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Conserved domains on  [gi|528484179|ref|XP_005166406|]
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H(+)/Cl(-) exchange transporter 3 isoform X3 [Danio rerio]

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
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 ...
140-648 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: 738.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 140 GLASGALAGGIDIAADWMNDLKEGVClsamwfnheqccwgsnkttfaerdkcpqwktwaelilgqeqgpgsyimNYFMFT 219
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 220 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 299
Cdd:cd03684   33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 300 FSYLFPKYSKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 379
Cdd:cd03684  113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 380 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNTSEL 459
Cdd:cd03684  193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 460 IKELFTDCGPLESSQLCQYRSLMNGSqadptgpdtasaatpGVYSAMWQLSLALVFKIIMTIFTFGLKVPSGLFIPSMAI 539
Cdd:cd03684  273 LELLFNECEPGDDNSLCCYRDPPAGD---------------GVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAV 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 540 GAIAGRIVGIAVEQLAYYHHDWFvFREWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAA 619
Cdd:cd03684  338 GALFGRIVGILVEQLAYSYPDSI-FFACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIA 416
                        490       500
                 ....*....|....*....|....*....
gi 528484179 620 VMTSKWVGDAFGREGIYEAHIRLNGYPFL 648
Cdd:cd03684  417 VMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
659-809 5.81e-43

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: 151.52  E-value: 5.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 659 LAREVMRPrrsdpPLAVLTQDdMTLAELQGIISETSYNGFPVIVSKESQRLVGFALRRDITIAIENarrkqegivlnsrv 738
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528484179 739 yftqhaptlpadsprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEH 809
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 ...
140-648 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: 738.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 140 GLASGALAGGIDIAADWMNDLKEGVClsamwfnheqccwgsnkttfaerdkcpqwktwaelilgqeqgpgsyimNYFMFT 219
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 220 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 299
Cdd:cd03684   33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 300 FSYLFPKYSKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 379
Cdd:cd03684  113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 380 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNTSEL 459
Cdd:cd03684  193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 460 IKELFTDCGPLESSQLCQYRSLMNGSqadptgpdtasaatpGVYSAMWQLSLALVFKIIMTIFTFGLKVPSGLFIPSMAI 539
Cdd:cd03684  273 LELLFNECEPGDDNSLCCYRDPPAGD---------------GVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAV 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 540 GAIAGRIVGIAVEQLAYYHHDWFvFREWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAA 619
Cdd:cd03684  338 GALFGRIVGILVEQLAYSYPDSI-FFACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIA 416
                        490       500
                 ....*....|....*....|....*....
gi 528484179 620 VMTSKWVGDAFGREGIYEAHIRLNGYPFL 648
Cdd:cd03684  417 VMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
225-628 3.33e-92

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: 293.30  E-value: 3.33e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  225 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 304
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  305 PKysKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 384
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  385 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNTSELIKELF 464
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  465 TDCGPLessqlcqyrslmngsqadptgpdtasaatpgvysamWQLSLALVFKIIMTIFTFGLKVPSGLFIPSMAIGAIAG 544
Cdd:pfam00654 232 NGNTSL------------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALG 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  545 RIVGIAVEQLAYYHHdwfvfrewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSK 624
Cdd:pfam00654 276 RAFGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAY 340

                  ....
gi 528484179  625 WVGD 628
Cdd:pfam00654 341 AVSR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
218-641 3.00e-53

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 190.73  E-value: 3.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 218 FTFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCC 296
Cdd:COG0038   52 LVLLLPPLGGLLVGlLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAI 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 297 GNIFSYLFPKyskNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNS 376
Cdd:COG0038  130 GSLLGRLLRL---SPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL--FGNG 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 377 rlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRAnIAWCRRRkSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNT 456
Cdd:COG0038  205 --PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSG 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 457 SELIKELFTdcgplessqlcqyrslmngsqadptgpdtasaatpGVYSAMWqLSLALVFKIIMTIFTFGLKVPSGLFIPS 536
Cdd:COG0038  281 YGLIEALLN-----------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFAPS 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 537 MAIGAIAGRIVGIAVEQLayyhhdwfvfrewceVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPL 616
Cdd:COG0038  325 LFIGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389
                        410       420
                 ....*....|....*....|....*
gi 528484179 617 MAAVMTSKWVGDAFGREGIYEAHIR 641
Cdd:COG0038  390 MIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
659-809 5.81e-43

