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Conserved domains on  [gi|1958688861|ref|XP_038950797|]
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H(+)/Cl(-) exchange transporter 3 isoform X2 [Rattus norvegicus]

Protein Classification

chloride channel protein( domain architecture ID 10132694)

ClC family voltage-gated chloride channel protein containing a C-terminal CBS pair domain, catalyzes the selective flow of Cl(-) ions across the cellular membrane

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
109-615 0e+00

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: 755.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 109 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 188
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 349 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 428
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 429 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGVGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418
                         490       500
                  ....*....|....*....|....*..
gi 1958688861 589 TSKWVGDAFGREGIYEAHIRLNGYPFL 615
Cdd:cd03684   419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
626-776 5.59e-44

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: 154.21  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 626 LAADVMRPrrsdpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegvvgssrv 705
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958688861 706 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEH 776
Cdd:cd04591    61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
109-615 0e+00

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: 755.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 109 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 188
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 349 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 428
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 429 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGVGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418
                         490       500
                  ....*....|....*....|....*..
gi 1958688861 589 TSKWVGDAFGREGIYEAHIRLNGYPFL 615
Cdd:cd03684   419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
194-595 7.72e-96

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  Cd Length: 344  Bit Score: 303.32  E-value: 7.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 194 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 273
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 274 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 353
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 354 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELF 433
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 434 TDCGPLessslcdyrndmnaskivddipdrpagvgvysaiWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 513
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 514 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 593
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342

                  ..
gi 1958688861 594 GD 595
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
187-613 2.13e-58

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


Pssm-ID: 223116 [Multi-domain]  Cd Length: 443  Bit Score: 206.03  E-value: 2.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 187 YIFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFIIRgyLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCC 265
Cdd:COG0038    66 LPLVPALGGLLVGAlLVYKFAPEARGSGIPQAIEALHGRKGR--ISPRVLPVKLVATLLTIGSGASLGREGPSVQIGAAI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 266 GNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEV-SYYFPLKTLWRSFFAALVAAFVLRSINPFGn 344
Cdd:COG0038   144 GSLLGRLLK---LSREDRRILLAAGAAAGLAAAFNAPLAGALFAIEVLyGRFLEYRALVPVLVAAVVALLVAGLFGGPH- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 345 srLVLFYVEYHTPWyLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGkyPVLEVIIVAAITAVIAFPNP-YTRL 423
Cdd:COG0038   220 --FLLPIVTTPHMS-LWDLLLYLVLGIIAGLFGVLLSRLLALSRRFFRRLPLP--PLLRPALGGLLVGALGLLFPeVLGN 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 424 NTSELIKELFTDCGPLessslcdyrndmnaskivddipdrpagvgvysaiwQLCLALIFKIIMTVFTFGIKVPSGLFIPS 503
Cdd:COG0038   295 GYGLIQLALAGEGGLL-----------------------------------VLLLLFLLKLLATLLSYGSGAPGGIFAPS 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 504 MAIGAIAGRIVGIAVEQLAyyhhdwfifkewcevGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPL 583
Cdd:COG0038   340 LFIGAALGLAFGALLGLLF---------------PPSILEPGLFALLGMAAFLAATTRAPLTAIVLVLEMTGNYQLLLPL 404
                         410       420       430
                  ....*....|....*....|....*....|
gi 1958688861 584 MAAVMTSKWVGDAFGREGIYEAHIRLNGYP 613
Cdd:COG0038   405 LIACLIAYLVSRLLGGRPIYTQLLARRGAP 434
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
626-776 5.59e-44

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: 154.21  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 626 LAADVMRPrrsdpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegvvgssrv 705
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958688861 706 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEH 776
Cdd:cd04591    61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
177-605 1.77e-27

