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Conserved domains on  [gi|1890274570|ref|NP_001230303|]
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H(+)/Cl(-) exchange transporter 3 isoform c [Homo sapiens]

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|GO:0055085
PubMed:  11182894|9207144|9046241
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: 748.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 109 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 188
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 349 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 428
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 429 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                         490       500
                  ....*....|....*....|....*..
gi 1890274570 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 4.85e-47

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: 162.69  E-value: 4.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 626 LAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegivgssrv 705
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890274570 706 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 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: 748.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 109 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 188
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 349 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 428
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 429 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                         490       500
                  ....*....|....*....|....*..
gi 1890274570 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 1.42e-94

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: 298.69  E-value: 1.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 194 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 273
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 274 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 353
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 354 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELF 433
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 434 TDCGPLessslcdyrndmnaskivddipdrpagigvysaiWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 513
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 514 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 593
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 1890274570 594 GD 595
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
187-608 8.15e-55

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 194.59  E-value: 8.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 187 YIFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCC 265
Cdd:COG0038    52 LVLLLPPLGGLLVGlLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 266 GNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNS 345
Cdd:COG0038   130 GSLLGRLLR---LSPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL--FGNG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 346 rlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRAnIAWCRRRkSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNT 425
Cdd:COG0038   205 --PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSG 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 426 SELIKELFTdcGPLessslcdyrndmnaskivddipdrpagigvysAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMA 505
Cdd:COG0038   281 YGLIEALLN--GEL--------------------------------SLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLF 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 506 IGAIAGRIVGIAVEQLayyhhdwfifkewceVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMA 585
Cdd:COG0038   327 IGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLMI 391

                         410       420
                  ....*....|....*....|...
gi 1890274570 586 AVMTSKWVGDAFGREGIYEAHIR 608
Cdd:COG0038   392 ACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 626-776 4.85e-47

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: 162.69  E-value: 4.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 626 LAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegivgssrv 705
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890274570 706 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 776
Cdd:cd04591    61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
177-605 4.39e-27

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 114.99  E-value: 4.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 177 PGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEG 256
Cdd:PRK05277   37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 257 PLVHVACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 334
Cdd:PRK05277  115 PTVQMGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 335 VLRSINpfGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTKFGKYpVLEVIIVAAIT 411
Cdd:PRK05277  193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLC 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 412 AVIAFPNPYTRLNTSELIKELFTdcgplessslcdyrndmnaskivddipdrpagiGVYSaIWQLCLALIFKIIMTVFTF 491
Cdd:PRK05277  268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNFS-IGMLLFIFVARFITTLLCF 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 492 GIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVF 571
Cdd:PRK05277  314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVL 378

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1890274570 572 ELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:PRK05277  379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
626-782 2.65e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 73.36  E-value: 2.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 626 LAADVMrprrnDPPLAVLTQDnMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKKQegivgssrv 705
Cdd:COG3448     3 TVRDIM-----TRDVVTVSPD-TTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE--------- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890274570 706 cfaqhtpslPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQTAN 782
Cdd:COG3448    66 ---------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 732-775 4.13e-09

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: 52.90  E-value: 4.13e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1890274570  732 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILR 775
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIK 46
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 724-778 1.85e-07

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: 48.36  E-value: 1.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1890274570 724 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 778
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 730-773 6.43e-05

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 46.12  E-value: 6.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1890274570 730 MSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDI 773
Cdd:PTZ00314  104 MDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
 
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: 748.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 109 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 188
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 349 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 428
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 429 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                         490       500
                  ....*....|....*....|....*..
gi 1890274570 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 2.96e-151

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: 448.33  E-value: 2.96e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 109 GLASGALAGLIDIAADWMTDLKEGICLSAlwynheqccwgsnettfeerdkcpqwktwaeliigqaegPGSYIMNYIMYI 188
Cdd:cd01036     1 GLLMGLVAVVLDYAVESSLDAGQWLLRRI---------------------------------------PGSYLLGYLMWV 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 189 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd01036    42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 269 FSYLFPKYS----------TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRS 338
Cdd:cd01036   122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 339 INPFGNSR----------LVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKF---GKYPVLEVI 405
Cdd:cd01036   202 YNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFrktARYRVLEPV 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 406 IVAAITAVIAFpnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagigvysaIWQLCLALIFKII 485
Cdd:cd01036   282 LFTLIYSTIHY--------------------------------------------------------APTLLLFLLIYFW 305