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: 151.52  E-value: 5.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 659 LAREVMRPrrsdpPLAVLTQDdMTLAELQGIISETSYNGFPVIVSKESQRLVGFALRRDITIAIENarrkqegivlnsrv 738
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528484179 739 yftqhaptlpadsprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEH 809
Cdd:cd04591   61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
221-638 1.94e-25

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 110.37  E-value: 1.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 221 WALSF------AFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVAC 294
Cdd:PRK05277  44 WIVAFlisavlAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 295 CCGNIFSYLFPKYSKNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFVLRSINp 372
Cdd:PRK05277 122 NIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN- 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 373 fGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTRFGKYpVLEVITVAAITAIVAFPN 449
Cdd:PRK05277 199 -GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLCGLLGLLA 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 450 PytrqntselikelftdcgplessqlcqyrSLMNGsqadptGPDTASAATPGVYSAMWQLSLaLVFKIIMTIFTFGLKVP 529
Cdd:PRK05277 275 P-----------------------------AAVGG------GFNLIPIALAGNFSIGMLLFI-FVARFITTLLCFGSGAP 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 530 SGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfvFREWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGG 609
Cdd:PRK05277 319 GGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDN 383
                        410       420
                 ....*....|....*....|....*....
gi 528484179 610 LEYIVPLMAAVMTSKWVGDAFGREGIYEA 638
Cdd:PRK05277 384 YQLILPLIITCLGATLLAQFLGGKPIYSA 412
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
575-810 6.72e-13

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 68.37  E-value: 6.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 575 ITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGdAFGREGIYEAHIRLNGYPFLDAKEEF 654
Cdd:COG2524    4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 655 THTTLAREVMrprrSDPPLAVltQDDMTLAELQGIISETSYNGFPVIvskESQRLVGFALRRDITIAIENARRKQEgivl 734
Cdd:COG2524   83 VLKMKVKDIM----TKDVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528484179 735 nsrvyftqhaptlpadsprpLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGIVLGIITKKNILEHL 810
Cdd:COG2524  150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
765-811 1.75e-06

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 45.58  E-value: 1.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 528484179   765 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGIVLGIITKKNILEHLE 811
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
757-812 1.43e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 42.97  E-value: 1.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528484179  757 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGIVLGIITKKNILEHLEE 812
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALLG 57
 
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 ...
140-648 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: 738.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 140 GLASGALAGGIDIAADWMNDLKEGVClsamwfnheqccwgsnkttfaerdkcpqwktwaelilgqeqgpgsyimNYFMFT 219
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 220 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 299
Cdd:cd03684   33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 300 FSYLFPKYSKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 379
Cdd:cd03684  113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 380 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNTSEL 459
Cdd:cd03684  193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 460 IKELFTDCGPLESSQLCQYRSLMNGSqadptgpdtasaatpGVYSAMWQLSLALVFKIIMTIFTFGLKVPSGLFIPSMAI 539
Cdd:cd03684  273 LELLFNECEPGDDNSLCCYRDPPAGD---------------GVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAV 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 540 GAIAGRIVGIAVEQLAYYHHDWFvFREWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAA 619
Cdd:cd03684  338 GALFGRIVGILVEQLAYSYPDSI-FFACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIA 416
                        490       500
                 ....*....|....*....|....*....
gi 528484179 620 VMTSKWVGDAFGREGIYEAHIRLNGYPFL 648
Cdd:cd03684  417 VMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
140-637 3.99e-146

