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Conserved domains on  [gi|1907170599|ref|XP_036021690|]
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chloride channel protein 1 isoform X2 [Mus musculus]

Protein Classification

chloride channel protein( domain architecture ID 66845)

ClC family voltage-gated chloride channel protein containing a C-terminal CBS pair domain, 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 super family cl02915
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 1-254 9.95e-109

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.


The actual alignment was detected with superfamily member cd03683:

Pssm-ID: 445960 [Multi-domain]  Cd Length: 426  Bit Score: 334.99  E-value: 9.95e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   1 MDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKCLSQFLAKHRLLYPGIVTFVIASLTFPpgmgqfmagel 80
Cdd:cd03683   223 VDFPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTFP----------- 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  81 mpreaistlfdnntwvkhigdpqslgqsavwlhpqvnvIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLV 160
Cdd:cd03683   292 --------------------------------------FLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLV 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 161 GEIMAMLFPEGIlFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLY 240
Cdd:cd03683   334 GEIMAVLFPEGI-RGGISNPIGPGGYAVVGAAAFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIY 412

                         250
                  ....*....|....
gi 1907170599 241 DSIIQVKKLPYLPD 254
Cdd:cd03683   413 DSIIKIKKLPYLPD 426
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 267-537 3.00e-17

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


The actual alignment was detected with superfamily member cd04591:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 114  Bit Score: 77.94  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 267 VEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDSMILLGSVERSELQSLLQRhlcaerrlkaaqdmarklsel 346
Cdd:cd04591     2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA--------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 347 pyngkaqlagdwhpggrpesfafvdededeDLSrkmelpltpappppspppppsqfpiapsnpeepngplpshkqppeas 426
Cdd:cd04591    61 ------------------------------DLR----------------------------------------------- 63

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 427 dsadqrsstfqrllhcllgkahskkkkitqdstdlvdnmspeeieawereqlsqpvcfdcCCIDQSPFQLVEQTTLHKTH 506
Cdd:cd04591    64 ------------------------------------------------------------PIMDPSPFTVTEETSLEKVH 83

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907170599 507 TLFSLLGLHLAYVTSMGKLRGVLALEELQKA 537
Cdd:cd04591    84 DLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
 
Name Accession Description Interval E-value
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 1-254 9.95e-109

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: 334.99  E-value: 9.95e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   1 MDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKCLSQFLAKHRLLYPGIVTFVIASLTFPpgmgqfmagel 80
Cdd:cd03683   223 VDFPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTFP----------- 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  81 mpreaistlfdnntwvkhigdpqslgqsavwlhpqvnvIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLV 160
Cdd:cd03683   292 --------------------------------------FLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLV 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 161 GEIMAMLFPEGIlFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLY 240
Cdd:cd03683   334 GEIMAVLFPEGI-RGGISNPIGPGGYAVVGAAAFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIY 412

                         250
                  ....*....|....
gi 1907170599 241 DSIIQVKKLPYLPD 254
Cdd:cd03683   413 DSIIKIKKLPYLPD 426
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 2-233 4.88e-43

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: 158.09  E-value: 4.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   2 DFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMlgvrkhKCLSQFLAKHRLLYPGIVTFVIASLT--FPPGMGQFMage 79
Cdd:pfam00654 154 PGSLSLLELPLFILLGILCGLLGALFNRLLLKVQ------RLFRKLLKIPPVLRPALGGLLVGLLGllFPEVLGGGY--- 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  80 lmprEAISTLFDNNTwvkhigdpqslgqsavwlhpqvnVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRL 159
Cdd:pfam00654 225 ----ELIQLLFNGNT-----------------------SLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907170599 160 VGEIMAMLFPEGIlfddiiykILPGGYAVIGAAALTGAVSH-TVSTAVICFELTGQIAHILPMMVAVILANMVAQ 233
Cdd:pfam00654 278 FGLLLALLFPIGG--------LPPGAFALVGMAAFLAAVTRaPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVSR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
4-242 1.84e-27

