQRIRNPLPL-AIFAGIILGVLGIISPYFLFSGEHNLLSFTRQ 91
Cdd:cd00400   197 LYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFRRLPIPPWLrPALGGLLLGLLGLFLPQVLGSGYGAILLALAG 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  92 AETmnFFILLLIGFGKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLLPY-------SPGLLVAVFTASACAVILKQ 164
Cdd:cd00400   277 ELS--LLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPAlfpglvaSPGAYALVGMAALLAAVLRA 354

                         170
                  ....*....|..
gi 1723628119 165 PFATACLFLLLF 176
Cdd:cd00400   355 PLTAILLVLELT 366
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
15-181 1.75e-18

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 84.80  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  15 SSFTWQGLLLVIPMILLGALFGKLFLVLQDRGEKLNQRIRNPLPL-AIFAGIILGVLGIISPYFLFSGEHNLLSFTrqAE 93
Cdd:COG0038   213 PALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRLKLPPWLrPAIGGLLVGLLGLFLPQVLGSGYGLIEALL--NG 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  94 TMNFFILLLIGFGKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLLPY-------SPGLLVAVFTASACAVILKQPF 166
Cdd:COG0038   291 ELSLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLlfpglglSPGLFALVGMAAVFAAVTRAPL 370

                         170
                  ....*....|....*
gi 1723628119 167 ATaclFLLLFpvELF 181
Cdd:COG0038   371 TA---ILLVL--EMT 380
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 16-174 1.89e-17

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: 81.44  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  16 SFTWQGLLLVIPMILLGALFGKLFLVLQDRGEKL--NQRIRNPLPLAIFAGIILGVLGIISPYFLFSGEHNLLSFTrqAE 93
Cdd:pfam00654 156 SLSLLELPLFILLGILCGLLGALFNRLLLKVQRLfrKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF--NG 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  94 TMNFFILLLIGFGKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLLPY-------SPGLLVAVFTASACAVILKQPF 166
Cdd:pfam00654 234 NTSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALlfpigglPPGAFALVGMAAFLAAVTRAPL 313


                  ....*...
gi 1723628119 167 aTACLFLL 174
Cdd:pfam00654 314 -TAIVIVF 320
PRK03655 PRK03655
putative ion channel protein; Provisional
 45-188 2.15e-08

putative ion channel protein; Provisional


Pssm-ID: 235148  Cd Length: 414  Bit Score: 54.73  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  45 RGEKLNQRIRNPLPLAIFAGIILGVLGIIS-PYFLFSG--EHNLLSFTRQAETMNFFILLLIgfgKLAITMICLACNWRG 121
Cdd:PRK03655  246 RLHALMHRLKNPVLVLGIGGFILGILGVIGgPLTLFKGldEMQQMAANQAFSASDYFLLAVV---KLAALVVAAASGFRG 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119 122 GTIFPMIFSSIAVALAFANLLPYSP----------GLLVAV--------FTAsacAVILKQPfataCLFLLLFPVELFLW 183
Cdd:PRK03655  323 GRIFPAVFVGVALGLMLHAHVPAVPaaitvscailGIVLVVtrdgwlslFMA---AVVVPDT----TLLPLLCIVMLPAW 395


                  ....*
gi 1723628119 184 IWLAG 188
Cdd:PRK03655  396 LLLAG 400
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 22-142 1.85e-06

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: 48.69  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  22 LLLVIPMILLGALFGKLFLVLQDRGEKLNqrIRNPLPLAIFAGIILGVLGIISPYFLFSGEHNLLSFTrqaeTMNFFILL 101
Cdd:cd01031   211 LLLGIIAGLLGYLFNRSLLKSQDLYRKLK--KLPRELRVLLPGLLIGPLGLLLPEALGGGHGLILSLA----GGNFSISL 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1723628119 102 LIGF--GKLAITMICLACNWRGGTIFPMIFSSIAVALAFANLL 142
Cdd:cd01031   285 LLLIfvLRFIFTMLSYGSGAPGGIFAPMLALGALLGLLFGTIL 327
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
19-153 3.62e-04