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


Pssm-ID: 235385  Cd Length: 438  Bit Score: 116.53  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 177 PGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEG 256
Cdd:PRK05277   37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 257 PLVHVACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 334
Cdd:PRK05277  115 PTVQMGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 335 VLRSINpfGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTKFGKYpVLEVIIVAAIT 411
Cdd:PRK05277  193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLC 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 412 AVIAFPNPYTRLNTSELIKELFTdcgplessslcdyrndmnaskivddipdrpagvGVYSaIWQLCLALIFKIIMTVFTF 491
Cdd:PRK05277  268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNFS-IGMLLFIFVARFITTLLCF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 492 GIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVF 571
Cdd:PRK05277  314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVL 378
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1958688861 572 ELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:PRK05277  379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
732-778 1.76e-06

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 45.58  E-value: 1.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958688861  732 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGIVLGIITKKNILEHLE 778
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
724-778 4.38e-05

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: 41.82  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958688861 724 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGIVLGIITKKNILEHLE 778
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS COG0517
CBS domain [Signal transduction mechanisms];
629-774 2.78e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 223591 [Multi-domain]  Cd Length: 117  Bit Score: 41.30  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 629 DVMRPRRsdpplaVLTQDNMTVDDIENMINETSYNGFPVImskESQRLVGFALRRDLTIAIESARKkqegvvgssrvcfa 708
Cdd:COG0517     3 DIMTKDV------ITVKPDTSVRDALLLMSENGVSAVPVV---DDGKLVGIITERDILRALAAGGK-------------- 59
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958688861 709 qhtpslpaespRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKL-GLRQCLVTHNGI--VLGIITKKNIL 774
Cdd:COG0517    60 -----------RLLPVKEVMTKPVVTVDPDTPLEEALELMVERhKIRRLPVVDDDGgkLVGIITLSDIL 117
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
109-615 0e+00

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: 755.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 109 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 188
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 349 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 428
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 429 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGVGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418
                         490       500
                  ....*....|....*....|....*..
gi 1958688861 589 TSKWVGDAFGREGIYEAHIRLNGYPFL 615
Cdd:cd03684   419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
109-604 1.03e-152

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  Cd Length: 416  Bit Score: 453.72  E-value: 1.03e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 109 GLASGALAGLIDIAADWMTDLKEGICLSAlwynheqccwgsnettfeerdkcpqwktwaeliigqaegPGSYIMNYIMYI 188
Cdd:cd01036     1 GLLMGLVAVVLDYAVESSLDAGQWLLRRI---------------------------------------PGSYLLGYLMWV 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd01036    42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 269 FSYLFPKYS----------TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRS 338
Cdd:cd01036   122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 339 INPFGNSR----------LVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKF---GKYPVLEVI 405
Cdd:cd01036   202 YNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFrktARYRVLEPV 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 406 IVAAITAVIAFpnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagvgvysaIWQLCLALIFKII 485
Cdd:cd01036   282 LFTLIYSTIHY--------------------------------------------------------APTLLLFLLIYFW 305
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 486 MTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewCEVGADCITPGLYAMVGAAACLGGVTRMTVS 565
Cdd:cd01036   306 MSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRLTFS 378
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1958688861 566 LVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGrEGIYE 604
Cdd:cd01036   379 ICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
194-595 7.72e-96

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  Cd Length: 344  Bit Score: 303.32  E-value: 7.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 194 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 273
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 274 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 353
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 354 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELF 433
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 434 TDCGPLessslcdyrndmnaskivddipdrpagvgvysaiWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 513
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 514 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 593
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342

                  ..
gi 1958688861 594 GD 595
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. ...
102-615 2.57e-95

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  Cd Length: 466  Bit Score: 306.12  E-value: 2.57e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 102 WLVVTLTGLASGALAGLIDIAADWMTDLKegicLSALWYNHEQCCwgsnettfeerdkcpqwktwaeliigqaegpgsYI 181
Cdd:cd03685    33 WIICLLIGIFTGLVAYFIDLAVENLAGLK----FLVVKNYIEKGR---------------------------------LF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 182 MNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 261
Cdd:cd03685    76 TAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 262 ACCCGNIFS----------YLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALV 331
Cdd:cd03685   156 GACIAAGLSqggstslrldFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 332 AAFVLRSINPFGNSR---------LVLFYVeYHTP--WYLFELFPFILLGVFGGLWGAFFIRANIAWCR-RRKSTKFGK- 398
Cdd:cd03685   236 VTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRfRKRINHKGKl 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 399 YPVLEVIIVAAITAVIAFPnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagvgvysaiWQLCL 478
Cdd:cd03685   315 LKVLEALLVSLVTSVVAFP--------------------------------------------------------QTLLI 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 479 ALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQlayyhhdwFIFKEWcevgadcITPGLYAMVGAAACLGG 558
Cdd:cd03685   339 FFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGS--------YFGFTS-------IDPGLYALLGAAAFLGG 403
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958688861 559 VTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFgREGIYEAHIRLNGYPFL 615
Cdd:cd03685   404 VMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
178-615 1.11e-82

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  Cd Length: 426  Bit Score: 271.43  E-value: 1.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 178 GSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGP 257
Cdd:cd03683    39 GNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 258 LVHVACCCGNIFSYLFPKYS---TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAF 334
Cdd:cd03683   119 FVHISSIVAALLSKLTTFFSgiyENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAF 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 335 VLRSINPF---GNSRLVLFYVEYHT--PWYLFELFPFILLGVFGGLWGAFFIRAN--IAWCRRRK---STKFGKYPVLEV 404
Cdd:cd03683   199 TFRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHrkIVRFRRKNrlfSKFLKRSPLLYP 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 405 IIVAAITAVIAFPnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagvgvysaIWQLCLALIFKI 484
Cdd:cd03683   279 AIVALLTAVLTFP-------------------------------------------------------FLTLFLFIVVKF 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 485 IMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGiavEQLAYyhhdWFIFKEWcEVGADCITPGLYAMVGAAACLGGVTRmTV 564
Cdd:cd03683   304 VLTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAV----LFPEGIR-GGISNPIGPGGYAVVGAAAFSGAVTH-TV 374
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958688861 565 SLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGReGIYEAHIRLNGYPFL 615
Cdd:cd03683   375 SVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQP-SIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
109-590 2.80e-61

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  Cd Length: 383  Bit Score: 212.04  E-value: 2.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 109 GLASGALAGLIDIAADWMTDLKEGICLSALwynheqccwgsnettfeerdkcpqwktwaeliigqaeGPGSYImnyIMYI 188
Cdd:cd00400     1 GVLSGLGAVLFRLLIELLQNLLFGGLPGEL-------------------------------------AAGSLS---PLYI 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 189 FWALSFAFLAVSLVKVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGN 267
Cdd:cd00400    41 LLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGS 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 268 IFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNsrl 347
Cdd:cd00400   118 WLGRRLR---LSRNDRRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEP--- 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 348 vLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKstKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSE 427
Cdd:cd00400   192 -AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYG 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 428 LIKELFtdcgplessslcdyrndmnaskivddipdrpagVGVYSaIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIG 507
Cdd:cd00400   269 AILLAL---------------------------------AGELS-LLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIG 314
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 508 AIAGRIVGIAVEQLAYyhhdwfifkewcevgADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAV 587
Cdd:cd00400   315 AALGAAFGLLLPALFP---------------GLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLMLAV 379

                  ...
gi 1958688861 588 MTS 590
Cdd:cd00400   380 VIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
187-613 2.13e-58