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 115.24  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   4 PFDLKELPAFAVIGICCGFLGAVFVYLhrqvMLGVRKhkcLSQFLAKHRLLYPGIVTFVIA--SLTFPPGMGqfmAGElm 81
Cdd:COG0038   214 ALSLLELPLYLLLGILAGLVGVLFNRL----LLKVER---LFKRLKLPPWLRPAIGGLLVGllGLFLPQVLG---SGY-- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  82 prEAISTLFDNNTwvkhigdpqslgqsavwlhpqvnVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVG 161
Cdd:COG0038   282 --GLIEALLNGEL-----------------------SLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFG 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 162 EIMAMLFPEGIlfddiiykILPGGYAVIGAAALTGAVSHT-VSTAVICFELTGQIAHILPMMVAVILANMVAQSLQP-SL 239
Cdd:COG0038   337 LLLNLLFPGLG--------LSPGLFALVGMAAVFAAVTRApLTAILLVLEMTGSYSLLLPLMIACVIAYLVSRLLFPrSI 408


                  ...
gi 1907170599 240 YDS 242
Cdd:COG0038   409 YTA 411
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 267-537 3.00e-17

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 77.94  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 267 VEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDSMILLGSVERSELQSLLQRhlcaerrlkaaqdmarklsel 346
Cdd:cd04591     2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA--------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 347 pyngkaqlagdwhpggrpesfafvdededeDLSrkmelpltpappppspppppsqfpiapsnpeepngplpshkqppeas 426
Cdd:cd04591    61 ------------------------------DLR----------------------------------------------- 63

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 427 dsadqrsstfqrllhcllgkahskkkkitqdstdlvdnmspeeieawereqlsqpvcfdcCCIDQSPFQLVEQTTLHKTH 506
Cdd:cd04591    64 ------------------------------------------------------------PIMDPSPFTVTEETSLEKVH 83

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907170599 507 TLFSLLGLHLAYVTSMGKLRGVLALEELQKA 537
Cdd:cd04591    84 DLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
7-243 3.77e-13

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 71.85  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   7 LKELPAFAVIGICCGFLGAVFvylHRQVMLGVRKHKCLSQFLAKHRLLYPGIV--TFVIASLTFPPGMGQFMagelmprE 84
Cdd:PRK05277  214 LNTLWLFLLLGIIFGIFGVLF---NKLLLRTQDLFDRLHGGNKKRWVLMGGAVggLCGLLGLLAPAAVGGGF-------N 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  85 AISTLFDNNTwvkhigdpqslgqsavwlhpqvnVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIM 164
Cdd:PRK05277  284 LIPIALAGNF-----------------------SIGMLLFIFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVA 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 165 AMLFPEgilfddiiYKILPGGYAVIGAAAL-TGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSL--QPsLYD 241
Cdd:PRK05277  341 AALFPQ--------YHIEPGTFAIAGMGALfAATVRAPLTGIVLVLEMTDNYQLILPLIITCLGATLLAQFLggKP-IYS 411


                  ..
gi 1907170599 242 SI 243
Cdd:PRK05277  412 AL 413
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
264-343 7.44e-04

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.23  E-value: 7.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 264 TIFVEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDsmILLGSVERSELQSLLQRHLCAERRLKAAQDMARKL 343
Cdd:COG3448     1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDG--RLVGIVTERDLLRALLPDRLDELEERLLDLPVEDV 78
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 267-319 3.77e-03

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.04  E-value: 3.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907170599 267 VEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDSmiLLGSVERSEL 319
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGK--LVGIVTLKDL 51
 
Name Accession Description Interval E-value
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 1-254 9.95e-109

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: 334.99  E-value: 9.95e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   1 MDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKCLSQFLAKHRLLYPGIVTFVIASLTFPpgmgqfmagel 80
Cdd:cd03683   223 VDFPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTFP----------- 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  81 mpreaistlfdnntwvkhigdpqslgqsavwlhpqvnvIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLV 160
Cdd:cd03683   292 --------------------------------------FLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLV 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 161 GEIMAMLFPEGIlFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLY 240
Cdd:cd03683   334 GEIMAVLFPEGI-RGGISNPIGPGGYAVVGAAAFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIY 412

                         250
                  ....*....|....
gi 1907170599 241 DSIIQVKKLPYLPD 254
Cdd:cd03683   413 DSIIKIKKLPYLPD 426
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 2-241 2.30e-62

