NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1653961719|ref|NP_000074|]
View 

chloride channel protein 1 [Homo sapiens]

Protein Classification

chloride channel protein( domain architecture ID 10132681)

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|GO:0055085
SCOP:  4003598

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

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. ...
131-592 0e+00

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: 680.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 131 VSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMK 210
Cdd:cd03683    15 ISIAMDFAVEKLLNARRWLYSLLTGNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 211 AFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSI 290
Cdd:cd03683    95 TLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTTFFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 291 EVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHR 370
Cdd:cd03683   175 EVTSTYFAVRNYWRGFFAATCGAFTFRLLAVFFSDQETITALFKTTFFVDFPFDVQELPIFALLGIICGLLGALFVFLHR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 371 QVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPpgmgqfmagelmpreaistlfdnntwvkhagdpeslgqsavwi 450
Cdd:cd03683   255 KIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTFP------------------------------------------- 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 451 hprvnvVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGIlFDDIIYKILPGGYAVIGAA 530
Cdd:cd03683   292 ------FLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVGEIMAVLFPEGI-RGGISNPIGPGGYAVVGAA 364
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653961719 531 ALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPD 592
Cdd:cd03683   365 AFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIYDSIIKIKKLPYLPD 426
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
605-869 8.37e-19

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: 82.95  E-value: 8.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 605 VEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLcperrlraaqemarklsel 684
Cdd:cd04591     2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEADL------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 685 pydgkarlageglpgappgrpesfafvdedededlsgkselppslalhpsttaplspeepngplpghkqqpeapepagqr 764
Cdd:cd04591       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 765 psifqsllhcllgrarptkkkttqdstdlvdnmspeeieaweqeqlsqpvcfdSCCIDQSPFQLVEQTTLHKTHTLFSLL 844
Cdd:cd04591    63 -----------------------------------------------------RPIMDPSPFTVTEETSLEKVHDLFRLL 89
                         250       260
                  ....*....|....*....|....*
gi 1653961719 845 GLHLAYVTSMGKLRGVLALEELQKA 869
Cdd:cd04591    90 GLRHLLVTNNGRLVGIVTRKDLLRA 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. ...
131-592 0e+00

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: 680.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 131 VSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMK 210
Cdd:cd03683    15 ISIAMDFAVEKLLNARRWLYSLLTGNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 211 AFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSI 290
Cdd:cd03683    95 TLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTTFFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 291 EVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHR 370
Cdd:cd03683   175 EVTSTYFAVRNYWRGFFAATCGAFTFRLLAVFFSDQETITALFKTTFFVDFPFDVQELPIFALLGIICGLLGALFVFLHR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 371 QVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPpgmgqfmagelmpreaistlfdnntwvkhagdpeslgqsavwi 450
Cdd:cd03683   255 KIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTFP------------------------------------------- 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 451 hprvnvVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGIlFDDIIYKILPGGYAVIGAA 530
Cdd:cd03683   292 ------FLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVGEIMAVLFPEGI-RGGISNPIGPGGYAVVGAA 364
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653961719 531 ALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPD 592
Cdd:cd03683   365 AFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIYDSIIKIKKLPYLPD 426
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
173-571 3.65e-83

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: 272.50  E-value: 3.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 173 LFSALFCHLISPQAVGSGIPEMKTILRGVvlKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSV 252
Cdd:pfam00654   3 LLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 253 FCGVYEQpyyysDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNkdavtitAL 332
Cdd:pfam00654  81 LSPRDRR-----ILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGNS-------PL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 333 FrtNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKhkalsqFLAKHRLLYPGIVTFVIA--SFTFPPGM 410
Cdd:pfam00654 149 F--SVGEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRK------LLKIPPVLRPALGGLLVGllGLLFPEVL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 411 GQFMagelmprEAISTLFDNNTwvkhagdpeslgqsavwihprvnVVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVL 490
Cdd:pfam00654 221 GGGY-------ELIQLLFNGNT-----------------------SLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAI 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 491 GAAFGRLVGEIMAMLFPDGIlfddiiykILPGGYAVIGAAALTGAVSH-TVSTAVICFELTGQIAHILPMMVAVILANMV 569
Cdd:pfam00654 271 GAALGRAFGLLLALLFPIGG--------LPPGAFALVGMAAFLAAVTRaPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342