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 41.80  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  19 WQGLLLVIPMILLGALFGKLFLVLQDRGEKLNQ-RIRNPLPLAIFAGIILGVLGIISPYFLFSGEHnlLSFTRQAETMNF 97
Cdd:PRK05277  218 WLFLLLGIIFGIFGVLFNKLLLRTQDLFDRLHGgNKKRWVLMGGAVGGLCGLLGLLAPAAVGGGFN--LIPIALAGNFSI 295

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1723628119  98 FILLLIGFGKLAITMICLACNWRGGTIFPMifssiavaLAFANLLPYSPGLLVAVF 153
Cdd:PRK05277  296 GMLLFIFVARFITTLLCFGSGAPGGIFAPM--------LALGTLLGLAFGMVAAAL 343
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 13-176 1.44e-03

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: 39.87  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  13 MESSFTWQgLLLVIPMILLGALFG---KLFLVLQDRGEKL-NQRIRNPLPLAIFAGIILGVLGIISPYFLFSG----EHN 84
Cdd:cd03682   189 IVFIPTLD-PLLFVKVILAGIIFGlagRLFAELLHFLKKLlKKRIKNPYLRPFVGGLLIILLVYLLGSRRYLGlgtpLIE 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  85 LLSFTRQAETMNFFillligfGKLAITMICLACNWRGGTIFPMIF--SSIAVALAFanLLPYSPGLL-----VAVFTAS- 156
Cdd:cd03682   268 DSFFGGTVYPYDWL-------LKLIFTVITLGAGFKGGEVTPLFFigATLGNALAP--ILGLPVSLLaalgfVAVFAGAt 338

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1723628119 157 ----ACAVI--------LKQPFATACLFLLLF 176
Cdd:cd03682   339 ntplACIIMgielfgaeNAPYFFIACLVAYLF 370
YfdV COG0679
Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];
53-190 1.66e-03

Predicted permease, AEC (auxin efflux carrier) family [General function prediction only];


Pssm-ID: 440443  Cd Length: 308  Bit Score: 39.40  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  53 IRNPLPLAIFAGIILGVLGIISPYFLFSGEHNLlsftrqAETMNFFILLLIGFGkLAITMIclacnwrGGTIFPMIFSSI 132
Cdd:COG0679   165 LRNPLIIAILLGLLLNLLGIPLPAPLDDTLDLL------GGAAIPLALLALGAS-LALSRL-------KGDLKLVLLASL 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1723628119 133 -------AVALAFANLLPYSPGLLVAVF------TASACAVI-----LKQPFATACLFL--LLFPVELFLWIWLAGYL 190
Cdd:COG0679   231 lkllllpLLALLLALLLGLDGLLLQVLVllaampTAVNAYVLaerygGDPELAASAVLLstLLSLVTLPLWLALLGLL 308
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 19-156 3.11e-03

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: 38.75  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1723628119  19 WQGLLLVIPMILLGALFGKLF---LVLQDRG---EKLNQRIRNPLPLAIFAGIILGVLGiispyfLFSGEHNLLSFTRQA 92
Cdd:cd01034   199 GEAWLLVLVCGVVGGLAGGLFarlLVALSSGlpgWVRRFRRRRPVLFAALCGLALALIG------LVSGGLTFGTGYLQA 272

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1723628119  93 ETMNF---FILLLIGFGKLAITMICLACNWRGGTIFPmifsSIAVALAFANLL-----PYSPGLLVAVFTAS 156
Cdd:cd01034   273 RAALEgggGLPLWFGLLKFLATLLSYWSGIPGGLFAP----SLAVGAGLGSLLaallgSVSQGALVLLGMAA 340
 
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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