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: 212.97  E-value: 2.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   2 DFPFDLKELPAFAVIGICCGFLGAVFVYLHRqVMLGVRKHkCLSQFLAKHRLLYPGIVTFVIASLTFPPgmgqfmagelm 81
Cdd:cd01036   228 HVPLNLYEFIPTVVIGVICGLLAALFVRLSI-IFLRWRRR-LLFRKTARYRVLEPVLFTLIYSTIHYAP----------- 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  82 preaisTLfdnntwvkhigdpqslgqsavwlhpqvnviiiiLLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVG 161
Cdd:cd01036   295 ------TL---------------------------------LLFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVG 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 162 EIMAMLFPEGILFDDIIYKILPGGYAVIGAAALTGAVS-HTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLY 240
Cdd:cd01036   336 LLVHRIAVAGIGAESATLWADPGVYALIGAAAFLGGTTrLTFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFCESLY 415


                  .
gi 1907170599 241 D 241
Cdd:cd01036   416 H 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 2-233 4.88e-43

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: 158.09  E-value: 4.88e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   2 DFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMlgvrkhKCLSQFLAKHRLLYPGIVTFVIASLT--FPPGMGQFMage 79
Cdd:pfam00654 154 PGSLSLLELPLFILLGILCGLLGALFNRLLLKVQ------RLFRKLLKIPPVLRPALGGLLVGLLGllFPEVLGGGY--- 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  80 lmprEAISTLFDNNTwvkhigdpqslgqsavwlhpqvnVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRL 159
Cdd:pfam00654 225 ----ELIQLLFNGNT-----------------------SLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907170599 160 VGEIMAMLFPEGIlfddiiykILPGGYAVIGAAALTGAVSH-TVSTAVICFELTGQIAHILPMMVAVILANMVAQ 233
Cdd:pfam00654 278 FGLLLALLFPIGG--------LPPGAFALVGMAAFLAAVTRaPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVSR 344
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 2-252 2.46e-35

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: 138.89  E-value: 2.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   2 DFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKclsqfLAKHRLLYPGIVTFVIASLTFP-PGMGQFMAgel 80
Cdd:cd03684   199 DRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSL-----LKRYPVLEVLLVALITALISFPnPYTRLDMT--- 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  81 mprEAISTLF-----DNNTWVKHIGDPQSlgqsavwlHPQVNVIIIILLF-FVMKFWMSIVATTMPIPCGGFMPVFVLGA 154
Cdd:cd03684   271 ---ELLELLFnecepGDDNSLCCYRDPPA--------GDGVYKALWSLLLaLIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 155 AFGRLVGEIMAML---FPEGILF-------DDIIykilPGGYAVIGAAALTGAVSH-TVSTAVICFELTGQIAHILPMMV 223
Cdd:cd03684   340 LFGRIVGILVEQLaysYPDSIFFacctagpSCIT----PGLYAMVGAAAFLGGVTRmTVSLVVIMFELTGALNYILPLMI 415

                         250       260       270
                  ....*....|....*....|....*....|
gi 1907170599 224 AVILANMVAQSLQP-SLYDSIIQVKKLPYL 252
Cdd:cd03684   416 AVMVSKWVADAIGKeGIYDAHIHLNGYPFL 445
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 1-229 1.08e-30

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: 124.21  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   1 MDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKhkclsqfLAKHRLLYPGIVTFVIASLT--FPPGMGqfmAG 78
Cdd:cd00400   197 LYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFRR-------LPIPPWLRPALGGLLLGLLGlfLPQVLG---SG 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  79 ElmprEAISTLFDNNTwvkhigdpqslgqsavwlhpqvnVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGR 158
Cdd:cd00400   267 Y----GAILLALAGEL-----------------------SLLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGA 319

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907170599 159 LVGEIMAMLFPEGIlfddiiykILPGGYAVIGAAALTGAVSHT-VSTAVICFELTGQIAHILPMMVAVILAN 229
Cdd:cd00400   320 AFGLLLPALFPGLV--------ASPGAYALVGMAALLAAVLRApLTAILLVLELTGDYSLLLPLMLAVVIAY 383
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
4-242 1.84e-27

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 115.24  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   4 PFDLKELPAFAVIGICCGFLGAVFVYLhrqvMLGVRKhkcLSQFLAKHRLLYPGIVTFVIA--SLTFPPGMGqfmAGElm 81
Cdd:COG0038   214 ALSLLELPLYLLLGILAGLVGVLFNRL----LLKVER---LFKRLKLPPWLRPAIGGLLVGllGLFLPQVLG---SGY-- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  82 prEAISTLFDNNTwvkhigdpqslgqsavwlhpqvnVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVG 161
Cdd:COG0038   282 --GLIEALLNGEL-----------------------SLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFG 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 162 EIMAMLFPEGIlfddiiykILPGGYAVIGAAALTGAVSHT-VSTAVICFELTGQIAHILPMMVAVILANMVAQSLQP-SL 239
Cdd:COG0038   337 LLLNLLFPGLG--------LSPGLFALVGMAAVFAAVTRApLTAILLVLEMTGSYSLLLPLMIACVIAYLVSRLLFPrSI 408