                  ..
gi 1653961719 570 AQ 571
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
158-580 8.73e-49

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 179.18  E-value: 8.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 158 PLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPE-MKTILRGvvlKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFV 236
Cdd:COG0038    47 HLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQvIEAIHLK---GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 237 HIASICAAVLSKFMSVfcgvyeQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVF 316
Cdd:COG0038   124 QIGAAIGSLLGRLLRL------SPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 317 RvlavwnkdavtitALFRTNFRMDFP----FDLKELPAFAAIGICCGLLGAVFVYLhrqvmlgVRKHKALSQFLAKHRLL 392
Cdd:COG0038   198 R-------------LLFGNGPLFGVPsvpaLSLLELPLYLLLGILAGLVGVLFNRL-------LLKVERLFKRLKLPPWL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 393 YPGIVTFVIA--SFTFPPGMGqfmAGElmprEAISTLFDNNTwvkhagdpeslgqsavwihprvnVVIIIFLFFVMKFWM 470
Cdd:COG0038   258 RPAIGGLLVGllGLFLPQVLG---SGY----GLIEALLNGEL-----------------------SLLLLLLLLLLKLLA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 471 SIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGIlfddiiykILPGGYAVIGAAALTGAVSHT-VSTAVICFEL 549
Cdd:COG0038   308 TALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG--------LSPGLFALVGMAAVFAAVTRApLTAILLVLEM 379
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1653961719 550 TGQIAHILPMMVAVILANMVAQSLQP-SLYDS 580
Cdd:COG0038   380 TGSYSLLLPLMIACVIAYLVSRLLFPrSIYTA 411
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
161-581 1.28e-25

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 111.14  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 161 FLVWvtfpLVLILFSALFC-------HLISPQAVGSGIPEMKTIL---RGVVLKEYLTMKaFVAKVVALtaglGSGIPVG 230
Cdd:PRK05277   41 LLLW----IVAFLISAVLAmigyflvRRFAPEAGGSGIPEIEGALeglRPVRWWRVLPVK-FFGGLGTL----GSGMVLG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 231 KEGPFVHI-ASICAAVLSKFMSVFCGvyeqpyyYSDILT-VGCAVGVGCCFGTPLGGVLFSIE---------VTStYFAV 299
Cdd:PRK05277  112 REGPTVQMgGNIGRMVLDIFRLRSDE-------ARHTLLaAGAAAGLAAAFNAPLAGILFVIEemrpqfrysLIS-IKAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 300 rnywrgFFAATFSAFVFRVLAvwNKDAV-TITALfrtnfrmDFPfDLKELPAFAAIGICCGLLGAVFvylHRQVMLGVRK 378
Cdd:PRK05277  184 ------FIGVIMATIVFRLFN--GEQAViEVGKF-------SAP-PLNTLWLFLLLGIIFGIFGVLF---NKLLLRTQDL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 379 HKALSQFLAKHRLLYPGIV--TFVIASFTFPPGMGQFMagelmprEAISTLFDNNtwvkhagdpESLGqsavwihprvnv 456
Cdd:PRK05277  245 FDRLHGGNKKRWVLMGGAVggLCGLLGLLAPAAVGGGF-------NLIPIALAGN---------FSIG------------ 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 457 viIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDgilfddiiYKILPGGYAVIGAAAL-TGA 535
Cdd:PRK05277  297 --MLLFIFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVAAALFPQ--------YHIEPGTFAIAGMGALfAAT 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1653961719 536 VSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSL--QPsLYDSI 581
Cdd:PRK05277  367 VRAPLTGIVLVLEMTDNYQLILPLIITCLGATLLAQFLggKP-IYSAL 413
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
605-869 8.37e-19