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: 436.39  E-value: 3.99e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 140 GLASGALAGGIDIAADWMNDLKEGVCLSAmwfnheqccwgsnkttfaerdkcpqwktwaelilgqeqgPGSYIMNYFMFT 219
Cdd:cd01036    1 GLLMGLVAVVLDYAVESSLDAGQWLLRRI---------------------------------------PGSYLLGYLMWV 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 220 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 299
Cdd:cd01036   42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 300 FSYLFPKYS----------KNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRS 369
Cdd:cd01036  122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 370 INPFGNSR----------LVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTRF---GKYPVLEVI 436
Cdd:cd01036  202 YNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFrktARYRVLEPV 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 437 TVAAITAIVAFPnpytrqntselikelftdcgplessqlcqyrslmngsqadptgpdtasaatpgvysamWQLSLALVFK 516
Cdd:cd01036  282 LFTLIYSTIHYA----------------------------------------------------------PTLLLFLLIY 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 517 IIMTIFTFGLKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDwfvfrewCEVGADCITPGLYAMVGAAACLGGVTRMT 596
Cdd:cd01036  304 FWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRLT 376
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 528484179 597 VSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGrEGIYE 637
Cdd:cd01036  377 FSICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-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. ...
209-648 2.67e-93

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: 300.72  E-value: 2.67e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 209 GSYIMNYFMFTFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGP 288
Cdd:cd03685   72 GRLFTAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGP 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 289 LVHVACCCGNIFS----------YLFPKYSKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFF 358
Cdd:cd03685  152 MIHIGACIAAGLSqggstslrldFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFF 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 359 AALVAAFVLRSINPFGNSR---------LVLFYVeYHTP--WYLFELFPFILLGVFGGLWGAFFIRANIAWCR-RRKSTR 426
Cdd:cd03685  232 SSMIVTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRfRKRINH 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 427 FGK-YPVLEVITVAAITAIVAFpnpytrqntselikelftdcgplessqlcqyrslmngsqadptgpdtasaatpgvysa 505
Cdd:cd03685  311 KGKlLKVLEALLVSLVTSVVAF---------------------------------------------------------- 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 506 MWQLSLALVFKIIMTIFTFGLKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfvfrewceVGADCITPGLYAMVGA 585
Cdd:cd03685  333 PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSY---------------FGFTSIDPGLYALLGA 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528484179 586 AACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFgREGIYEAHIRLNGYPFL 648
Cdd:cd03685  398 AAFLGGVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
225-628 3.33e-92

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: 293.30  E-value: 3.33e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  225 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 304
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  305 PKysKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 384
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  385 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNTSELIKELF 464
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  465 TDCGPLessqlcqyrslmngsqadptgpdtasaatpgvysamWQLSLALVFKIIMTIFTFGLKVPSGLFIPSMAIGAIAG 544
Cdd:pfam00654 232 NGNTSL------------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALG 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179  545 RIVGIAVEQLAYYHHdwfvfrewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSK 624
Cdd:pfam00654 276 RAFGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAY 340

                  ....
gi 528484179  625 WVGD 628
Cdd:pfam00654 341 AVSR 344
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
209-648 2.37e-81

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: 267.58  E-value: 2.37e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 209 GSYIMNYFMFTFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGP 288
Cdd:cd03683   39 GNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGP 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 289 LVHVACCCGNIFSYLFPKYS---KNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAF 365
Cdd:cd03683  119 FVHISSIVAALLSKLTTFFSgiyENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAF 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 366 VLRSINPF---GNSRLVLFYVEYHT--PWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTR-----FGKYPVLEV 435
Cdd:cd03683  199 TFRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRlfskfLKRSPLLYP 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 436 ITVAAITAIVAFPnpytrqntselikeLFTdcgplessqlcqyrslmngsqadptgpdtasaatpgvysamwqLSLALVF 515
Cdd:cd03683  279 AIVALLTAVLTFP--------------FLT-------------------------------------------LFLFIVV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 516 KIIMTIFTFGLKVPSGLFIPSMAIGAIAGRIVG-IAVEQLAYYHHDWFVFRewcevgadcITPGLYAMVGAAACLGGVTR 594
Cdd:cd03683  302 KFVLTALAITLPVPAGIFMPVFVIGAALGRLVGeIMAVLFPEGIRGGISNP---------IGPGGYAVVGAAAFSGAVTH 372
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528484179 595 mTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGReGIYEAHIRLNGYPFL 648
Cdd:cd03683  373 -TVSVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQP-SIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
199-623 1.85e-59