                  ...
gi 1907170599 240 YDS 242
Cdd:COG0038   409 YTA 411
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 5-252 1.30e-26

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: 113.52  E-value: 1.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   5 FDLKELPAFAVIGICCGFLGAVFVYLHRQV----MLGVRKHKCLSQFLAkhrllypgivtFVIASLTfppGMGQFMagel 80
Cdd:cd03685   272 YTYFELIPFMLIGVIGGLLGALFNHLNHKVtrfrKRINHKGKLLKVLEA-----------LLVSLVT---SVVAFP---- 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  81 mpreaiSTLFdnntwvkhigdpqslgqsavwlhpqvnviiiilLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLV 160
Cdd:cd03685   334 ------QTLL---------------------------------IFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 161 GEIMAMLFPEGilfddiiyKILPGGYAVIGAAALTGAVSH-TVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSL 239
Cdd:cd03685   375 GILLGSYFGFT--------SIDPGLYALLGAAAFLGGVMRmTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGI 446

                         250
                  ....*....|...
gi 1907170599 240 YDSIIQVKKLPYL 252
Cdd:cd03685   447 YDIIIQLKGVPFL 459
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 4-245 2.28e-26

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: 111.86  E-value: 2.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   4 PFDLKELPAFAVIGICCGFLGAVFvylhrQVMLgVRKHKCLSQFLAKHRLLYPGIVTFVIA--SLTFPPGMGQfmaGELM 81
Cdd:cd01031   201 ALPLKSYWLLLLLGIIAGLLGYLF-----NRSL-LKSQDLYRKLKKLPRELRVLLPGLLIGplGLLLPEALGG---GHGL 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  82 preaISTLFDNNTWvkhigdpqslgqsavwlhpqvnvIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVG 161
Cdd:cd01031   272 ----ILSLAGGNFS-----------------------ISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLGLLFG 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 162 EIMAMLFPEGIlfddiiykILPGGYAVIGAAALTGAVSHTVSTAVI-CFELTGQIAHILPMMVAVILANMVAQSLQ-PSL 239
Cdd:cd01031   325 TILVQLGPIPI--------SAPATFAIAGMAAFFAAVVRAPITAIIlVTEMTGNFNLLLPLMVVCLVAYLVADLLGgKPI 396


                  ....*.
gi 1907170599 240 YDSIIQ 245
Cdd:cd01031   397 YEALLE 402
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 267-537 3.00e-17

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 77.94  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 267 VEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDSMILLGSVERSELQSLLQRhlcaerrlkaaqdmarklsel 346
Cdd:cd04591     2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA--------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 347 pyngkaqlagdwhpggrpesfafvdededeDLSrkmelpltpappppspppppsqfpiapsnpeepngplpshkqppeas 426
Cdd:cd04591    61 ------------------------------DLR----------------------------------------------- 63

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 427 dsadqrsstfqrllhcllgkahskkkkitqdstdlvdnmspeeieawereqlsqpvcfdcCCIDQSPFQLVEQTTLHKTH 506
Cdd:cd04591    64 ------------------------------------------------------------PIMDPSPFTVTEETSLEKVH 83

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907170599 507 TLFSLLGLHLAYVTSMGKLRGVLALEELQKA 537
Cdd:cd04591    84 DLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
7-243 3.77e-13

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 71.85  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   7 LKELPAFAVIGICCGFLGAVFvylHRQVMLGVRKHKCLSQFLAKHRLLYPGIV--TFVIASLTFPPGMGQFMagelmprE 84
Cdd:PRK05277  214 LNTLWLFLLLGIIFGIFGVLF---NKLLLRTQDLFDRLHGGNKKRWVLMGGAVggLCGLLGLLAPAAVGGGF-------N 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  85 AISTLFDNNTwvkhigdpqslgqsavwlhpqvnVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIM 164
Cdd:PRK05277  284 LIPIALAGNF-----------------------SIGMLLFIFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVA 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 165 AMLFPEgilfddiiYKILPGGYAVIGAAAL-TGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSL--QPsLYD 241
Cdd:PRK05277  341 AALFPQ--------YHIEPGTFAIAGMGALfAATVRAPLTGIVLVLEMTDNYQLILPLIITCLGATLLAQFLggKP-IYS 411