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: 82.95  E-value: 8.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 605 VEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLcperrlraaqemarklsel 684
Cdd:cd04591     2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEADL------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 685 pydgkarlageglpgappgrpesfafvdedededlsgkselppslalhpsttaplspeepngplpghkqqpeapepagqr 764
Cdd:cd04591       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 765 psifqsllhcllgrarptkkkttqdstdlvdnmspeeieaweqeqlsqpvcfdSCCIDQSPFQLVEQTTLHKTHTLFSLL 844
Cdd:cd04591    63 -----------------------------------------------------RPIMDPSPFTVTEETSLEKVHDLFRLL 89
                         250       260
                  ....*....|....*....|....*
gi 1653961719 845 GLHLAYVTSMGKLRGVLALEELQKA 869
Cdd:cd04591    90 GLRHLLVTNNGRLVGIVTRKDLLRA 114
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
602-681 2.07e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 602 TIFVEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDsmILLGSVERSELQALLQRHLCPERRLRAAQEMARKL 681
Cdd:COG3448     1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDG--RLVGIVTERDLLRALLPDRLDELEERLLDLPVEDV 78
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
605-657 5.39e-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: 5.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1653961719 605 VEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSmiLLGSVERSEL 657
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. ...
131-592 0e+00

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: 680.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 131 VSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMK 210
Cdd:cd03683    15 ISIAMDFAVEKLLNARRWLYSLLTGNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 211 AFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCGVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSI 290
Cdd:cd03683    95 TLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTTFFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSI 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 291 EVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHR 370
Cdd:cd03683   175 EVTSTYFAVRNYWRGFFAATCGAFTFRLLAVFFSDQETITALFKTTFFVDFPFDVQELPIFALLGIICGLLGALFVFLHR 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 371 QVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTFPpgmgqfmagelmpreaistlfdnntwvkhagdpeslgqsavwi 450
Cdd:cd03683   255 KIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTFP------------------------------------------- 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 451 hprvnvVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGIlFDDIIYKILPGGYAVIGAA 530
Cdd:cd03683   292 ------FLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVGEIMAVLFPEGI-RGGISNPIGPGGYAVVGAA 364
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653961719 531 ALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPD 592
Cdd:cd03683   365 AFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIYDSIIKIKKLPYLPD 426
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
131-579 2.55e-141

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: 428.69  E-value: 2.55e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 131 VSWSMDYVSAKSLQAYKWSYAQMQPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMK 210
Cdd:cd01036     7 VAVVLDYAVESSLDAGQWLLRRIPGSYLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 211 AFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSVFCG-------VYEQPYYYSDILTVGCAVGVGCCFGTPL 283
Cdd:cd01036    87 TLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLGchvhlfqLFRNPRDRRDFLVAGAAAGVASAFGAPI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 284 GGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTIT-----ALFRTNFRMDFPFDLKELPAFAAIGICC 358
Cdd:cd01036   167 GGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFELLDrssamFLSLTVFELHVPLNLYEFIPTVVIGVIC 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 359 GLLGAVFVYLHRqVMLGVRKHkALSQFLAKHRLLYPGIVTFVIASFTFPPgmgqfmagelmpreaistlfdnntwvkhag 438
Cdd:cd01036   247 GLLAALFVRLSI-IFLRWRRR-LLFRKTARYRVLEPVLFTLIYSTIHYAP------------------------------ 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 439 dpeslgqsavwihprvnvviIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGILFDDIIYK 518
Cdd:cd01036   295 --------------------TLLLFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIGAESATLW 354
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1653961719 519 ILPGGYAVIGAAALTGAVS-HTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYD 579
Cdd:cd01036   355 ADPGVYALIGAAAFLGGTTrLTFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFCESLYH 416
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
161-590 1.82e-83