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 486 MTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewCEVGADCITPGLYAMVGAAACLGGVTRMTVS 565
Cdd:cd01036   306 MSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRLTFS 378

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1890274570 566 LVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGrEGIYE 604
Cdd:cd01036   379 ICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
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 8.05e-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 [Multi-domain]  Cd Length: 466  Bit Score: 303.81  E-value: 8.05e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 102 WLVVTLTGLASGALAGLIDIAADWMTDLKegicLSALWYNHEQCCwgsnettfeerdkcpqwktwaeliigqaegpgsYI 181
Cdd:cd03685    33 WIICLLIGIFTGLVAYFIDLAVENLAGLK----FLVVKNYIEKGR---------------------------------LF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 182 MNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 261
Cdd:cd03685    76 TAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 262 ACCCGNIFS----------YLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALV 331
Cdd:cd03685   156 GACIAAGLSqggstslrldFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 332 AAFVLRSINPFGNSR---------LVLFYVeYHTP--WYLFELFPFILLGVFGGLWGAFFIRANIAWCR-RRKSTKFGK- 398
Cdd:cd03685   236 VTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRfRKRINHKGKl 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 399 YPVLEVIIVAAITAVIAFPnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagigvysaiWQLCL 478
Cdd:cd03685   315 LKVLEALLVSLVTSVVAFP--------------------------------------------------------QTLLI 338

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 479 ALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQlayyhhdwFIFKEWcevgadcITPGLYAMVGAAACLGG 558
Cdd:cd03685   339 FFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGS--------YFGFTS-------IDPGLYALLGAAAFLGG 403

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1890274570 559 VTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFgREGIYEAHIRLNGYPFL 615
Cdd:cd03685   404 VMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 194-595 1.42e-94

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: 298.69  E-value: 1.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 194 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 273
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 274 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 353
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 354 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELF 433
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 434 TDCGPLessslcdyrndmnaskivddipdrpagigvysaiWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 513
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 514 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 593
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 1890274570 594 GD 595
Cdd:pfam00654 343 SR 344
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 3.97e-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 [Multi-domain]  Cd Length: 426  Bit Score: 269.12  E-value: 3.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 178 GSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGP 257
Cdd:cd03683    39 GNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 258 LVHVACCCGNIFSYLFPKYS---TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAF 334
Cdd:cd03683   119 FVHISSIVAALLSKLTTFFSgiyENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAF 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 335 VLRSINPF---GNSRLVLFYVEYHT--PWYLFELFPFILLGVFGGLWGAFFIRAN--IAWCRRRK---STKFGKYPVLEV 404
Cdd:cd03683   199 TFRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHrkIVRFRRKNrlfSKFLKRSPLLYP 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 405 IIVAAITAVIAFPnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagigvysaIWQLCLALIFKI 484
Cdd:cd03683   279 AIVALLTAVLTFP-------------------------------------------------------FLTLFLFIVVKF 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 485 IMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGiavEQLAYyhhdWFIFKEWcEVGADCITPGLYAMVGAAACLGGVTRmTV 564
Cdd:cd03683   304 VLTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAV----LFPEGIR-GGISNPIGPGGYAVVGAAAFSGAVTH-TV 374

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890274570 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 3.33e-60

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: 208.57  E-value: 3.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 109 GLASGALAGLIDIAADWMTDLKEGICLSALwynheqccwgsnettfeerdkcpqwktwaeliigqaeGPGSYImnyIMYI 188
Cdd:cd00400     1 GVLSGLGAVLFRLLIELLQNLLFGGLPGEL-------------------------------------AAGSLS---PLYI 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 189 FWALSFAFLAVSLVKVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGN 267
Cdd:cd00400    41 LLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGS 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 268 IFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNsrl 347
Cdd:cd00400   118 WLGRRLR---LSRNDRRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEP--- 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 348 vLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKstKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSE 427
Cdd:cd00400   192 -AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYG 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 428 LIkelftdcgplessslcdyrndmnaskivddipdrPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIG 507
Cdd:cd00400   269 AI----------------------------------LLALAGELSLLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIG 314

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 508 AIAGRIVGIAVEQLAYyhhdwfifkewcevgADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAV 587
Cdd:cd00400   315 AALGAAFGLLLPALFP---------------GLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLMLAV 379


                  ...
gi 1890274570 588 MTS 590
Cdd:cd00400   380 VIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
187-608 8.15e-55

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 194.59  E-value: 8.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 187 YIFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCC 265
Cdd:COG0038    52 LVLLLPPLGGLLVGlLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAI 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 266 GNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNS 345
Cdd:COG0038   130 GSLLGRLLR---LSPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL--FGNG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 346 rlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRAnIAWCRRRkSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNT 425
Cdd:COG0038   205 --PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSG 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 426 SELIKELFTdcGPLessslcdyrndmnaskivddipdrpagigvysAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMA 505
Cdd:COG0038   281 YGLIEALLN--GEL--------------------------------SLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLF 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 506 IGAIAGRIVGIAVEQLayyhhdwfifkewceVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMA 585
Cdd:COG0038   327 IGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLMI 391

                         410       420
                  ....*....|....*....|...
gi 1890274570 586 AVMTSKWVGDAFGREGIYEAHIR 608
Cdd:COG0038   392 ACVIAYLVSRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 184-605 2.89e-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 [Multi-domain]  Cd Length: 402  Bit Score: 184.28  E-value: 2.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 184 YIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVAC 263
Cdd:cd01031    37 LLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 264 CCGNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFG 343
Cdd:cd01031   115 AIGQGVSKWFK---TSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 344 nsrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIA---WCRRRKSTKfgkyPVLEVIIVAAITAVIAFPNPY 420
Cdd:cd01031   192 ----PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKsqdLYRKLKKLP----RELRVLLPGLLIGPLGLLLPE 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 421 TRLNTSELIKELFTdcGPLessslcdyrndmnaskivddipdrpagigvysAIWQLCLALIFKIIMTVFTFGIKVPSGLF 500
Cdd:cd01031   264 ALGGGHGLILSLAG--GNF--------------------------------SISLLLLIFVLRFIFTMLSYGSGAPGGIF 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 501 IPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewcevgadciTPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYI 580
Cdd:cd01031   310 APMLALGALLGLLFGTILVQLGPIPIS---------------APATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLL 374

                         410       420
                  ....*....|....*....|....*
gi 1890274570 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 4.85e-47

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: 162.69  E-value: 4.85e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 626 LAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegivgssrv 705
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890274570 706 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 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 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: 116.56  E-value: 6.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 187 YIFWALSFAFLAVS--LVKVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 261
Cdd:cd01034    27 WLPLLLTPAGFALIawLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 262 ACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFVLR 337
Cdd:cd01034   107 GAAVMLAIGRRLPKWGGLSE--RGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 338 SINPFGNSRLVLfyveyhTPWYLfeLFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFG---KYPVLEVIIVAAITAVI 414
Cdd:cd01034   185 NYPYFGVAAVAL------PLGEA--WLLVLVCGVVGGLAGGLFARLLVALSSGLPGWVRRfrrRRPVLFAALCGLALALI 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 415 AFPNPYTRLNTSELIkelftdcgplessslcdyrndmnaskivddipDRPAGIGVYSAIWQLCLAlifKIIMTVFTFGIK 494
Cdd:cd01034   257 GLVSGGLTFGTGYLQ--------------------------------ARAALEGGGGLPLWFGLL---KFLATLLSYWSG 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 495 VPSGLFIPSMAIGAiagrIVGIAVEQLAYYHHdwfifkewcevgadcitPGLYAMVGAAACLGGVTRMTVSLVVIVFELT 574
Cdd:cd01034   302 IPGGLFAPSLAVGA----GLGSLLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVMEMT 360

                         410       420
                  ....*....|....*....|....*....
gi 1890274570 575 GGLEYIVPLMAAVMTSKWVGDAFGREGIY 603
Cdd:cd01034   361 GDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
177-605 4.39e-27

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 114.99  E-value: 4.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 177 PGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEG 256
Cdd:PRK05277   37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 257 PLVHVACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 334
Cdd:PRK05277  115 PTVQMGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 335 VLRSINpfGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTKFGKYpVLEVIIVAAIT 411
Cdd:PRK05277  193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLC 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 412 AVIAFPNPYTRLNTSELIKELFTdcgplessslcdyrndmnaskivddipdrpagiGVYSaIWQLCLALIFKIIMTVFTF 491
Cdd:PRK05277  268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNFS-IGMLLFIFVARFITTLLCF 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 492 GIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVF 571
Cdd:PRK05277  314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVL 378

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1890274570 572 ELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:PRK05277  379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
236-686 3.93e-19

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 91.73  E-value: 3.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 236 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYL--FPKystneAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEV 313
Cdd:PRK01862  119 LWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFahFDP-----PRLRLLVACGAAAGITSAYNAPIAGAFFVAEIV 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 314 SYYFPLKTLWRSFFAALVAAFVLRSinpFGNSRlVLFYVEYH---TPWylfELFPFILLGVFGGLWGAFFIRAniawcRR 390
Cdd:PRK01862  194 LGSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRL-----LD 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 391 RKSTKFGKYPVLEVIIVA---AITAVIAFPNPYTRLNTSELIKELftdcgpLESSSLcdyrndmnaskivddipdrpagi 467
Cdd:PRK01862  262 ASKNQFKRLPVPLPVRLAlggLLVGVISVWVPEVWGNGYSVVNTI------LHAPWT----------------------- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 468 gvysaiWQ-LCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfifkeWCEVGADcitPGL 546
Cdd:PRK01862  313 ------WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHAL------------WPGHTSA---PFA 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 547 YAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNgypflDAKEEFTH--T 624
Cdd:PRK01862  372 YAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLRRH-----QDEAERERlrT 446

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890274570 625 TLAADVMRPRrndpplAVLTQDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLT 686
Cdd:PRK01862  447 TQMRELIQPA------QTVVPPTASVADMTRVFLEYPVKYLYVV--DDDGRFRGAVALKDIT 500
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
626-782 2.65e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 73.36  E-value: 2.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 626 LAADVMrprrnDPPLAVLTQDnMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKKQegivgssrv 705
Cdd:COG3448     3 TVRDIM-----TRDVVTVSPD-TTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE--------- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890274570 706 cfaqhtpslPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQTAN 782
Cdd:COG3448    66 ---------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
542-777 1.25e-14

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 73.38  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 542 ITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGdAFGREGIYEAHIRLNGYPFLDAKEEF 621
Cdd:COG2524     4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 622 THTTLAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVImskESQRLVGFALRRDLTIAIESARKKQEgivg 701
Cdd:COG2524    83 VLKMKVKDIMTK-----DVITVSPD-TTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890274570 702 ssrvcfaqhtpslpaesprpLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHM 777
Cdd:COG2524   150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
620-779 6.86e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 66.47  E-value: 6.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 620 EFTHTTLAADVMRprRNDPplAVLTqDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLtiaiesarkkqegi 699
Cdd:COG4109    11 TFKEILLVEDIMT--LEDV--ATLS-EDDTVEDALELLEKTGHSRFPVV--DENGRLVGIVTSKDI-------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 700 vgssrvcfaqhtpslpAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 778
Cdd:COG4109    70 ----------------LGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKALQ 133


                  .
gi 1890274570 779 Q 779
Cdd:COG4109   134 K 134
CBS COG0517
CBS domain [Signal transduction mechanisms];
626-779 1.00e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 65.66  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 626 LAADVMRPrrnDPPLAvltQDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESarkkqegivgssrv 705
Cdd:COG0517     2 KVKDIMTT---DVVTV---SPDATVREALELMSEKRIGGLPVV--DEDGKLVGIVTDRDLRRALAA-------------- 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890274570 706 cfaqhtpslPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLV-THNGRLLGIITKKDILRHMAQ 779
Cdd:COG0517    60 ---------EGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 233-590 1.13e-12

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: 70.40  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 233 WTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkySTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE- 311
Cdd:cd01033    83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWL---GLTVADRRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 312 ---EVSyyfplktlWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLfeLFPF-ILLGVFGGLWGAFFIRANiAW 387
Cdd:cd01033   160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTP--LLIWaLLAGPVLGVVAAGFRRLS-QA 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 388 CRRRKSTkfGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDcgplessslcdyrndmnaskivddipdrpaGI 467
Cdd:cd01033   229 ARAKRPK--GKRILWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFST------------------------------TL 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 468 GVYSAIWQLCLalifKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIaveqlaYYHHDWFIfkewcevgadcITPGLY 547
Cdd:cd01033   277 TLSLLLILLVL----KIVATLLALRAGAYGGLLTPSLALGALLGALLGI------VWNALLPP-----------LSIAAF 335

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1890274570 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 ...
 646-775 3.15e-10

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: 58.02  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 646 DNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKkqegivgssrvcfaqhtpslpaesPRPLKLR 725
Cdd:cd02205     9 PDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRALVEGGL------------------------ALDTPVA 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890274570 726 SILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILR 775
Cdd:cd02205    63 EVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 627-779 3.19e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 55.61  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 627 AADVMRprrnDPPLAVltQDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKkqegivgssrvc 706
Cdd:COG2905     1 VKDIMS----RDVVTV--SPDATVREAARLMTEKGVGSLVVV--DDDGRLVGIITDRDLRRRVLAEGL------------ 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890274570 707 faqhtpslpaeSPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQ 779
Cdd:COG2905    61 -----------DPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSE 122
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 732-775 4.13e-09

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: 52.90  E-value: 4.13e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1890274570  732 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILR 775
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
722-778 5.28e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 52.18  E-value: 5.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890274570 722 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHMA 778
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVdEDGKLVGIVTDRDLRRALA 58
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 724-778 1.85e-07

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: 48.36  E-value: 1.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1890274570 724 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 778
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 629-775 2.55e-07

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: 49.87  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 629 DVMRPRrndpplAVLTQDNMTVDDIENMINETSYNGFPVImskESQRLVGFalrrdltIAIESARKKQEGIVGSSRVcfa 708
Cdd:cd04801     1 DIMTPE------VVTVTPEMTVSELLDRMFEEKHLGYPVV---ENGRLVGI-------VTLEDIRKVPEVEREATRV--- 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 709 qhtpslpaesprplklRSILDMSPFTVTDHTPmeiVVDIFRKL---GLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04801    62 ----------------RDVMTKDVITVSPDAD---AMEALKLMsqnNIGRLPVVEDGELVGIISRTDLMR 112
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 647-775 3.90e-07

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: 49.03  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 647 NMTVDDIENMINETSYNGFPVImskESQRLVGFALRRDltiaIESARKKQEGivgssrvcfaqHTPslpaesprplkLRS 726
Cdd:cd04595    10 DTTIEEARKIMLRYGHTGLPVV---EDGKLVGIISRRD----VDKAKHHGLG-----------HAP-----------VKG 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1890274570 727 ILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04595    61 YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLR 109
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
722-784 1.75e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 47.94  E-value: 1.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890274570 722 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHMAQTANQD 784
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLPDRLDE 65
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 730-781 9.18e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. 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: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 45.88  E-value: 9.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1890274570 730 MS--PFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQTA 781
Cdd:cd04584     6 MTknVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 718-777 3.25e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 43.86  E-value: 3.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890274570 718 SPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLrqcL----VTHNGRLLGIITKKDILRHM 777
Cdd:cd04606    61 ADPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 730-775 3.92e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. 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: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 43.96  E-value: 3.92e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1890274570 730 MS--PFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04586    89 MTrpVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
720-779 4.57e-05

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 45.26  E-value: 4.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 720 RPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQ 779
Cdd:COG2524    84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 730-773 6.43e-05

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 46.12  E-value: 6.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1890274570 730 MSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDI 773
Cdd:PTZ00314  104 MDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 666-775 1.00e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. 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: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 42.79  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 666 PVImskESQRLVGFALRRDLTIAIESarkkqegIVGSSRVcfaQHTPSLPAEsprpLKLRSIldMS--PFTVTDHTPMEI 743
Cdd:cd04584    35 PVV---DDGKLVGIVTDRDLLRASPS-------KATSLSI---YELNYLLSK----IPVKDI--MTkdVITVSPDDTVEE 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1890274570 744 VVDIFR--KLGlrqCL-VTHNGRLLGIITKKDILR 775
Cdd:cd04584    96 AALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 732-788 1.99e-04

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: 41.46  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890274570 732 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILRHMAQTANQDPASI 788
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDdDGKLVGIVTERDILRALVEGGLALDTPV 61
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 724-788 3.21e-04

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. 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: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 41.37  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 724 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQC----------------LVTHNGRLLGIITKKDILRHMAQTANQDPAS 787
Cdd:cd04620     1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                  .
gi 1890274570 788 I 788
Cdd:cd04620    81 I 81
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 724-788 1.55e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.04  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890274570 724 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHMAQtANQDPASI 788
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVdDDGRLVGIITDRDLRRRVLA-EGLDPLDT 65
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 236-606 1.59e-03

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 41.69  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 236 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSY 315
Cdd:PRK01610  101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF----TPRQEWKLWIACGAAAGMASAYHAPLAGSLFIAEILFG 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 316 YFPLKTLWRSFFAALVAAFVLRSINPfgnSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTK 395
Cdd:PRK01610  177 TLMLASLGPVVISAVVALLTTNLLNG---SDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLLLTLMNASHRGFVSLK 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 396 FGkyPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDcgplessslcdyrndmnaskivddipdrPAGIGVYSAIwq 475
Cdd:PRK01610  254 LA--PPWQLALGGLIVGLLSLFTPAVWGNGYSVVQSFLTA----------------------------PPLLMLIAGI-- 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 476 lclaLIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIaveqlayyhhdwfIFKEWCEVGADciTPGLYAMVGAAAC 555
Cdd:PRK01610  302 ----FLCKLLAVLASSGSGAPGGVFTPTLFVGLAIGMLYGR-------------SLGLWLPDGEE--ITLLLGLTGMATL 362

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890274570 556 LGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAH 606
Cdd:PRK01610  363 LAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLRRDSIYRQH 413
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 731-773 1.66e-03

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: 38.63  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1890274570 731 SP-FTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDI 773
Cdd:cd04595     2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 45
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 249-416 1.68e-03

ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it facilitates acid resistance in acidic soil. Mutation of this gene (sycA) in Rhizobium tropici CIAT899 causes serious deficiencies in nodule development, nodulation competitiveness, and N2 fixation on Phaseolus vulgaris plants, due to its reduced ability for acid resistance. This family is part of the ClC chloride channel superfamiy. These proteins catalyse the selective flow of Cl- ions across cell membranes and Cl-/H+ exchange transport. These proteins share two characteristics that are apparently inherent to the entire ClC chloride channel superfamily: a unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge.


Pssm-ID: 239654 [Multi-domain]  Cd Length: 378  Bit Score: 41.41  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 249 GLSLGKEGPLVHVAcccGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlkt 321
Cdd:cd03682    92 GGSAGREGTAVQMG---GSLADAFGRVFKLPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP--- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 322 lwrSFFAALVAAFVLRSINPFGNSRLVLFYVEYhTPWYLFELfpfILLGVFGGLWGAFFIRAnIAWCrRRKSTKFGKYPV 401
Cdd:cd03682   166 ---CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNPY 236

                         170
                  ....*....|....*
gi 1890274570 402 LEVIIVAAITAVIAF 416
Cdd:cd03682   237 LRPFVGGLLIILLVY 251
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
718-784 1.69e-03

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 41.59  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1890274570 718 SPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQTANQD 784
Cdd:COG2239   189 ADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLL-ALpvVDEEGRLVGIITVDDVVDVIEEEATED 256
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 722-775 2.92e-03

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. 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.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 38.36  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1890274570 722 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04631    75 VPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILR 128
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 647-775 6.46e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 37.01  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890274570 647 NMTVDDIENMINETSYNGFPVIMSKEsqRLVGFALRRDLTIaiesarkkqegivgssrvcfaqhtpslpaESPRPLKLRS 726
Cdd:cd04601    10 DATVADVLELKAEYGISGVPVTEDGG--KLVGIVTSRDIRF-----------------------------ETDLSTPVSE 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1890274570 727 IldMSPF----TVTDHTPMEIVVDIFR--KLGlRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04601    59 V--MTPDerlvTAPEGITLEEAKEILHkhKIE-KLPIVDDNGELVGLITRKDIEK 110
 
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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