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Conserved domains on  [gi|922582198|ref|NP_001300531|]
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Chloride channel protein [Caenorhabditis elegans]

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

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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. ...
83-575 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: 661.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   83 DWIFLALLGFIMASLSFGMDYAILNLQNGQMRLFDLVKEYHFtLAYLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPEMK 162
Cdd:cd03683     1 DWLFLALLGILMALISIAMDFAVEKLLNARRWLYSLLTGNSL-LQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  163 TILRGVILKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHgSSGGIFENESRSGEMLAAGCAVG 242
Cdd:cd03683    80 TILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTT-FFSGIYENESRRMEMLAAACAVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  243 VACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILRMFsVSAAVTVEAHYQTNFPPQNVFLPQELPIFAL 322
Cdd:cd03683   159 VACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTFRLLAVF-FSDQETITALFKTTFFVDFPFDVQELPIFAL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  323 IGLVCGLAGSIFVYLHRRTVLFLRRNWLAKMIFQKYWLIYPIFIATFISSLSFplglgkfmggeerfshtmkeffvdcaw 402
Cdd:cd03683   238 LGIICGLLGALFVFLHRKIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTF--------------------------- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  403 tappndsyacpmptsnatssdsfdirhwkgdnydysPFVTLSSFQVVYFFLAILASTLPVPSGIFMPVFVLGAAFGRLVG 482
Cdd:cd03683   291 ------------------------------------PFLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVG 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  483 EGVFSLDPYGhISGDIQFFVRPGVYAVVGAAAFCGAVTHTVSVAVIVFELTGQLCHLLPVMIAVLIANAVASYLQPSIYD 562
Cdd:cd03683   335 EIMAVLFPEG-IRGGISNPIGPGGYAVVGAAAFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIYD 413
                         490
                  ....*....|...
gi 922582198  563 SIIRIKNLPYLPD 575
Cdd:cd03683   414 SIIKIKKLPYLPD 426
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
814-868 7.14e-15

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: 71.78  E-value: 7.14e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922582198  814 DLSQLdIDSTPFQLSEYTSLFKAHSLFSLLGLNRAYVTKKGQLIGVVALKELRLA 868
Cdd:cd04591    61 DLRPI-MDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
587-642 1.75e-14

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: 70.63  E-value: 1.75e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922582198  587 LIEQFMISPLVYIAKDSTVGDIKRALETkTRIRAFPLVENMESLALVGSVSRSQLQ 642
Cdd:cd04591     1 TAEDVMRPPLTVLARDETVGDIVSVLKT-TDHNGFPVVDSTESQTLVGFILRSQLI 55
 
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. ...
83-575 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: 661.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   83 DWIFLALLGFIMASLSFGMDYAILNLQNGQMRLFDLVKEYHFtLAYLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPEMK 162
Cdd:cd03683     1 DWLFLALLGILMALISIAMDFAVEKLLNARRWLYSLLTGNSL-LQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  163 TILRGVILKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHgSSGGIFENESRSGEMLAAGCAVG 242
Cdd:cd03683    80 TILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTT-FFSGIYENESRRMEMLAAACAVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  243 VACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILRMFsVSAAVTVEAHYQTNFPPQNVFLPQELPIFAL 322
Cdd:cd03683   159 VACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTFRLLAVF-FSDQETITALFKTTFFVDFPFDVQELPIFAL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  323 IGLVCGLAGSIFVYLHRRTVLFLRRNWLAKMIFQKYWLIYPIFIATFISSLSFplglgkfmggeerfshtmkeffvdcaw 402
Cdd:cd03683   238 LGIICGLLGALFVFLHRKIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTF--------------------------- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  403 tappndsyacpmptsnatssdsfdirhwkgdnydysPFVTLSSFQVVYFFLAILASTLPVPSGIFMPVFVLGAAFGRLVG 482
Cdd:cd03683   291 ------------------------------------PFLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVG 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  483 EGVFSLDPYGhISGDIQFFVRPGVYAVVGAAAFCGAVTHTVSVAVIVFELTGQLCHLLPVMIAVLIANAVASYLQPSIYD 562
Cdd:cd03683   335 EIMAVLFPEG-IRGGISNPIGPGGYAVVGAAAFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIYD 413
                         490
                  ....*....|...
gi 922582198  563 SIIRIKNLPYLPD 575
Cdd:cd03683   414 SIIKIKKLPYLPD 426
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
140-554 5.04e-79