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: 207.03  E-value: 1.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 199 ELILGQEQGPGSYIMNYFMFTFWALSFAFLAVSLVKVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLMIKTITLVLAV 277
Cdd:cd00400   20 NLLFGGLPGELAAGSLSPLYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 278 ASGLSLGKEGPLVHVACCCGNIFSYLFpKYSKNEakKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 357
Cdd:cd00400   97 GSGGSVGREGPIVQIGAAIGSWLGRRL-RLSRND--RRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 358 FAALVAAFVLRSINPFGNsrlvLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKstRFGKYPVLEVIT 437
Cdd:cd00400  174 LASVAAALVSRLLFGAEP----AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPAL 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 438 VAAITAIVAFPNPYTRqntselikelftdcgplessqlcqyrslmngsqadPTGPDTASAATPGVYSAmWQLSLALVFKI 517
Cdd:cd00400  248 GGLLLGLLGLFLPQVL-----------------------------------GSGYGAILLALAGELSL-LLLLLLLLLKL 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 518 IMTIFTFGLKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYyhhdwfvfrewcevgADCITPGLYAMVGAAACLGGVTRMTV 597
Cdd:cd00400  292 LATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALFP---------------GLVASPGAYALVGMAALLAAVLRAPL 356
                        410       420
                 ....*....|....*....|....*.
gi 528484179 598 SLVVIVFELTGGLEYIVPLMAAVMTS 623
Cdd:cd00400  357 TAILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
218-641 3.00e-53

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 190.73  E-value: 3.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 218 FTFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCC 296
Cdd:COG0038   52 LVLLLPPLGGLLVGlLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAI 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 297 GNIFSYLFPKyskNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNS 376
Cdd:COG0038  130 GSLLGRLLRL---SPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL--FGNG 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 377 rlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRAnIAWCRRRkSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNT 456
Cdd:COG0038  205 --PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSG 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 457 SELIKELFTdcgplessqlcqyrslmngsqadptgpdtasaatpGVYSAMWqLSLALVFKIIMTIFTFGLKVPSGLFIPS 536
Cdd:COG0038  281 YGLIEALLN-----------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFAPS 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 537 MAIGAIAGRIVGIAVEQLayyhhdwfvfrewceVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPL 616
Cdd:COG0038  325 LFIGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389
                        410       420
                 ....*....|....*....|....*
gi 528484179 617 MAAVMTSKWVGDAFGREGIYEAHIR 641
Cdd:COG0038  390 MIACVIAYLVSRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
217-638 4.69e-48

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: 175.81  E-value: 4.69e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 217 MFTFWALsFAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCC 296
Cdd:cd01031   40 LPLISAV-LGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 297 GNIFSYLFPKyskNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGns 376
Cdd:cd01031  117 GQGVSKWFKT---SPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG-- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 377 rlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRAnIAWCRRRKSTRFGKYPVLEVITVAAITAIVAFPNPYTRQNT 456
Cdd:cd01031  192 --PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRS-LLKSQDLYRKLKKLPRELRVLLPGLLIGPLGLLLPEALGGG 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 457 SELIKELFTdcGPLessqlcqyrslmngsqadptgpdtasaatpgvysAMWQLSLALVFKIIMTIFTFGLKVPSGLFIPS 536
Cdd:cd01031  269 HGLILSLAG--GNF----------------------------------SISLLLLIFVLRFIFTMLSYGSGAPGGIFAPM 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 537 MAIGAIAGRIVGIAVEQLAYYHHDwfvfrewcevgadciTPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPL 616
Cdd:cd01031  313 LALGALLGLLFGTILVQLGPIPIS---------------APATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPL 377
                        410       420
                 ....*....|....*....|..
gi 528484179 617 MAAVMTSKWVGDAFGREGIYEA 638
Cdd:cd01031  378 MVVCLVAYLVADLLGGKPIYEA 399
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
659-809 5.81e-43

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: 151.52  E-value: 5.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 659 LAREVMRPrrsdpPLAVLTQDdMTLAELQGIISETSYNGFPVIVSKESQRLVGFALRRDITIAIENarrkqegivlnsrv 738
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528484179 739 yftqhaptlpadsprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEH 809
Cdd:cd04591   61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
215-636 3.92e-29

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: 120.41  E-value: 3.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 215 YFMFTFWALSFA------FLAVSLVKVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLMIKTITLVLAVASGLSLGK 285
Cdd:cd01034   20 RLTATHPWLPLLltpagfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGR 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 286 EGPLVHVACCCGNIFSYLFPKysKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAAL 361
Cdd:cd01034  100 EGPSVQIGAAVMLAIGRRLPK--WGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 362 VAAFVLRSINPFGNSRLVLfyveyhTPWYLfeLFPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFG---KYPVLeviTV 438
Cdd:cd01034  178 VSLAVLGNYPYFGVAAVAL------PLGEA--WLLVLVCGVVGGLAGGLFARLLVALSSGLPGWVRRfrrRRPVL---FA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 439 AAITAIVAFpnpytrqntselikelftdCGplessqlcqyrsLMNGSQADPTGPDTASAATPGVYSAMWQLSLAlvfKII 518
Cdd:cd01034  247 ALCGLALAL-------------------IG------------LVSGGLTFGTGYLQARAALEGGGGLPLWFGLL---KFL 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 519 MTIFTFGLKVPSGLFIPSMAIGAiagrIVGIAVEQLAYYHHdwfvfrewcevgadcitPGLYAMVGAAACLGGVTRMTVS 598
Cdd:cd01034  293 ATLLSYWSGIPGGLFAPSLAVGA----GLGSLLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLT 351
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 528484179 599 LVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIY 636
Cdd:cd01034  352 AFVIVMEMTGDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
221-638 1.94e-25

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 110.37  E-value: 1.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 221 WALSF------AFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVAC 294
Cdd:PRK05277  44 WIVAFlisavlAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 295 CCGNIFSYLFPKYSKNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFVLRSINp 372
Cdd:PRK05277 122 NIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN- 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 373 fGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTRFGKYpVLEVITVAAITAIVAFPN 449
Cdd:PRK05277 199 -GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLCGLLGLLA 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 450 PytrqntselikelftdcgplessqlcqyrSLMNGsqadptGPDTASAATPGVYSAMWQLSLaLVFKIIMTIFTFGLKVP 529
Cdd:PRK05277 275 P-----------------------------AAVGG------GFNLIPIALAGNFSIGMLLFI-FVARFITTLLCFGSGAP 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 530 SGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfvFREWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGG 609
Cdd:PRK05277 319 GGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDN 383
                        410       420
                 ....*....|....*....|....*....
gi 528484179 610 LEYIVPLMAAVMTSKWVGDAFGREGIYEA 638
Cdd:PRK05277 384 YQLILPLIITCLGATLLAQFLGGKPIYSA 412
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
267-752 1.84e-21

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 99.43  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 267 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYL--FPKyskneAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEV 344
Cdd:PRK01862 119 LWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFahFDP-----PRLRLLVACGAAAGITSAYNAPIAGAFFVAEIV 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 345 SYYFPLKTLWRSFFAALVAAFVLRSinpFGNSRlVLFYVEYH---TPWylfELFPFILLGVFGGLWGAFFIRAniawcRR 421
Cdd:PRK01862 194 LGSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRL-----LD 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 422 RKSTRFGKYPVLEVITVA---AITAIVAFPNPYTRQNTSELIKELFTdcgplessqlcqyrslmngsqadptgpdtasaa 498
Cdd:PRK01862 262 ASKNQFKRLPVPLPVRLAlggLLVGVISVWVPEVWGNGYSVVNTILH--------------------------------- 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 499 TPGVYSAMWqlsLALVFKIIMTIFTFGLKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfvfreWCEVGADcitPG 578
Cdd:PRK01862 309 APWTWQALV---AVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHAL------------WPGHTSA---PF 370
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 579 LYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNgypflDAKEEFTH-- 656
Cdd:PRK01862 371 AYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLRRH-----QDEAERERlr 445
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 657 TTLAREVMRPRRSDPPLavltqdDMTLAELQGIISETSYNGfpVIVSKESQRLVGFALRRDITIAIENARRKQEGIVLNs 736
Cdd:PRK01862 446 TTQMRELIQPAQTVVPP------TASVADMTRVFLEYPVKY--LYVVDDDGRFRGAVALKDITSDLLDKRDTTDKTAAD- 516
                        490
                 ....*....|....*.
gi 528484179 737 rvYFTQHAPTLPADSP 752
Cdd:PRK01862 517 --YAHTPFPLLTPDMP 530
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
575-810 6.72e-13

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 68.37  E-value: 6.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 575 ITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGdAFGREGIYEAHIRLNGYPFLDAKEEF 654
Cdd:COG2524    4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 655 THTTLAREVMrprrSDPPLAVltQDDMTLAELQGIISETSYNGFPVIvskESQRLVGFALRRDITIAIENARRKQEgivl 734
Cdd:COG2524   83 VLKMKVKDIM----TKDVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528484179 735 nsrvyftqhaptlpadsprpLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGIVLGIITKKNILEHL 810
Cdd:COG2524  150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
659-810 2.67e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 61.81  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 659 LAREVMrprrSDPPLAVltQDDMTLAELQGIISETSYNGFPVIvsKESQRLVGFALRRDITIAIENARRKQegivlnsrv 738
Cdd:COG3448    3 TVRDIM----TRDVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE--------- 65
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528484179 739 yftqhaptlPADSPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRqCL--VTHNGIVLGIITKKNILEHL 810
Cdd:COG3448   66 ---------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRAL 129
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
264-623 7.75e-11

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: 65.01  E-value: 7.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 264 WTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkySKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE- 342
Cdd:cd01033   83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWL---GLTVADRRLLVACAAGAGLAAVYNVPLAGALFALEi 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 343 ---EVSyyfplktlWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLfeLFPF-ILLGVFGGLWGAFFIRANiAW 418
Cdd:cd01033  160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTP--LLIWaLLAGPVLGVVAAGFRRLS-QA 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 419 CRRRKSTrfGKYPVLEVITVAAITAIVAFPNPYTRQNTSELIKELFTDCGPLESsqlcqyrslmngsqadptgpdtasaa 498
Cdd:cd01033  229 ARAKRPK--GKRILWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSL-------------------------- 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 499 tpgvysamwqLSLALVFKIIMTIFTFGLKVPSGLFIPSMAIGAIAGRIVGIaveqlayyhhdwfvfrewcevGADCITPG 578
Cdd:cd01033  281 ----------LLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGI---------------------VWNALLPP 329
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 528484179 579 L----YAMVGAAACLGGVTRMTVSLVVIVFELTG-GLEYIVPLMAAVMTS 623
Cdd:cd01033  330 LsiaaFALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS COG0517
CBS domain [Signal transduction mechanisms];
659-812 2.04e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 59.11  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 659 LAREVMRprrSDPPLAvltQDDMTLAELQGIISETSYNGFPVIvsKESQRLVGFALRRDITIAIEnarrkQEGIVLNSRv 738
Cdd:COG0517    2 KVKDIMT---TDVVTV---SPDATVREALELMSEKRIGGLPVV--DEDGKLVGIVTDRDLRRALA-----AEGKDLLDT- 67
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528484179 739 yftqhaptlpadsprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLV-THNGIVLGIITKKNILEHLEE 812
Cdd:COG0517   68 -----------------PVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
670-807 1.22e-07