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: 276.80  E-value: 1.82e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 161 FLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIAS 240
Cdd:cd03684    28 YIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIAT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 241 ICAAVLSKFMsvfcgvyeqPYYYS------DILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAF 314
Cdd:cd03684   108 CVGNIISRLF---------PKYRRneakrrEILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAF 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 315 VFRVLAVWNKDAvtiTALFRTNFrmDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKHKalsqfLAKHRLLYP 394
Cdd:cd03684   179 TLKSLNPFGTGR---LVLFEVEY--DRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSL-----LKRYPVLEV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 395 GIVTFVIASFTFP-PGMGQFMAgelmprEAISTLFDNNTwvkhAGDPESLGQSAVWIHPRVNVVIIIFLFF--VMKFWMS 471
Cdd:cd03684   249 LLVALITALISFPnPYTRLDMT------ELLELLFNECE----PGDDNSLCCYRDPPAGDGVYKALWSLLLalIIKLLLT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 472 IVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAML---FPDGILF-------DDIIykilPGGYAVIGAAALTGAVSH-TV 540
Cdd:cd03684   319 IFTFGIKVPAGIFVPSMAVGALFGRIVGILVEQLaysYPDSIFFacctagpSCIT----PGLYAMVGAAAFLGGVTRmTV 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1653961719 541 STAVICFELTGQIAHILPMMVAVILANMVAQSLQP-SLYDSIIQVKKLPYL 590
Cdd:cd03684   395 SLVVIMFELTGALNYILPLMIAVMVSKWVADAIGKeGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
173-571 3.65e-83

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: 272.50  E-value: 3.65e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 173 LFSALFCHLISPQAVGSGIPEMKTILRGVvlKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSV 252
Cdd:pfam00654   3 LLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 253 FCGVYEQpyyysDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNkdavtitAL 332
Cdd:pfam00654  81 LSPRDRR-----ILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGNS-------PL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 333 FrtNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMLGVRKhkalsqFLAKHRLLYPGIVTFVIA--SFTFPPGM 410
Cdd:pfam00654 149 F--SVGEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRK------LLKIPPVLRPALGGLLVGllGLLFPEVL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 411 GQFMagelmprEAISTLFDNNTwvkhagdpeslgqsavwihprvnVVIIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVL 490
Cdd:pfam00654 221 GGGY-------ELIQLLFNGNT-----------------------SLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAI 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 491 GAAFGRLVGEIMAMLFPDGIlfddiiykILPGGYAVIGAAALTGAVSH-TVSTAVICFELTGQIAHILPMMVAVILANMV 569
Cdd:pfam00654 271 GAALGRAFGLLLALLFPIGG--------LPPGAFALVGMAAFLAAVTRaPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342

                  ..
gi 1653961719 570 AQ 571
Cdd:pfam00654 343 SR 344
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
161-590 1.78e-65

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: 228.31  E-value: 1.78e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 161 FLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIAS 240
Cdd:cd03685    78 FLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGA 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 241 ICAAVLSKFMSVFCGVYEQ--PYYYS-----DILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSA 313
Cdd:cd03685   158 CIAAGLSQGGSTSLRLDFRwfRYFRNdrdkrDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVT 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 314 FVFRVLAVW---NKDAVTITALFRTNFRMDFP--FDLKELPAFAAIGICCGLLGAVFVYLHRQVmLGVRKhkalsQFLAK 388
Cdd:cd03685   238 FTLNFFLSGcnsGKCGLFGPGGLIMFDGSSTKylYTYFELIPFMLIGVIGGLLGALFNHLNHKV-TRFRK-----RINHK 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 389 HRLLYPgIVTFVIASFTfppGMGQFMagelmpreaiSTLfdnntwvkhagdpeslgqsavwihprvnvviiiFLFFVMKF 468
Cdd:cd03685   312 GKLLKV-LEALLVSLVT---SVVAFP----------QTL---------------------------------LIFFVLYY 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 469 WMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGilfddiiyKILPGGYAVIGAAALTGAVSH-TVSTAVICF 547
Cdd:cd03685   345 FLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFT--------SIDPGLYALLGAAAFLGGVMRmTVSLTVILL 416
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1653961719 548 ELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYL 590
Cdd:cd03685   417 ELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
162-567 2.20e-53