                  ..
gi 1907170599 242 SI 243
Cdd:PRK05277  412 AL 413
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 15-241 1.17e-10

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: 63.79  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  15 VIGICCGFLGAVFVYLhrqVMLGVRK-HKCLSQFLAKHRLLYPGIVTFVIASLTFPPGMGQFMAGELMPREAISTlfdnn 93
Cdd:cd01034   207 VCGVVGGLAGGLFARL---LVALSSGlPGWVRRFRRRRPVLFAALCGLALALIGLVSGGLTFGTGYLQARAALEG----- 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  94 twvkhigdpqslGQSAVWLhpqvnviiiillFFVMKFwMSIVATTMP-IPCGGFMPVFVLGAAFGrlvgEIMAMLFPEgi 172
Cdd:cd01034   279 ------------GGGLPLW------------FGLLKF-LATLLSYWSgIPGGLFAPSLAVGAGLG----SLLAALLGS-- 327

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907170599 173 lfddiiykILPGGYAVIGAAA-LTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQP-SLYD 241
Cdd:cd01034   328 --------VSQGALVLLGMAAfLAGVTQAPLTAFVIVMEMTGDQQMLLPLLAAALLASGVSRLVCPePLYH 390
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
9-245 4.12e-06

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 49.74  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   9 ELPAFAVIGICCGFLGAVFVYLHRqvmlgvrkhkclsqfLAKHRLlypgivtfviASLTFPPGMGQFMAGELMPREAIst 88
Cdd:PRK01862  238 EVLLFVALGVLCGAAAPQFLRLLD---------------ASKNQF----------KRLPVPLPVRLALGGLLVGVISV-- 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  89 lfdnntWVKHI-GDPQSLGQSAVWLHPQVNVIIIILLFFvmkfWMSIVATTMPIPCGG-FMPVFVLGAAFGRLVGEIMAM 166
Cdd:PRK01862  291 ------WVPEVwGNGYSVVNTILHAPWTWQALVAVLVAK----LIATAATAGSGAVGGvFTPTLFVGAVVGSLFGLAMHA 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 167 LFPEGILfddiiykiLPGGYAVIGAAALTGAVSHTVSTAVI-CFELTGQIAHILPMMVAVILANMVAQSLQP-SLYDSII 244
Cdd:PRK01862  361 LWPGHTS--------APFAYAMVGMGAFLAGATQAPLMAILmIFEMTLSYQVVLPLMVSCVVAYFTARALGTtSMYEITL 432


                  .
gi 1907170599 245 Q 245
Cdd:PRK01862  433 R 433
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 3-225 1.13e-04

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: 44.98  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599   3 FPFDLKELPAFAVIGICCGFLGAVFVYLhrqvmlgvrkhkclSQFLAKHR-----LLYPGIVTFVIA---SLTFPpgmgq 74
Cdd:cd01033   198 MQLSTPLLIWALLAGPVLGVVAAGFRRL--------------SQAARAKRpkgkrILWQMPLAFLVIgllSIFFP----- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599  75 fmagELMpreaistlfdnntwvkhiGDPQSLGQSAvwLHPQVNVIIIILLFFVMkfwmsIVATTMPIPCGGF----MPVF 150
Cdd:cd01033   259 ----QIL------------------GNGRALAQLA--FSTTLTLSLLLILLVLK-----IVATLLALRAGAYggllTPSL 309

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907170599 151 VLGAAFGRLVGEIMAMLFPegilfddiiykILP-GGYAVIGAAALTGAVSHTVSTAVI-CFELTGQIAH-ILPMMVAV 225
Cdd:cd01033   310 ALGALLGALLGIVWNALLP-----------PLSiAAFALIGAAAFLAATQKAPLTALIlVLEFTRQNPLfLIPLMLAV 376
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
264-343 7.44e-04

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.23  E-value: 7.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907170599 264 TIFVEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDsmILLGSVERSELQSLLQRHLCAERRLKAAQDMARKL 343
Cdd:COG3448     1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDG--RLVGIVTERDLLRALLPDRLDELEERLLDLPVEDV 78
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 267-319 3.77e-03

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.04  E-value: 3.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907170599 267 VEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDSmiLLGSVERSEL 319
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGK--LVGIVTLKDL 51
 
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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