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: 261.71  E-value: 5.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   140 LLSAVCAHYIAPQAIGSGIPEMKTILRGVilKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHG 219
Cdd:pfam00654    3 LLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLFR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   220 SSggifENESRsgEMLAAGCAVGVACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILrmFSVSAAVTVE 299
Cdd:pfam00654   81 LS----PRDRR--ILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNSPLFSVG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   300 AHYQTNfppqnvflPQELPIFALIGLVCGLAGSIFVYLHRRtVLFLRRNWLakmifQKYWLIYPIFIATFISSLSfpLGL 379
Cdd:pfam00654  153 EPGSLS--------LLELPLFILLGILCGLLGALFNRLLLK-VQRLFRKLL-----KIPPVLRPALGGLLVGLLG--LLF 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   380 GKFMGGEErfsHTMKEFFVDCawtappndsyacpmptsnatssdsfdirhwkgdnydySPFVTLSSFQVVYFFLAILAST 459
Cdd:pfam00654  217 PEVLGGGY---ELIQLLFNGN-------------------------------------TSLSLLLLLLLLKFLATALSLG 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   460 LPVPSGIFMPVFVLGAAFGRLVGEGVFSLDPYGHISgdiqffvrPGVYAVVGAAAFCGAVTH-TVSVAVIVFELTGQLCH 538
Cdd:pfam00654  257 SGAPGGIFAPSLAIGAALGRAFGLLLALLFPIGGLP--------PGAFALVGMAAFLAAVTRaPLTAIVIVFELTGSLQL 328
                          410
                   ....*....|....*.
gi 922582198   539 LLPVMIAVLIANAVAS 554
Cdd:pfam00654  329 LLPLMLAVLIAYAVSR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
84-566 5.48e-56

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 199.98  E-value: 5.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   84 WIFLALL-GFIMASLSFGMDYAILNLQNgqMRLFDLVKEYHFTLAYLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPE-M 161
Cdd:COG0038     7 LLLLAVLvGILAGLAAVLFRLLLELATH--LFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQvI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  162 KTILRGvilKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHGSsggifENESRSgeMLAAGCAV 241
Cdd:COG0038    85 EAIHLK---GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLS-----PEDRRI--LLAAGAAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  242 GVACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILRMFsvsaavtvEAHYQtnFPPQNVFLPQELPIFA 321
Cdd:COG0038   155 GLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLLFGN--------GPLFG--VPSVPALSLLELPLYL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  322 LIGLVCGLAGSIFVylhrRTVLFLRRnWLAKMIFQKYWLIYPIFIATFISSLSFP--LGLGKfmggeerfsHTMKEFFvd 399
Cdd:COG0038   225 LLGILAGLVGVLFN----RLLLKVER-LFKRLKLPPWLRPAIGGLLVGLLGLFLPqvLGSGY---------GLIEALL-- 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  400 cawtappndsyacpmptsnatsSDSFDIrhwkgdnydyspfvtlsSFQVVYFFLAILASTLPV----PSGIFMPVFVLGA 475
Cdd:COG0038   289 ----------------------NGELSL-----------------LLLLLLLLLKLLATALTLgsggPGGIFAPSLFIGA 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  476 AFGRLVGEGVFSLDPYGHISgdiqffvrPGVYAVVGAAAFCGAVTHT-VSVAVIVFELTGQLCHLLPVMIAVLIANAVAS 554
Cdd:COG0038   330 LLGAAFGLLLNLLFPGLGLS--------PGLFALVGMAAVFAAVTRApLTAILLVLEMTGSYSLLLPLMIACVIAYLVSR 401
                         490
                  ....*....|...
gi 922582198  555 YLQP-SIYDSIIR 566
Cdd:COG0038   402 LLFPrSIYTAQLE 414
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
88-566 6.17e-30

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 124.23  E-value: 6.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   88 ALLGFIMASLSFGMDYAILNLQNGQMRLFDLVKEYhftlAYLVWVGYvvglILLSAVCA-------HYIAPQAIGSGIPE 160
Cdd:PRK05277    5 AVVGTLTGLVGVAFELAVDWVQNQRLGLLASVADN----GLLLWIVA----FLISAVLAmigyflvRRFAPEAGGSGIPE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  161 MKTIL---RGVILKEYLSVrtllsKMIGLTLSLGSGLPMGKEGPFVHVASVVAsqltRLVhgssGGIFenESRSGE---- 233
Cdd:PRK05277   77 IEGALeglRPVRWWRVLPV-----KFFGGLGTLGSGMVLGREGPTVQMGGNIG----RMV----LDIF--RLRSDEarht 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  234 MLAAGCAVGVACTFSAPIGGVLFSIE---------VTSvYFAVrnywrgfFAATCSATLfrILRMFSVSAAVTVEAHYQt 304
Cdd:PRK05277  142 LLAAGAAAGLAAAFNAPLAGILFVIEemrpqfrysLIS-IKAV-------FIGVIMATI--VFRLFNGEQAVIEVGKFS- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  305 nFPPQNVflpqeLPIFALIGLVCGLAGSIFVYLHRRTV-LFLRRNWLAKmifQKYWLIYPIFIATFisslsfplGLGkfm 383
Cdd:PRK05277  211 -APPLNT-----LWLFLLLGIIFGIFGVLFNKLLLRTQdLFDRLHGGNK---KRWVLMGGAVGGLC--------GLL--- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  384 ggeerfshtmkeffvdcAWTAPPndsyacpmptsnaTSSDSFDIRHWKGDNydYSPFVTLSSFQVVYFFLAILASTLPVP 463
Cdd:PRK05277  271 -----------------GLLAPA-------------AVGGGFNLIPIALAG--NFSIGMLLFIFVARFITTLLCFGSGAP 318
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  464 SGIFMPVFVLGAAFGRLVGEGVFSLDPyghisgdiQFFVRPGVYAVVGAAA-FCGAVTHTVSVAVIVFELTGQLCHLLPV 542
Cdd:PRK05277  319 GGIFAPMLALGTLLGLAFGMVAAALFP--------QYHIEPGTFAIAGMGAlFAATVRAPLTGIVLVLEMTDNYQLILPL 390
                         490       500
                  ....*....|....*....|....*.
gi 922582198  543 MIAVLIANAVASYL--QPsIYDSIIR 566
Cdd:PRK05277  391 IITCLGATLLAQFLggKP-IYSALLE 415
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
814-868 7.14e-15