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: 191.24  E-value: 2.20e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 162 LVWVTFPLVLILFSALFCHLISPqAVGSGIPE-MKTILRGvvlKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFVHIAS 240
Cdd:cd00400    38 LYILLVPVIGGLLVGLLVRLLGP-ARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 241 ICAAVLSKFMSVfcgvyeqPYYYSDILTV-GCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVL 319
Cdd:cd00400   114 AIGSWLGRRLRL-------SRNDRRILVAcGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 320 AVWnkdavtiTALFrtNFRMDFPFDLKELPAFAAIGICCGLLGAVFVYLHRQVMlgvrkhkALSQFLAKHRLLYP---GI 396
Cdd:cd00400   187 FGA-------EPAF--GVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIE-------RLFRRLPIPPWLRPalgGL 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 397 VTFVIASFtFPPGMGqfmAGElmprEAISTLFDNNTwvkhagdpeslgqsavwihprvnVVIIIFLFFVMKFWMSIVATT 476
Cdd:cd00400   251 LLGLLGLF-LPQVLG---SGY----GAILLALAGEL-----------------------SLLLLLLLLLLKLLATALTLG 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 477 MPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGIlfddiiykILPGGYAVIGAAALTGAVSHT-VSTAVICFELTGQIAH 555
Cdd:cd00400   300 SGFPGGVFAPSLFIGAALGAAFGLLLPALFPGLV--------ASPGAYALVGMAALLAAVLRApLTAILLVLELTGDYSL 371
                         410
                  ....*....|..
gi 1653961719 556 ILPMMVAVILAN 567
Cdd:cd00400   372 LLPLMLAVVIAY 383
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
158-580 8.73e-49

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 179.18  E-value: 8.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 158 PLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPE-MKTILRGvvlKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPFV 236
Cdd:COG0038    47 HLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQvIEAIHLK---GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 237 HIASICAAVLSKFMSVfcgvyeQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVF 316
Cdd:COG0038   124 QIGAAIGSLLGRLLRL------SPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVS 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 317 RvlavwnkdavtitALFRTNFRMDFP----FDLKELPAFAAIGICCGLLGAVFVYLhrqvmlgVRKHKALSQFLAKHRLL 392
Cdd:COG0038   198 R-------------LLFGNGPLFGVPsvpaLSLLELPLYLLLGILAGLVGVLFNRL-------LLKVERLFKRLKLPPWL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 393 YPGIVTFVIA--SFTFPPGMGqfmAGElmprEAISTLFDNNTwvkhagdpeslgqsavwihprvnVVIIIFLFFVMKFWM 470
Cdd:COG0038   258 RPAIGGLLVGllGLFLPQVLG---SGY----GLIEALLNGEL-----------------------SLLLLLLLLLLKLLA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 471 SIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGIlfddiiykILPGGYAVIGAAALTGAVSHT-VSTAVICFEL 549
Cdd:COG0038   308 TALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG--------LSPGLFALVGMAAVFAAVTRApLTAILLVLEM 379
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1653961719 550 TGQIAHILPMMVAVILANMVAQSLQP-SLYDS 580
Cdd:COG0038   380 TGSYSLLLPLMIACVIAYLVSRLLFPrSIYTA 411
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
133-583 1.06e-45

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: 169.64  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 133 WSMDYVSAKSLQAYKWSyaqmqPSLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMKTILRGvvLKEYLTMKAF 212
Cdd:cd01031    14 LGIDKLGNLRLSLYDFA-----ANNPPLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAG--LLPPNWWRVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 213 VAKVVALTAGLGSGIPVGKEGPFVHI-ASICAAVLSKFMSvfcgvyeQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIE 291
Cdd:cd01031    87 PVKFVGGVLALGSGLSLGREGPSVQIgAAIGQGVSKWFKT-------SPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 292 VTSTYFAVRNYWRGFFAATFSAFVFRVlavwnkdavtitaLFRTNFRMDFP----FDLKELPAFAAIGICCGLLGAVFvy 367
Cdd:cd01031   160 ELRHSFSPLALLTALVASIAADFVSRL-------------FFGLGPVLSIPplpaLPLKSYWLLLLLGIIAGLLGYLF-- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 368 lhrQVMLgVRKHKALSQFLAKHRLLYPGIVTFVIA--SFTFPPGMGQfmaGELMpreaISTLFDNNTWVKhagdpeslgq 445
Cdd:cd01031   225 ---NRSL-LKSQDLYRKLKKLPRELRVLLPGLLIGplGLLLPEALGG---GHGL----ILSLAGGNFSIS---------- 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 446 savwihprvnvviIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDGIlfddiiykILPGGYA 525
Cdd:cd01031   284 -------------LLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLGLLFGTILVQLGPIPI--------SAPATFA 342
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 526 VIGAAALTGAVSHTVSTAVI-CFELTGQIAHILPMMVAVILANMVAQSLQ-PSLYDSIIQ 583
Cdd:cd01031   343 IAGMAAFFAAVVRAPITAIIlVTEMTGNFNLLLPLMVVCLVAYLVADLLGgKPIYEALLE 402
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
161-581 1.28e-25