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 50.71  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 670 DPPLAVLTqDDMTLAELQGIISETSYNGFPVIvsKESQRLVGFALRRDITIAIenarrkqegivlnsrvyftqhaptLPA 749
Cdd:cd02205    1 TRDVVTVD-PDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRAL------------------------VEG 53
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528484179 750 DSPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGIVLGIITKKNIL 807
Cdd:cd02205   54 GLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
653-813 1.74e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 51.07  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 653 EFTHTTLAREVMRprRSDPplAVLTqDDMTLAELQGIISETSYNGFPVIvsKESQRLVGFALRRDItiaienarrkqegi 732
Cdd:COG4109   11 TFKEILLVEDIMT--LEDV--ATLS-EDDTVEDALELLEKTGHSRFPVV--DENGRLVGIVTSKDI-------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 733 vlnsrvyftqhaptlpADSPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGIVLGIITKKNILEHLE 811
Cdd:COG4109   70 ----------------LGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKALQ 133

                 ..
gi 528484179 812 EI 813
Cdd:COG4109  134 KI 135
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
660-812 4.79e-07

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 49.44  E-value: 4.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 660 AREVMrprrSDPPLAVltQDDMTLAELQGIISETSYNGfpVIVSKESQRLVGFALRRDItiaienaRRKqegIVLNSRvy 739
Cdd:COG2905    1 VKDIM----SRDVVTV--SPDATVREAARLMTEKGVGS--LVVVDDDGRLVGIITDRDL-------RRR---VLAEGL-- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528484179 740 ftqhaptlpadSPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILEHLEE 812
Cdd:COG2905   61 -----------DPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSE 122
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
765-811 1.75e-06

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 45.58  E-value: 1.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 528484179   765 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGIVLGIITKKNILEHLE 811
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIKALA 49
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
680-808 5.73e-06

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: 45.95  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 680 DMTLAELQGIISETSYNGFPVIvskESQRLVGFALRRDItiaiENARRKQEGivlnsrvyftqHAPtlpadsprplkLRS 759
Cdd:cd04595   10 DTTIEEARKIMLRYGHTGLPVV---EDGKLVGIISRRDV----DKAKHHGLG-----------HAP-----------VKG 60
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 528484179 760 ILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNILE 808
Cdd:cd04595   61 YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLR 109
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
757-812 1.43e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 42.97  E-value: 1.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 528484179  757 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGIVLGIITKKNILEHLEE 812
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
680-807 2.79e-04

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: 41.65  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 680 DMTLAELQGIISETSYNGFPVIvsKESQRLVGFA-----LRRDITIAIENARRKQEGIVLNSRVYFTQHAPTlpadspRP 754
Cdd:cd04586   11 DTSVREAARLLLEHRISGLPVV--DDDGKLVGIVsegdlLRREEPGTEPRRVWWLDALLESPERLAEEYVKA------HG 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528484179 755 LKLRSIldMS--PFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGIVLGIITKKNIL 807
Cdd:cd04586   83 RTVGDV--MTrpVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLL 135
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
662-807 5.56e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 40.24  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 662 EVMRPR-RSDPPlavltqdDMTLAELQGIISETSYNGFPVIvskESQRLVGFalrrditIAIENARRKQEGIVLNSRVyf 740
Cdd:cd04801    1 DIMTPEvVTVTP-------EMTVSELLDRMFEEKHLGYPVV---ENGRLVGI-------VTLEDIRKVPEVEREATRV-- 61
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 741 tqhaptlpadsprplklRSILDMSPFTVTDHTPmeiVVDIFRKL---GLRQCLVTHNGIVLGIITKKNIL 807
Cdd:cd04801   62 -----------------RDVMTKDVITVSPDAD---AMEALKLMsqnNIGRLPVVEDGELVGIISRTDLM 111
CBS COG0517
CBS domain [Signal transduction mechanisms];
755-812 9.21e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 39.85  E-value: 9.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528484179 755 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGIVLGIITKKNILEHLEE 812
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVdEDGKLVGIVTDRDLRRALAA 59
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
755-814 1.61e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 1.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528484179 755 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGIVLGIITKKNILEHLEEIK 814
Cdd:COG3448    2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLPDR 62
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
280-636 1.96e-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: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 280 GLSLGKEGPLVHVAcccGNIFSYLFPKYSKNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlkt 352
Cdd:cd03682   92 GGSAGREGTAVQMG---GSLADAFGRVFKLPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP--- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 353 lwrSFFAALVAAFVLRSINPFGNSRLVLFYVEYhTPWYLFELfpfILLGVFGGLWGAFFIRAnIAWCrRRKSTRFGKYPV 432
Cdd:cd03682  166 ---CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNPY 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 433 LEVITVAAITAIVAFpnpytrqntselikelftdcgplessQLCQYRSLMNGsqadpTGPDTASAATPGVYSAMWqlsla 512
Cdd:cd03682  237 LRPFVGGLLIILLVY--------------------------LLGSRRYLGLG-----TPLIEDSFFGGTVYPYDW----- 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 513 lVFKIIMTIFTFGLKVPSGLFIPSMAIGAIAGRIvgiaveqLAYYHHdwfvfrewcevgadcITPGLYAMVGAAACLGGV 592
Cdd:cd03682  281 -LLKLIFTVITLGAGFKGGEVTPLFFIGATLGNA-------LAPILG---------------LPVSLLAALGFVAVFAGA 337
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 528484179 593 TRMTVSLVVIVFELTGGlEYIVPLMAAVMTSKWVGdafGREGIY 636
Cdd:cd03682  338 TNTPLACIIMGIELFGA-ENAPYFFIACLVAYLFS---GHTGIY 377
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
660-724 4.03e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.04  E-value: 4.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528484179  660 AREVMRPrrsdPPLAVltQDDMTLAELQGIISETSYNGFPVIvsKESQRLVGFALRRDITIAIEN 724
Cdd:pfam00571   1 VKDIMTK----DVVTV--SPDTTLEEALELMREHGISRLPVV--DEDGKLVGIVTLKDLLRALLG 57
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
667-809 4.52e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, 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: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 37.90  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 667 RRSDPPLAVLTQDDMTLAELQGIISETSYNGFPVIvsKESQRLVGFALRRDITIAIENARRKQEGIVlnSRVYFTQhAPT 746
Cdd:cd04608    5 RRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVV--DEDGRVVGMVTEGNLLSSLLAGRAQPSDPV--SKAMYKQ-FKQ 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528484179 747 LPADSPrpL-KLRSILDMSPFTvtdhtpmeIVVDifrklglrqclvtHNGIVLGIITKKNILEH 809
Cdd:cd04608   80 VDLDTP--LgALSRILERDHFA--------LVVD-------------GQGKVLGIVTRIDLLNY 120
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
678-810 5.55e-03

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: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 37.55  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528484179 678 QDDMTLAEL--QGIISETSYNGFPVIvsKESQRLVGfALRRDITIAIEnarrkqegivlnsrvyfTQHAPTLPadsprpl 755
Cdd:cd04639   11 DADLTLREFadDYLIGKKSWREFLVT--DEAGRLVG-LITVDDLRAIP-----------------TSQWPDTP------- 63
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 528484179 756 kLRSIL--DMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGIVLGIITKKNILEHL 810
Cdd:cd04639   64 -VRELMkpLEEIPTVAADQSLLEVVKLLEEQQLPALAVVSeNGTLVGLIEKEDIIELL 120
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
675-723 6.26e-03

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: 35.57  E-value: 6.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 528484179   675 VLTQDDMTLAELQGIISETSYNGFPVIVSKesQRLVGFALRRDITIAIE 723
Cdd:smart00116   3 VTVSPDTTLEEALELLRENGIRRLPVVDEE--GRLVGIVTRRDIIKALA 49
 
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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