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: 71.78  E-value: 7.14e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922582198  814 DLSQLdIDSTPFQLSEYTSLFKAHSLFSLLGLNRAYVTKKGQLIGVVALKELRLA 868
Cdd:cd04591    61 DLRPI-MDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
587-642 1.75e-14

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: 70.63  E-value: 1.75e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922582198  587 LIEQFMISPLVYIAKDSTVGDIKRALETkTRIRAFPLVENMESLALVGSVSRSQLQ 642
Cdd:cd04591     1 TAEDVMRPPLTVLARDETVGDIVSVLKT-TDHNGFPVVDSTESQTLVGFILRSQLI 55
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
586-664 1.47e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.85  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582198  586 MLIEQFMISPLVYIAKDSTVGDIKRALETKtRIRAFPLVEnmESLALVGSVSRSQLQRYVDSQIGTKARFAEATRRIKQ 664
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREH-GIRGLPVVD--EDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVED 77
 
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. ...
83-575 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: 661.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   83 DWIFLALLGFIMASLSFGMDYAILNLQNGQMRLFDLVKEYHFtLAYLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPEMK 162
Cdd:cd03683     1 DWLFLALLGILMALISIAMDFAVEKLLNARRWLYSLLTGNSL-LQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  163 TILRGVILKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHgSSGGIFENESRSGEMLAAGCAVG 242
Cdd:cd03683    80 TILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTT-FFSGIYENESRRMEMLAAACAVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  243 VACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILRMFsVSAAVTVEAHYQTNFPPQNVFLPQELPIFAL 322
Cdd:cd03683   159 VACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTFRLLAVF-FSDQETITALFKTTFFVDFPFDVQELPIFAL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  323 IGLVCGLAGSIFVYLHRRTVLFLRRNWLAKMIFQKYWLIYPIFIATFISSLSFplglgkfmggeerfshtmkeffvdcaw 402
Cdd:cd03683   238 LGIICGLLGALFVFLHRKIVRFRRKNRLFSKFLKRSPLLYPAIVALLTAVLTF--------------------------- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  403 tappndsyacpmptsnatssdsfdirhwkgdnydysPFVTLSSFQVVYFFLAILASTLPVPSGIFMPVFVLGAAFGRLVG 482
Cdd:cd03683   291 ------------------------------------PFLTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVG 334
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  483 EGVFSLDPYGhISGDIQFFVRPGVYAVVGAAAFCGAVTHTVSVAVIVFELTGQLCHLLPVMIAVLIANAVASYLQPSIYD 562
Cdd:cd03683   335 EIMAVLFPEG-IRGGISNPIGPGGYAVVGAAAFSGAVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQPSIYD 413
                         490
                  ....*....|...
gi 922582198  563 SIIRIKNLPYLPD 575
Cdd:cd03683   414 SIIKIKKLPYLPD 426
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
91-562 4.16e-118

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: 368.98  E-value: 4.16e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   91 GFIMASLSFGMDYAILN-LQNGQMRLFDLVKEYhfTLAYLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPEMKTILRGVI 169
Cdd:cd01036     1 GLLMGLVAVVLDYAVESsLDAGQWLLRRIPGSY--LLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  170 LKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHGSSG------GIFENESRSGEMLAAGCAVGV 243
Cdd:cd01036    79 LPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLGchvhlfQLFRNPRDRRDFLVAGAAAGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  244 ACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILRMF----------SVSAAVTVEAHYQTnfpPQNVFl 313
Cdd:cd01036   159 ASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNSFnsgfelldrsSAMFLSLTVFELHV---PLNLY- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  314 pqELPIFALIGLVCGLAGSIFVYLHRRtvLFLRRNWLAKMIFQKYWLIYPIFIATFISSLSFplglgkfmggeerfshtm 393
Cdd:cd01036   235 --EFIPTVVIGVICGLLAALFVRLSII--FLRWRRRLLFRKTARYRVLEPVLFTLIYSTIHY------------------ 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  394 keffvdcawtappndsyacpmptsnatssdsfdirhwkgdnydyspFVTLSSFQVVYFFLAILASTLPVPSGIFMPVFVL 473
Cdd:cd01036   293 ----------------------------------------------APTLLLFLLIYFWMSALAFGIAVPGGTFIPSLVI 326
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  474 GAAFGRLVGEGVFSLDPYGHISGDIQFFVRPGVYAVVGAAAFCGAVT-HTVSVAVIVFELTGQLCHLLPVMIAVLIANAV 552
Cdd:cd01036   327 GAAIGRLVGLLVHRIAVAGIGAESATLWADPGVYALIGAAAFLGGTTrLTFSICVIMMELTGDLHHLLPLMVAILIAKAV 406
                         490
                  ....*....|
gi 922582198  553 ASYLQPSIYD 562
Cdd:cd01036   407 ADAFCESLYH 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 ...
128-573 3.52e-92

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: 301.06  E-value: 3.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  128 YLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPEMKTILRGVILKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVAS 207
Cdd:cd03684    28 YIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIAT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  208 VVASQLTRLVhgssGGIFENESRSGEMLAAGCAVGVACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRIL 287
Cdd:cd03684   108 CVGNIISRLF----PKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  288 RMFSVSAAVTVEAHYQTNfppqnvFLPQELPIFALIGLVCGLAGSIFVYLHRRTVLFLRRNwlakmiFQKYWLIYPIFIA 367
Cdd:cd03684   184 NPFGTGRLVLFEVEYDRD------WHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKS------LLKRYPVLEVLLV 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  368 TFISSL-SFPLGLGKfMGGEErfshTMKEFFVDC-AWTAPPNDSYACPmptsnaTSSDSFdirhwkgdnydYSPFVTLSS 445
Cdd:cd03684   252 ALITALiSFPNPYTR-LDMTE----LLELLFNECePGDDNSLCCYRDP------PAGDGV-----------YKALWSLLL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  446 FQVVYFFLAILASTLPVPSGIFMPVFVLGAAFGRLVGEGVFSLDPYGHisgDIQFF---------VRPGVYAVVGAAAFC 516
Cdd:cd03684   310 ALIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGILVEQLAYSYP---DSIFFacctagpscITPGLYAMVGAAAFL 386
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 922582198  517 GAVTH-TVSVAVIVFELTGQLCHLLPVMIAVLIANAVASYLQP-SIYDSIIRIKNLPYL 573
Cdd:cd03684   387 GGVTRmTVSLVVIMFELTGALNYILPLMIAVMVSKWVADAIGKeGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
140-554 5.04e-79

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: 261.71  E-value: 5.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   140 LLSAVCAHYIAPQAIGSGIPEMKTILRGVilKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHG 219
Cdd:pfam00654    3 LLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLFR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   220 SSggifENESRsgEMLAAGCAVGVACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILrmFSVSAAVTVE 299
Cdd:pfam00654   81 LS----PRDRR--ILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNSPLFSVG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   300 AHYQTNfppqnvflPQELPIFALIGLVCGLAGSIFVYLHRRtVLFLRRNWLakmifQKYWLIYPIFIATFISSLSfpLGL 379
Cdd:pfam00654  153 EPGSLS--------LLELPLFILLGILCGLLGALFNRLLLK-VQRLFRKLL-----KIPPVLRPALGGLLVGLLG--LLF 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   380 GKFMGGEErfsHTMKEFFVDCawtappndsyacpmptsnatssdsfdirhwkgdnydySPFVTLSSFQVVYFFLAILAST 459
Cdd:pfam00654  217 PEVLGGGY---ELIQLLFNGN-------------------------------------TSLSLLLLLLLLKFLATALSLG 256
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   460 LPVPSGIFMPVFVLGAAFGRLVGEGVFSLDPYGHISgdiqffvrPGVYAVVGAAAFCGAVTH-TVSVAVIVFELTGQLCH 538
Cdd:pfam00654  257 SGAPGGIFAPSLAIGAALGRAFGLLLALLFPIGGLP--------PGAFALVGMAAFLAAVTRaPLTAIVIVFELTGSLQL 328
                          410
                   ....*....|....*.
gi 922582198   539 LLPVMIAVLIANAVAS 554
Cdd:pfam00654  329 LLPLMLAVLIAYAVSR 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. ...
74-573 1.03e-75

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: 257.20  E-value: 1.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   74 KTFFRTVIRDWIFLALLGFIMASLSFGMDYAILNLQNGQMRL-FDLVKEYHFTLAYLVWVGYVVGLILLSAVCAHYIAPQ 152
Cdd:cd03685    23 KQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVvKNYIEKGRLFTAFLVYLGLNLVLVLVAALLVAYIAPT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  153 AIGSGIPEMKTILRGVILKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLtrlvhgSSGG--------- 223
Cdd:cd03685   103 AAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIAAGL------SQGGstslrldfr 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  224 ---IFENESRSGEMLAAGCAVGVACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILRMFSVSAA----- 295
Cdd:cd03685   177 wfrYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVTFTLNFFLSGCNSGKcglfg 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  296 ---------VTVEAHYQTnfppqnvflpQELPIFALIGLVCGLAGSIFVYLHRRtVLFLRRNWLAKMIFQKywLIYPIFI 366
Cdd:cd03685   257 pgglimfdgSSTKYLYTY----------FELIPFMLIGVIGGLLGALFNHLNHK-VTRFRKRINHKGKLLK--VLEALLV 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  367 ATFISSLSFPlglgkfmggeerfshtmkeffvdcawtappndsyacpmptsnatssdsfdirhwkgdnydyspfVTLSSF 446
Cdd:cd03685   324 SLVTSVVAFP----------------------------------------------------------------QTLLIF 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  447 QVVYFFLAILASTLPVPSGIFMPVFVLGAAFGRLVGEGVFSLDPYGHISgdiqffvrPGVYAVVGAAAFCGAVTH-TVSV 525
Cdd:cd03685   340 FVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSID--------PGLYALLGAAAFLGGVMRmTVSL 411
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 922582198  526 AVIVFELTGQLCHLLPVMIAVLIANAVASYLQPSIYDSIIRIKNLPYL 573
Cdd:cd03685   412 TVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
84-566 5.48e-56

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 199.98  E-value: 5.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   84 WIFLALL-GFIMASLSFGMDYAILNLQNgqMRLFDLVKEYHFTLAYLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPE-M 161
Cdd:COG0038     7 LLLLAVLvGILAGLAAVLFRLLLELATH--LFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQvI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  162 KTILRGvilKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHGSsggifENESRSgeMLAAGCAV 241
Cdd:COG0038    85 EAIHLK---GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLS-----PEDRRI--LLAAGAAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  242 GVACTFSAPIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILRMFsvsaavtvEAHYQtnFPPQNVFLPQELPIFA 321
Cdd:COG0038   155 GLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLLFGN--------GPLFG--VPSVPALSLLELPLYL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  322 LIGLVCGLAGSIFVylhrRTVLFLRRnWLAKMIFQKYWLIYPIFIATFISSLSFP--LGLGKfmggeerfsHTMKEFFvd 399
Cdd:COG0038   225 LLGILAGLVGVLFN----RLLLKVER-LFKRLKLPPWLRPAIGGLLVGLLGLFLPqvLGSGY---------GLIEALL-- 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  400 cawtappndsyacpmptsnatsSDSFDIrhwkgdnydyspfvtlsSFQVVYFFLAILASTLPV----PSGIFMPVFVLGA 475
Cdd:COG0038   289 ----------------------NGELSL-----------------LLLLLLLLLKLLATALTLgsggPGGIFAPSLFIGA 329
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  476 AFGRLVGEGVFSLDPYGHISgdiqffvrPGVYAVVGAAAFCGAVTHT-VSVAVIVFELTGQLCHLLPVMIAVLIANAVAS 554
Cdd:COG0038   330 LLGAAFGLLLNLLFPGLGLS--------PGLFALVGMAAVFAAVTRApLTAILLVLEMTGSYSLLLPLMIACVIAYLVSR 401
                         490
                  ....*....|...
gi 922582198  555 YLQP-SIYDSIIR 566
Cdd:COG0038   402 LLFPrSIYTAQLE 414
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
91-550 3.87e-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: 190.85  E-value: 3.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   91 GFIMASLSFGMDYAILNLQN-GQMRLFDLVKEYHFTLAYLVWVGYVVGLILLSAVcahYIAPQAIGSGIPE-MKTILRGv 168
Cdd:cd00400     1 GVLSGLGAVLFRLLIELLQNlLFGGLPGELAAGSLSPLYILLVPVIGGLLVGLLV---RLLGPARGHGIPEvIEAIALG- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  169 ilKEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHGSsggifENESRsgEMLAAGCAVGVACTFS 248
Cdd:cd00400    77 --GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLS-----RNDRR--ILVACGAAAGIAAAFN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  249 APIGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRILrmFSVSAAVTVeahyqtnfPPQNVFLPQELPIFALIGLVCG 328
Cdd:cd00400   148 APLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLL--FGAEPAFGV--------PLYDPLSLLELPLYLLLGLLAG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  329 LAGSIFVYLHRRTvlflrRNWLAKMIfqKYWLIYPIFIATFISSLSFPLGLGKFMGGEERFSHTMKEFfvdcawtappnd 408
Cdd:cd00400   218 LVGVLFVRLLYKI-----ERLFRRLP--IPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLALAGEL------------ 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  409 syacpmptsnatssdsfdirhwkgdnydysPFVTLSSFQVVYFFLAILASTLPVPSGIFMPVFVLGAAFGRLVGEGVFSL 488
Cdd:cd00400   279 ------------------------------SLLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPAL 328
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922582198  489 DPYGHISgdiqffvrPGVYAVVGAAAFCGAVTHT-VSVAVIVFELTGQLCHLLPVMIAVLIAN 550
Cdd:cd00400   329 FPGLVAS--------PGAYALVGMAALLAAVLRApLTAILLVLELTGDYSLLLPLMLAVVIAY 383
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
91-566 1.62e-49

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: 180.82  E-value: 1.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   91 GFIMASLSFGMDYAILNLQNGQMRLFDLVKeyHFTLAYLVWVGYVVGLILLSAVCAHYIAPQAIGSGIPEMKTILRGviL 170
Cdd:cd01031     2 GLLAGLVAVLFRLGIDKLGNLRLSLYDFAA--NNPPLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAG--L 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  171 KEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVASQLTRLVHGSSGgifenESRSgeMLAAGCAVGVACTFSAP 250
Cdd:cd01031    78 LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSKWFKTSPE-----ERRQ--LIAAGAAAGLAAAFNAP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  251 IGGVLFSIEVTSVYFAVRNYWRGFFAATCSATLFRIlrMFSVSAAVtveahyqtNFPPQNVFLPQELPIFALIGLVCGLA 330
Cdd:cd01031   151 LAGVLFVLEELRHSFSPLALLTALVASIAADFVSRL--FFGLGPVL--------SIPPLPALPLKSYWLLLLLGIIAGLL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  331 GSIFvylhRRTVLFLrRNWLAKM-IFQKYWLIYPIFIATFISSLSFPLGLGkfmGGEErfshtmkefFVDCAWTAPPnds 409
Cdd:cd01031   221 GYLF----NRSLLKS-QDLYRKLkKLPRELRVLLPGLLIGPLGLLLPEALG---GGHG---------LILSLAGGNF--- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  410 yacpmptsnatssdsfdirhwkgdnydysPFVTLSSFQVVYFFLAILASTLPVPSGIFMPVFVLGAAFGRLVGEGVFSLD 489
Cdd:cd01031   281 -----------------------------SISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLGLLFGTILVQLG 331
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582198  490 PYGHISgdiqffvrPGVYAVVGAAAFCGAVTHTVSVAVI-VFELTGQLCHLLPVMIAVLIANAVASYLQ-PSIYDSIIR 566
Cdd:cd01031   332 PIPISA--------PATFAIAGMAAFFAAVVRAPITAIIlVTEMTGNFNLLLPLMVVCLVAYLVADLLGgKPIYEALLE 402
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
88-566 6.17e-30

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 124.23  E-value: 6.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   88 ALLGFIMASLSFGMDYAILNLQNGQMRLFDLVKEYhftlAYLVWVGYvvglILLSAVCA-------HYIAPQAIGSGIPE 160
Cdd:PRK05277    5 AVVGTLTGLVGVAFELAVDWVQNQRLGLLASVADN----GLLLWIVA----FLISAVLAmigyflvRRFAPEAGGSGIPE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  161 MKTIL---RGVILKEYLSVrtllsKMIGLTLSLGSGLPMGKEGPFVHVASVVAsqltRLVhgssGGIFenESRSGE---- 233
Cdd:PRK05277   77 IEGALeglRPVRWWRVLPV-----KFFGGLGTLGSGMVLGREGPTVQMGGNIG----RMV----LDIF--RLRSDEarht 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  234 MLAAGCAVGVACTFSAPIGGVLFSIE---------VTSvYFAVrnywrgfFAATCSATLfrILRMFSVSAAVTVEAHYQt 304
Cdd:PRK05277  142 LLAAGAAAGLAAAFNAPLAGILFVIEemrpqfrysLIS-IKAV-------FIGVIMATI--VFRLFNGEQAVIEVGKFS- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  305 nFPPQNVflpqeLPIFALIGLVCGLAGSIFVYLHRRTV-LFLRRNWLAKmifQKYWLIYPIFIATFisslsfplGLGkfm 383
Cdd:PRK05277  211 -APPLNT-----LWLFLLLGIIFGIFGVLFNKLLLRTQdLFDRLHGGNK---KRWVLMGGAVGGLC--------GLL--- 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  384 ggeerfshtmkeffvdcAWTAPPndsyacpmptsnaTSSDSFDIRHWKGDNydYSPFVTLSSFQVVYFFLAILASTLPVP 463
Cdd:PRK05277  271 -----------------GLLAPA-------------AVGGGFNLIPIALAG--NFSIGMLLFIFVARFITTLLCFGSGAP 318
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  464 SGIFMPVFVLGAAFGRLVGEGVFSLDPyghisgdiQFFVRPGVYAVVGAAA-FCGAVTHTVSVAVIVFELTGQLCHLLPV 542
Cdd:PRK05277  319 GGIFAPMLALGTLLGLAFGMVAAALFP--------QYHIEPGTFAIAGMGAlFAATVRAPLTGIVLVLEMTDNYQLILPL 390
                         490       500
                  ....*....|....*....|....*.
gi 922582198  543 MIAVLIANAVASYL--QPsIYDSIIR 566
Cdd:PRK05277  391 IITCLGATLLAQFLggKP-IYSALLE 415
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
114-553 6.55e-28

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: 117.33  E-value: 6.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  114 RLFDLVKE--YHFTLAYLVWVGYVVGLIL-LSAVCAHYIAPQAIGSGIPEMKTILR---GVILKEYLSVRTLLSKMIGLT 187
Cdd:cd01034     9 KLADLALAlfQRLTATHPWLPLLLTPAGFaLIAWLTRRFFPGAAGSGIPQVIAALElpsAAARRRLLSLRTAVGKILLTL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  188 LSLGSGLPMGKEGPFVHVASVVASQLTRLVHGSSGGifenesRSGEMLAAGCAVGVACTFSAPIGGVLFSIEVTSvyfav 267
Cdd:cd01034    89 LGLLGGASVGREGPSVQIGAAVMLAIGRRLPKWGGL------SERGLILAGGAAGLAAAFNTPLAGIVFAIEELS----- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  268 rnywRGFFAATCSATLfrILRMFSVSAAVTVEAHYqTNF--PPQNVFLPQELPIFALIGLVCGLAGSIFVYLhrrtvLFL 345
Cdd:cd01034   158 ----RDFELRFSGLVL--LAVIAAGLVSLAVLGNY-PYFgvAAVALPLGEAWLLVLVCGVVGGLAGGLFARL-----LVA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  346 RRNWLAkMIFQKYWLIYPIFIAtFISSLSFpLGLGKFMGGeerfshtmKEFfvdcawtappNDSYACPMPTSNATSSDSF 425
Cdd:cd01034   226 LSSGLP-GWVRRFRRRRPVLFA-ALCGLAL-ALIGLVSGG--------LTF----------GTGYLQARAALEGGGGLPL 284
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  426 DIRHWKgdnydyspfvtlssfqvvyfFLAILASTLP-VPSGIFMPVFVLGAAFGRLVgegvfsldpyGHISGdiqfFVRP 504
Cdd:cd01034   285 WFGLLK--------------------FLATLLSYWSgIPGGLFAPSLAVGAGLGSLL----------AALLG----SVSQ 330
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 922582198  505 GVYAVVGAAAFCGAVTHT-VSVAVIVFELTGQLCHLLPVMIAVLIANAVA 553
Cdd:cd01034   331 GALVLLGMAAFLAGVTQApLTAFVIVMEMTGDQQMLLPLLAAALLASGVS 380
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
126-566 2.17e-21

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 99.82  E-value: 2.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  126 LAYLVWV----GYVVGLILLSAV-------CAHYIAPQAIGSG-IPEMKTILRgvilkeylSVRTLLSkmigltlsLGSG 193
Cdd:PRK01862   69 WYVRVWLpaagGFLAGCVLLLANrgarkggKTDYMEAVALGDGvVPVRQSLWR--------SASSLLT--------IGSG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  194 LPMGKEGPFVHVASVVASQLTRLVHGSSggifeneSRSGEMLAAGCAVGVACTFSAPIGGVLFSIEVTSVYFAVRNYWRG 273
Cdd:PRK01862  133 GSIGREGPMVQLAALAASLVGRFAHFDP-------PRLRLLVACGAAAGITSAYNAPIAGAFFVAEIVLGSIAMESFGPL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  274 FFAatcsatlfrilrmfSVSAAVTVEAH------YQTN-FPPQNvflPQELPIFALIGLVCGLAGSifvylhrrtvLFLR 346
Cdd:PRK01862  206 VVA--------------SVVANIVMREFagyqppYEMPvFPAVT---GWEVLLFVALGVLCGAAAP----------QFLR 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  347 RNWLAKMIFQKywliYPIfiatfisSLSFPLGLGKFMGGeerfshtmkeffVDCAWTappndsyacPMPTSNATSSDSfD 426
Cdd:PRK01862  259 LLDASKNQFKR----LPV-------PLPVRLALGGLLVG------------VISVWV---------PEVWGNGYSVVN-T 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  427 IRHwkgdnydySPFVTLSSFQVVYFFLAILASTL--PVPSGIFMPVFVLGAAFGRLVGEGVFSLDPyGHISGdiqffvrP 504
Cdd:PRK01862  306 ILH--------APWTWQALVAVLVAKLIATAATAgsGAVGGVFTPTLFVGAVVGSLFGLAMHALWP-GHTSA-------P 369
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582198  505 GVYAVVGAAAFCGAVTHTVSVAVI-VFELTGQLCHLLPVMIAVLIANAVASYLQP-SIYDSIIR 566
Cdd:PRK01862  370 FAYAMVGMGAFLAGATQAPLMAILmIFEMTLSYQVVLPLMVSCVVAYFTARALGTtSMYEITLR 433
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
814-868 7.14e-15

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: 71.78  E-value: 7.14e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922582198  814 DLSQLdIDSTPFQLSEYTSLFKAHSLFSLLGLNRAYVTKKGQLIGVVALKELRLA 868
Cdd:cd04591    61 DLRPI-MDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
587-642 1.75e-14

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: 70.63  E-value: 1.75e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 922582198  587 LIEQFMISPLVYIAKDSTVGDIKRALETkTRIRAFPLVENMESLALVGSVSRSQLQ 642
Cdd:cd04591     1 TAEDVMRPPLTVLARDETVGDIVSVLKT-TDHNGFPVVDSTESQTLVGFILRSQLI 55
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
191-552 3.87e-10