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


Pssm-ID: 223116 [Multi-domain]  Cd Length: 443  Bit Score: 206.03  E-value: 2.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 187 YIFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFIIRgyLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCC 265
Cdd:COG0038    66 LPLVPALGGLLVGAlLVYKFAPEARGSGIPQAIEALHGRKGR--ISPRVLPVKLVATLLTIGSGASLGREGPSVQIGAAI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 266 GNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEV-SYYFPLKTLWRSFFAALVAAFVLRSINPFGn 344
Cdd:COG0038   144 GSLLGRLLK---LSREDRRILLAAGAAAGLAAAFNAPLAGALFAIEVLyGRFLEYRALVPVLVAAVVALLVAGLFGGPH- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 345 srLVLFYVEYHTPWyLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGkyPVLEVIIVAAITAVIAFPNP-YTRL 423
Cdd:COG0038   220 --FLLPIVTTPHMS-LWDLLLYLVLGIIAGLFGVLLSRLLALSRRFFRRLPLP--PLLRPALGGLLVGALGLLFPeVLGN 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 424 NTSELIKELFTDCGPLessslcdyrndmnaskivddipdrpagvgvysaiwQLCLALIFKIIMTVFTFGIKVPSGLFIPS 503
Cdd:COG0038   295 GYGLIQLALAGEGGLL-----------------------------------VLLLLFLLKLLATLLSYGSGAPGGIFAPS 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 504 MAIGAIAGRIVGIAVEQLAyyhhdwfifkewcevGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPL 583
Cdd:COG0038   340 LFIGAALGLAFGALLGLLF---------------PPSILEPGLFALLGMAAFLAATTRAPLTAIVLVLEMTGNYQLLLPL 404
                         410       420       430
                  ....*....|....*....|....*....|
gi 1958688861 584 MAAVMTSKWVGDAFGREGIYEAHIRLNGYP 613
Cdd:COG0038   405 LIACLIAYLVSRLLGGRPIYTQLLARRGAP 434
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
184-605 1.11e-51

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  Cd Length: 402  Bit Score: 185.82  E-value: 1.11e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 184 YIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVAC 263
Cdd:cd01031    37 LLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 264 CCGNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFG 343
Cdd:cd01031   115 AIGQGVSKWFK---TSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 344 nsrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIA---WCRRRKSTKfgkyPVLEVIIVAAITAVIAFPNPY 420
Cdd:cd01031   192 ----PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKsqdLYRKLKKLP----RELRVLLPGLLIGPLGLLLPE 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 421 TRLNTSELIKELFTdcGPLessslcdyrndmnaskivddipdrpagvgvysAIWQLCLALIFKIIMTVFTFGIKVPSGLF 500
Cdd:cd01031   264 ALGGGHGLILSLAG--GNF--------------------------------SISLLLLIFVLRFIFTMLSYGSGAPGGIF 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 501 IPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewcevgadciTPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYI 580
Cdd:cd01031   310 APMLALGALLGLLFGTILVQLGPIPIS---------------APATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLL 374
                         410       420
                  ....*....|....*....|....*
gi 1958688861 581 VPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:cd01031   375 LPLMVVCLVAYLVADLLGGKPIYEA 399
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
626-776 5.59e-44

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: 154.21  E-value: 5.59e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 626 LAADVMRPrrsdpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegvvgssrv 705
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958688861 706 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEH 776
Cdd:cd04591    61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
187-603 2.28e-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  Cd Length: 390  Bit Score: 118.10  E-value: 2.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 187 YIFWALSFA--FLAVSLVKVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 261
Cdd:cd01034    27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 262 ACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFVLR 337
Cdd:cd01034   107 GAAVMLAIGRRLPKWGGLSE--RGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 338 SINPFGNSRLVLfyveyhTPWYLfeLFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFG---KYPVLEVIIVAAITAVI 414
Cdd:cd01034   185 NYPYFGVAAVAL------PLGEA--WLLVLVCGVVGGLAGGLFARLLVALSSGLPGWVRRfrrRRPVLFAALCGLALALI 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 415 AFPNPYTRLNTSELIkelftdcgplessslcdyrndmnaskivddipDRPAGVGVYSAIWQLCLAlifKIIMTVFTFGIK 494
Cdd:cd01034   257 GLVSGGLTFGTGYLQ--------------------------------ARAALEGGGGLPLWFGLL---KFLATLLSYWSG 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 495 VPSGLFIPSMAIGAiagrIVGIAVEQLAYYHHdwfifkewcevgadcitPGLYAMVGAAACLGGVTRMTVSLVVIVFELT 574
Cdd:cd01034   302 IPGGLFAPSLAVGA----GLGSLLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVMEMT 360
                         410       420
                  ....*....|....*....|....*....
gi 1958688861 575 GGLEYIVPLMAAVMTSKWVGDAFGREGIY 603
Cdd:cd01034   361 GDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
177-605 1.77e-27