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 111.14  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 161 FLVWvtfpLVLILFSALFC-------HLISPQAVGSGIPEMKTIL---RGVVLKEYLTMKaFVAKVVALtaglGSGIPVG 230
Cdd:PRK05277   41 LLLW----IVAFLISAVLAmigyflvRRFAPEAGGSGIPEIEGALeglRPVRWWRVLPVK-FFGGLGTL----GSGMVLG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 231 KEGPFVHI-ASICAAVLSKFMSVFCGvyeqpyyYSDILT-VGCAVGVGCCFGTPLGGVLFSIE---------VTStYFAV 299
Cdd:PRK05277  112 REGPTVQMgGNIGRMVLDIFRLRSDE-------ARHTLLaAGAAAGLAAAFNAPLAGILFVIEemrpqfrysLIS-IKAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 300 rnywrgFFAATFSAFVFRVLAvwNKDAV-TITALfrtnfrmDFPfDLKELPAFAAIGICCGLLGAVFvylHRQVMLGVRK 378
Cdd:PRK05277  184 ------FIGVIMATIVFRLFN--GEQAViEVGKF-------SAP-PLNTLWLFLLLGIIFGIFGVLF---NKLLLRTQDL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 379 HKALSQFLAKHRLLYPGIV--TFVIASFTFPPGMGQFMagelmprEAISTLFDNNtwvkhagdpESLGqsavwihprvnv 456
Cdd:PRK05277  245 FDRLHGGNKKRWVLMGGAVggLCGLLGLLAPAAVGGGF-------NLIPIALAGN---------FSIG------------ 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 457 viIIFLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPDgilfddiiYKILPGGYAVIGAAAL-TGA 535
Cdd:PRK05277  297 --MLLFIFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVAAALFPQ--------YHIEPGTFAIAGMGALfAAT 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1653961719 536 VSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSL--QPsLYDSI 581
Cdd:PRK05277  367 VRAPLTGIVLVLEMTDNYQLILPLIITCLGATLLAQFLggKP-IYSAL 413
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
151-579 3.81e-24

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: 105.77  E-value: 3.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 151 AQMQPSLPLqfLVWVTFPLVLILfSALFCHLISPQAVGSGIPEMKTILR---GVVLKEYLTMKAFVAKVVALTAGLGSGI 227
Cdd:cd01034    19 QRLTATHPW--LPLLLTPAGFAL-IAWLTRRFFPGAAGSGIPQVIAALElpsAAARRRLLSLRTAVGKILLTLLGLLGGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 228 PVGKEGPFVHIAsicAAVLSKFMSVfCGVYEQPYYYSDILTvGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFF 307
Cdd:cd01034    96 SVGREGPSVQIG---AAVMLAIGRR-LPKWGGLSERGLILA-GGAAGLAAAFNTPLAGIVFAIEELSRDFELRFSGLVLL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 308 AATFSAFVfrVLAVWNkdavTITALFRTNFRMDFPFDLkeLPAfAAIGICCGLLGAVFVYLhrQVMLGVRKHKALSQFLA 387
Cdd:cd01034   171 AVIAAGLV--SLAVLG----NYPYFGVAAVALPLGEAW--LLV-LVCGVVGGLAGGLFARL--LVALSSGLPGWVRRFRR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 388 KHRLLYPGIVTFVIASFTFPPGMGQFMAGELMPREAISTlfdnntwvkhagdpeslGQSAVWihprvnvviiifLFFVMK 467
Cdd:cd01034   240 RRPVLFAALCGLALALIGLVSGGLTFGTGYLQARAALEG-----------------GGGLPL------------WFGLLK 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 468 FwMSIVATTMP-IPCGGFMPVFVLGAAFGRLVGEIMAmlfpdgilfddiiyKILPGGYAVIGAAA-LTGAVSHTVSTAVI 545
Cdd:cd01034   291 F-LATLLSYWSgIPGGLFAPSLAVGAGLGSLLAALLG--------------SVSQGALVLLGMAAfLAGVTQAPLTAFVI 355
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1653961719 546 CFELTGQIAHILPMMVAVILANMVAQSLQP-SLYD 579
Cdd:cd01034   356 VMEMTGDQQMLLPLLAAALLASGVSRLVCPePLYH 390
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
605-869 8.37e-19