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: 63.08  E-value: 3.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  191 GSGLPMGKEGPFVHVASVVASQLTRLvhgssGGIFENESRSgeMLAAGCAVGVACTFSAPIGGVLFSIEVTSVYFAVRNY 270
Cdd:cd01033    97 GLGAPLGREVAPREVGALLAQRFSDW-----LGLTVADRRL--LVACAAGAGLAAVYNVPLAGALFALEILLRTISLRSV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  271 WRGFFAATCSAtlfrilrmfSVSAAVTVEAHYQTNFPPQnvFLPQELPIFALIGLVCGLAGSIFVYLHRRTVLFLRRNWl 350
Cdd:cd01033   170 VAALATSAIAA---------AVASLLKGDHPIYDIPPMQ--LSTPLLIWALLAGPVLGVVAAGFRRLSQAARAKRPKGK- 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  351 akmifqKYWLIYPI-FIATFISSLSFP--LGLGKfMGGEERFSHTMkeffvdcawtappndsyacpmptsnatssdsfdi 427
Cdd:cd01033   238 ------RILWQMPLaFLVIGLLSIFFPqiLGNGR-ALAQLAFSTTL---------------------------------- 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  428 rhwkgdnydyspFVTLSSFQVVyffLAILASTLPVPS----GIFMPVFVLGAAFGRLVGEGVFSLDPYGHISGdiqffvr 503
Cdd:cd01033   277 ------------TLSLLLILLV---LKIVATLLALRAgaygGLLTPSLALGALLGALLGIVWNALLPPLSIAA------- 334
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922582198  504 pgvYAVVGAAAFCGAVTHT-VSVAVIVFELTGQ-LCHLLPVMIAVLIANAV 552
Cdd:cd01033   335 ---FALIGAAAFLAATQKApLTALILVLEFTRQnPLFLIPLMLAVAGAVAV 382
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
453-561 9.08e-05

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 46.31  E-value: 9.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198  453 LAILASTLP-VPSGIFMPVFVLGAAFGRLVGEgVFSLDPYGhisGDIQffvrPGVYAVVGAAAFCGAVTHT-VSVAVIVF 530
Cdd:PRK01610  307 LAVLASSGSgAPGGVFTPTLFVGLAIGMLYGR-SLGLWLPD---GEEI----TLLLGLTGMATLLAATTHApIMSTLMIC 378
                          90       100       110
                  ....*....|....*....|....*....|...
gi 922582198  531 ELTGQLcHLLP-VMIAVLIANAVASYLQP-SIY 561
Cdd:PRK01610  379 EMTGEY-QLLPgLLIACVIASVISRTLRRdSIY 410
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
81-261 6.89e-04

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


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 42.92  E-value: 6.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198    81 IRDWIFLALLGFIMASLSFGMDYAILNLQNGQMRLFDLvkeyhftlaYLVWVGYVVGLILlsaVCAHYIAPQAIGSGIPE 160
Cdd:pfam00654  159 LLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLKI---------PPVLRPALGGLLV---GLLGLLFPEVLGGGYEL 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922582198   161 MKTILRGVILkEYLSVRTLLSKMIGLTLSLGSGLPMGKEGPFVHVASVVAsqltRLVhgssGGIFENESRSGEMLAAGCA 240
Cdd:pfam00654  227 IQLLFNGNTS-LSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALG----RAF----GLLLALLFPIGGLPPGAFA 297
                          170       180
                   ....*....|....*....|....*.
gi 922582198   241 -VGVACTFS----APIGGVLFSIEVT 261
Cdd:pfam00654  298 lVGMAAFLAavtrAPLTAIVIVFELT 323
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
586-664 1.47e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.85  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922582198  586 MLIEQFMISPLVYIAKDSTVGDIKRALETKtRIRAFPLVEnmESLALVGSVSRSQLQRYVDSQIGTKARFAEATRRIKQ 664
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREH-GIRGLPVVD--EDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVED 77
CBS COG0517
CBS domain [Signal transduction mechanisms];
584-648 2.07e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 39.46  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922582198  584 HQMLIEQFMISPLVYIAKDSTVGDIKRALEtKTRIRAFPLVEnmESLALVGSVSRSQLQRYVDSQ 648
Cdd:COG0517    65 LDTPVSEVMTRPPVTVSPDTSLEEAAELME-EHKIRRLPVVD--DDGRLVGIITIKDLLKALLEP 126
CBS COG0517
CBS domain [Signal transduction mechanisms];
586-648 4.09e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 38.31  E-value: 4.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922582198  586 MLIEQFMISPLVYIAKDSTVGDIKRALeTKTRIRAFPLV-ENMEslaLVGSVSRSQLQRYVDSQ 648
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELM-SEKRIGGLPVVdEDGK---LVGIVTDRDLRRALAAE 60
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
584-649 4.30e-03

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 38.27  E-value: 4.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922582198  584 HQMLIEQFMISPLVYIAKDSTVGDikrALE--TKTRIRAFPLVENMEslaLVGSVSRSQLQRYVDSQI 649
Cdd:COG2905    63 LDTPVSEVMTRPPITVSPDDSLAE---ALElmEEHRIRHLPVVDDGK---LVGIVSITDLLRALSEEL 124
 
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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