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


Pssm-ID: 235385  Cd Length: 438  Bit Score: 116.53  E-value: 1.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 177 PGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEG 256
Cdd:PRK05277   37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 257 PLVHVACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 334
Cdd:PRK05277  115 PTVQMGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 335 VLRSINpfGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTKFGKYpVLEVIIVAAIT 411
Cdd:PRK05277  193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLC 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 412 AVIAFPNPYTRLNTSELIKELFTdcgplessslcdyrndmnaskivddipdrpagvGVYSaIWQLCLALIFKIIMTVFTF 491
Cdd:PRK05277  268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNFS-IGMLLFIFVARFITTLLCF 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 492 GIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVF 571
Cdd:PRK05277  314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVL 378
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1958688861 572 ELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:PRK05277  379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
236-686 2.06e-19

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 92.89  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 236 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYL--FPKystneAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEV 313
Cdd:PRK01862  119 LWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFahFDP-----PRLRLLVACGAAAGITSAYNAPIAGAFFVAEIV 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 314 SYYFPLKTLWRSFFAALVAAFVLRSinpFGNSRlVLFYVEYH---TPWylfELFPFILLGVFGGLWGAFFIRAniawcRR 390
Cdd:PRK01862  194 LGSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRL-----LD 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 391 RKSTKFGKYPVLEVIIVA---AITAVIAFPNPYTRLNTSELIKELftdcgpLESSSLcdyrndmnaskivddipdrpagv 467
Cdd:PRK01862  262 ASKNQFKRLPVPLPVRLAlggLLVGVISVWVPEVWGNGYSVVNTI------LHAPWT----------------------- 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 468 gvysaiWQ-LCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfifkeWCEVGADcitPGL 546
Cdd:PRK01862  313 ------WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHAL------------WPGHTSA---PFA 371
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 547 YAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNgypflDAKEEFTH--T 624
Cdd:PRK01862  372 YAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLRRH-----QDEAERERlrT 446
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958688861 625 TLAADVMRPRRSDPPLavltqdNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLT 686
Cdd:PRK01862  447 TQMRELIQPAQTVVPP------TASVADMTRVFLEYPVKYLYVV--DDDGRFRGAVALKDIT 500
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
233-590 5.50e-13

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  Cd Length: 388  Bit Score: 71.56  E-value: 5.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 233 WTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkySTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE- 311
Cdd:cd01033    83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWL---GLTVADRRLLVACAAGAGLAAVYNVPLAGALFALEi 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 312 ---EVSyyfplktlWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLfeLFPF-ILLGVFGGLWGAFFIRANiAW 387
Cdd:cd01033   160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTP--LLIWaLLAGPVLGVVAAGFRRLS-QA 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 388 CRRRKSTkfGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDcgplessslcdyrndmnaskivddipdrpaGV 467
Cdd:cd01033   229 ARAKRPK--GKRILWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFST------------------------------TL 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 468 GVYSAIWQLCLalifKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIaveqlaYYHHDWFIfkewcevgadcITPGLY 547
Cdd:cd01033   277 TLSLLLILLVL----KIVATLLALRAGAYGGLLTPSLALGALLGALLGI------VWNALLPP-----------LSIAAF 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1958688861 548 AMVGAAACLGGVTRMTVSLVVIVFELTG-GLEYIVPLMAAVMTS 590
Cdd:cd01033   336 ALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
646-774 3.44e-07

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).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 49.55  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 646 DNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKkqegvvgssrvcfaqhtpslpaesPRPLKLR 725
Cdd:cd02205     9 PDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRALVEGGL------------------------ALDTPVA 62
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958688861 726 SILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGIVLGIITKKNIL 774
Cdd:cd02205    63 EVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDIL 112
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
732-778 1.76e-06

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 45.58  E-value: 1.76e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958688861  732 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGIVLGIITKKNILEHLE 778
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
724-778 4.38e-05

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: 41.82  E-value: 4.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958688861 724 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGIVLGIITKKNILEHLE 778
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
647-775 5.12e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. 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: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 43.25  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 647 NMTVDDIENMINETSYNGFPVImskESQRLVGFALRRDltiaIESARKKQEGvvgssrvcfaqHTPslpaesprplkLRS 726
Cdd:cd04595    10 DTTIEEARKIMLRYGHTGLPVV---EDGKLVGIISRRD----VDKAKHHGLG-----------HAP-----------VKG 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958688861 727 ILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILE 775
Cdd:cd04595    61 YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLR 109
CBS COG0517
CBS domain [Signal transduction mechanisms];
629-774 2.78e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 223591 [Multi-domain]  Cd Length: 117  Bit Score: 41.30  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 629 DVMRPRRsdpplaVLTQDNMTVDDIENMINETSYNGFPVImskESQRLVGFALRRDLTIAIESARKkqegvvgssrvcfa 708
Cdd:COG0517     3 DIMTKDV------ITVKPDTSVRDALLLMSENGVSAVPVV---DDGKLVGIITERDILRALAAGGK-------------- 59
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958688861 709 qhtpslpaespRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKL-GLRQCLVTHNGI--VLGIITKKNIL 774
Cdd:COG0517    60 -----------RLLPVKEVMTKPVVTVDPDTPLEEALELMVERhKIRRLPVVDDDGgkLVGIITLSDIL 117
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
629-774 3.28e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. 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: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 41.01  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 629 DVMRPR-RSDPPlavltqdNMTVDDIENMINETSYNGFPVImskESQRLVGFalrrdltIAIESARKKQEGVVGSSRVcf 707
Cdd:cd04801     1 DIMTPEvVTVTP-------EMTVSELLDRMFEEKHLGYPVV---ENGRLVGI-------VTLEDIRKVPEVEREATRV-- 61
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 708 aqhtpslpaesprplklRSILDMSPFTVTDHTPmeiVVDIFRKL---GLRQCLVTHNGIVLGIITKKNIL 774
Cdd:cd04801    62 -----------------RDVMTKDVITVSPDAD---AMEALKLMsqnNIGRLPVVEDGELVGIISRTDLM 111
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
236-606 1.15e-03

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 42.07  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 236 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSY 315
Cdd:PRK01610  101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF----TPRQEWKLWIACGAAAGMASAYHAPLAGSLFIAEILFG 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 316 YFPLKTLWRSFFAALVAAFVLRSINPfgnSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTK 395
Cdd:PRK01610  177 TLMLASLGPVVISAVVALLTTNLLNG---SDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLLLTLMNASHRGFVSLK 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 396 FGkyPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDcgplessslcdyrndmnaskivddipdrPAGVGVYSAIwq 475
Cdd:PRK01610  254 LA--PPWQLALGGLIVGLLSLFTPAVWGNGYSVVQSFLTA----------------------------PPLLMLIAGI-- 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 476 lclaLIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIaveqlayyhhdwfIFKEWCEVGADciTPGLYAMVGAAAC 555
Cdd:PRK01610  302 ----FLCKLLAVLASSGSGAPGGVFTPTLFVGLAIGMLYGR-------------SLGLWLPDGEE--ITLLLGLTGMATL 362
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958688861 556 LGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAH 606
Cdd:PRK01610  363 LAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLRRDSIYRQH 413
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
249-416 1.22e-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  Cd Length: 378  Bit Score: 42.18  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 249 GLSLGKEGPLVHVAcccGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlkt 321
Cdd:cd03682    92 GGSAGREGTAVQMG---GSLADAFGRVFKLPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP--- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958688861 322 lwrSFFAALVAAFVLRSINPFGNSRLVLFYVEYhTPWYLFELfpfILLGVFGGLWGAFFIRAnIAWCrRRKSTKFGKYPV 401
Cdd:cd03682   166 ---CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNPY 236
                         170
                  ....*....|....*
gi 1958688861 402 LEVIIVAAITAVIAF 416
Cdd:cd03682   237 LRPFVGGLLIILLVY 251
CBS COG0517
CBS domain [Signal transduction mechanisms];
725-777 1.68e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 223591 [Multi-domain]  Cd Length: 117  Bit Score: 38.99  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958688861 725 RSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEHL 777
Cdd:COG0517     2 KDIMTKDVITVKPDTSVRDALLLMSENGVSAVPVVDDGKLVGIITERDILRAL 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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