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: 82.95  E-value: 8.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 605 VEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSMILLGSVERSELQALLQRHLcperrlraaqemarklsel 684
Cdd:cd04591     2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEADL------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 685 pydgkarlageglpgappgrpesfafvdedededlsgkselppslalhpsttaplspeepngplpghkqqpeapepagqr 764
Cdd:cd04591       --------------------------------------------------------------------------------
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 765 psifqsllhcllgrarptkkkttqdstdlvdnmspeeieaweqeqlsqpvcfdSCCIDQSPFQLVEQTTLHKTHTLFSLL 844
Cdd:cd04591    63 -----------------------------------------------------RPIMDPSPFTVTEETSLEKVHDLFRLL 89
                         250       260
                  ....*....|....*....|....*
gi 1653961719 845 GLHLAYVTSMGKLRGVLALEELQKA 869
Cdd:cd04591    90 GLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
223-583 6.94e-14

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 75.55  E-value: 6.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 223 LGSGIPVGKEGPFVHIASICAAVLSKFmsvfcgVYEQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNY 302
Cdd:PRK01862  129 IGSGGSIGREGPMVQLAALAASLVGRF------AHFDPPRLRLLVACGAAAGITSAYNAPIAGAFFVAEIVLGSIAMESF 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 303 WRGFFAATFSAFVFRVLAVwnkdavtitalFRTNFRMD-FPFDL-KELPAFAAIGICCGLLGAVFVylhRQVMLGVRKHK 380
Cdd:PRK01862  203 GPLVVASVVANIVMREFAG-----------YQPPYEMPvFPAVTgWEVLLFVALGVLCGAAAPQFL---RLLDASKNQFK 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 381 ALSQFLAKhRLLYPGIVTFVIASFtFPP--GMGQFMAGELmpreaistLFDNNTWVkhagdpeslgqsAVWihprvnvvi 458
Cdd:PRK01862  269 RLPVPLPV-RLALGGLLVGVISVW-VPEvwGNGYSVVNTI--------LHAPWTWQ------------ALV--------- 317
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 459 iifLFFVMKfWMSIVATTMPIPCGG-FMPVFVLGAAFGRLVGEIMAMLFPDGILfddiiykiLPGGYAVIGAAALTGAVS 537
Cdd:PRK01862  318 ---AVLVAK-LIATAATAGSGAVGGvFTPTLFVGAVVGSLFGLAMHALWPGHTS--------APFAYAMVGMGAFLAGAT 385
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1653961719 538 HTVSTAVI-CFELTGQIAHILPMMVAVILANMVAQSLQP-SLYDSIIQ 583
Cdd:PRK01862  386 QAPLMAILmIFEMTLSYQVVLPLMVSCVVAYFTARALGTtSMYEITLR 433
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
224-563 5.42e-07

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: 53.07  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 224 GSGIPVGKEGpfvhiAS-ICAAVLSKFMSVFCGVYEqpyyySD---ILTVGCAVGVGCCFGTPLGGVLFSIEVTstyfAV 299
Cdd:cd01033    97 GLGAPLGREV-----APrEVGALLAQRFSDWLGLTV-----ADrrlLVACAAGAGLAAVYNVPLAGALFALEIL----LR 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 300 RNYWRGFFAATFSAFVfrvlavwnkdAVTITALF---RTNFR-MDFPFDLKELPAFAAIGICCGLLGAVFVYLhrqvMLG 375
Cdd:cd01033   163 TISLRSVVAALATSAI----------AAAVASLLkgdHPIYDiPPMQLSTPLLIWALLAGPVLGVVAAGFRRL----SQA 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 376 VRKHKALSQflakhRLLYPGIVTFVIA---SFTFPpgmgqfmagELMpreaistlfdnntwvkhaGDPESLGQSAvwIHP 452
Cdd:cd01033   229 ARAKRPKGK-----RILWQMPLAFLVIgllSIFFP---------QIL------------------GNGRALAQLA--FST 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 453 RVNVVIIIFLFFVMkfwmsIVATTMPIPCGGF----MPVFVLGAAFGRLVGEIMAMLFPdgilfddiiykILP-GGYAVI 527
Cdd:cd01033   275 TLTLSLLLILLVLK-----IVATLLALRAGAYggllTPSLALGALLGALLGIVWNALLP-----------PLSiAAFALI 338
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1653961719 528 GAAALTGAVSHTVSTAVI-CFELTGQIAH-ILPMMVAV 563
Cdd:cd01033   339 GAAAFLAATQKAPLTALIlVLEFTRQNPLfLIPLMLAV 376
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
480-578 1.45e-04

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 45.54  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 480 PCGGFMPVFVLGAAFGRLVGEIMAMLFPDGilfDDIIykILPGgyaVIGAAALTGAVSHT--VSTAVICfELTGQIAHIL 557
Cdd:PRK01610  318 PGGVFTPTLFVGLAIGMLYGRSLGLWLPDG---EEIT--LLLG---LTGMATLLAATTHApiMSTLMIC-EMTGEYQLLP 388
                          90       100
                  ....*....|....*....|..
gi 1653961719 558 PMMVAVILANMVAQSLQP-SLY 578
Cdd:PRK01610  389 GLLIACVIASVISRTLRRdSIY 410
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
602-681 2.07e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 602 TIFVEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDsmILLGSVERSELQALLQRHLCPERRLRAAQEMARKL 681
Cdd:COG3448     1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDG--RLVGIVTERDLLRALLPDRLDELEERLLDLPVEDV 78
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
229-413 2.12e-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: 41.41  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 229 VGKEGPFVHIASICAAVLSKFMSVfcgvyeQPYYYSDILTVGCAVGVGCCFGTPLGGVLFSIEVTS----TYFAVrnywr 304
Cdd:cd03682    95 AGREGTAVQMGGSLADAFGRVFKL------PEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEVLVlgrlRYSAL----- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 305 gffaatFSAFVFRVLAVWnkdAVTITALFRTNFRMDFPFDLKELP--AFAAIGICCGLLGAVFVYLhrqvmlgVRKHKAL 382
Cdd:cd03682   164 ------IPCLVAAIVADW---VSHALGLEHTHYHIVFIPTLDPLLfvKVILAGIIFGLAGRLFAEL-------LHFLKKL 227
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1653961719 383 SQFLAKHRLLYPGIVTFVIASFTFPPGMGQF 413
Cdd:cd03682   228 LKKRIKNPYLRPFVGGLLIILLVYLLGSRRY 258
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
145-296 2.28e-03

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 41.38  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1653961719 145 AYKWSYAQMQPSLPLQFLVW-VTFPLVLILFSALfCHLISPQAVGSGIPEMKTILRGVVLKEYLTMkAFVAKVVALTAGL 223
Cdd:pfam00654 178 LFNRLLLKVQRLFRKLLKIPpVLRPALGGLLVGL-LGLLFPEVLGGGYELIQLLFNGNTSLSLLLL-LLLLKFLATALSL 255
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1653961719 224 GSGIPVGKEGPFVHIASICAAVLSKFM-SVFCGVYEQPYYYsdILtVGCAVGVGCCFGTPLGGVLFSIEVTSTY 296
Cdd:pfam00654 256 GSGAPGGIFAPSLAIGAALGRAFGLLLaLLFPIGGLPPGAF--AL-VGMAAFLAAVTRAPLTAIVIVFELTGSL 326
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
605-657 5.39e-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: 5.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1653961719 605 VEDIMVRDVKFVSASYTYGELRTLLQTTTVKTLPLVDSKDSmiLLGSVERSEL 657
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH