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Conserved domains on  [gi|379643013|ref|NP_001243873|]
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H(+)/Cl(-) exchange transporter 4 isoform 2 [Homo sapiens]

Protein Classification

chloride channel protein( domain architecture ID 10132694)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 42-490 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: 714.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  42 SELLVNQSEGasayILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVV 121
Cdd:cd03684   15 ASWLSDLKEG----YCNYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 122 SSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:cd03684   91 ASGLSLGKEGPLVHIATCVGNIISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 202 FAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKTTRLGKYPVLEVIV 281
Cdd:cd03684  171 FCALVAAFTLKSLNPFGTGRLVLFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 282 VTAITAIIAYPNPYTRQSTSELISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVV 361
Cdd:cd03684  251 VALITALISFPNPYTRLDMTELLELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 362 TIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:cd03684  318 TIFTFGIKVPAGIFVPSMAVGALFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSL 396

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 379643013 442 VVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFL 490
Cdd:cd03684  397 VVIMFELTGALNYILPLMIAVMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 501-651 5.47e-46

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: 158.84  E-value: 5.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 501 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 580
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379643013 581 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 651
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 ...
 42-490 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: 714.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  42 SELLVNQSEGasayILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVV 121
Cdd:cd03684   15 ASWLSDLKEG----YCNYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 122 SSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:cd03684   91 ASGLSLGKEGPLVHIATCVGNIISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 202 FAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKTTRLGKYPVLEVIV 281
Cdd:cd03684  171 FCALVAAFTLKSLNPFGTGRLVLFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 282 VTAITAIIAYPNPYTRQSTSELISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVV 361
Cdd:cd03684  251 VALITALISFPNPYTRLDMTELLELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 362 TIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:cd03684  318 TIFTFGIKVPAGIFVPSMAVGALFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSL 396

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 379643013 442 VVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFL 490
Cdd:cd03684  397 VVIMFELTGALNYILPLMIAVMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 69-470 2.16e-93

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: 292.53  E-value: 2.16e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013   69 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 148
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  149 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 228
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  229 YHTPWYMAELFPFILLGVFGGLWGTLFIRCNIaWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELF 308
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  309 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRM 388
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  389 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 468
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 379643013  469 AD 470
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
42-483 1.58e-57

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 199.98  E-value: 1.58e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  42 SELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVV 121
Cdd:COG0038   33 THLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 122 SSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:COG0038  111 GSGGSLGREGPSVQIGAAIGSLLGRLL-RLSPED--RRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 202 FAALVAAFTLRSInpFGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCnIAWCRRRkTTRLGKYPVLEVIV 281
Cdd:COG0038  188 IASVVAYLVSRLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAI 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 282 VTAITAIIAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVV 361
Cdd:COG0038  262 GGLLVGLLGLFLPQVLGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLA 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 362 TIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:COG0038  308 TALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG---------------LSPGLFALVGMAAVFAAVTRAPLTA 372

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 379643013 442 VVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIH 483
Cdd:COG0038  373 ILLVLEMTGSYSLLLPLMIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 501-651 5.47e-46

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: 158.84  E-value: 5.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 501 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 580
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379643013 581 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 651
Cdd:cd04591   61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
52-522 4.03e-27

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 114.60  E-value: 4.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  52 ASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEG 131
Cdd:PRK05277  37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 132 PLVHVACCCGNFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 209
Cdd:PRK05277 115 PTVQMGGNIGRMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 210 TLRSINpfGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIA---WCRRRKTTRLGKYpVLEVIVVTAIT 286
Cdd:PRK05277 193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRW-VLMGGAVGGLC 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 287 AIIAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVVTIFTF 366
Cdd:PRK05277 268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCF 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 367 GMKIPSGLFIPSMAVGAIAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMF 446
Cdd:PRK05277 314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVL 378

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013 447 ELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 522
Cdd:PRK05277 379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
417-652 1.53e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 75.69  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 417 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 496
Cdd:COG2524    4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 497 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 576
Cdd:COG2524   83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379643013 577 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 652
Cdd:COG2524  154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 607-650 8.55e-08

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: 49.05  E-value: 8.55e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 379643013   607 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 650
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 599-653 2.44e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 47.98  E-value: 2.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013  599 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 653
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 606-648 7.59e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 7.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 379643013 606 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 648
Cdd:PTZ00314 105 DPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 42-490 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: 714.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  42 SELLVNQSEGasayILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVV 121
Cdd:cd03684   15 ASWLSDLKEG----YCNYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 122 SSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:cd03684   91 ASGLSLGKEGPLVHIATCVGNIISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 202 FAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKTTRLGKYPVLEVIV 281
Cdd:cd03684  171 FCALVAAFTLKSLNPFGTGRLVLFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 282 VTAITAIIAYPNPYTRQSTSELISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVV 361
Cdd:cd03684  251 VALITALISFPNPYTRLDMTELLELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 362 TIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:cd03684  318 TIFTFGIKVPAGIFVPSMAVGALFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSL 396

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 379643013 442 VVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFL 490
Cdd:cd03684  397 VVIMFELTGALNYILPLMIAVMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 33-479 1.18e-135

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: 404.03  E-value: 1.18e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  33 DKCPLWQKWSELLVNQSegasaYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLI 112
Cdd:cd01036   16 ESSLDAGQWLLRRIPGS-----YLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 113 KTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYS----------KNEGKRREVLSAAAAAGVSVAFGAPIGGVL 182
Cdd:cd01036   91 KTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 183 FSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSR----------LVLFYVEYHTPWYMAELFPFILLGVFGGLWG 252
Cdd:cd01036  171 FVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLA 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 253 TLFIRCNIAWCRRR---KTTRLGKYPVLEVIVVTAITAIIAYPnpytrqstseliselfndcgalessqlcdyindpnmt 329
Cdd:cd01036  251 ALFVRLSIIFLRWRrrlLFRKTARYRVLEPVLFTLIYSTIHYA------------------------------------- 293

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 330 rpvddipdrpagvgvytamWQLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHDwiifrnw 409
Cdd:cd01036  294 -------------------PTLLLFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG------- 347

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 410 CRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYE 479
Cdd:cd01036  348 AESATLWADPGVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 69-470 2.16e-93

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: 292.53  E-value: 2.16e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013   69 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 148
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  149 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 228
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  229 YHTPWYMAELFPFILLGVFGGLWGTLFIRCNIaWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELF 308
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  309 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRM 388
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  389 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 468
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 379643013  469 AD 470
Cdd:pfam00654 343 SR 344
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 39-490 6.81e-90

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: 287.63  E-value: 6.81e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  39 QKWSELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLV 118
Cdd:cd03685   58 AGLKFLVVKNYIEKGRLFTAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVI 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 119 LVVSSGLSLGKEGPLVHVACCCGNFFSSLFSK----------YSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV 188
Cdd:cd03685  138 LSVSGGLALGKEGPMIHIGACIAAGLSQGGSTslrldfrwfrYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEV 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 189 SYYFPLKTLWRSFFAALVAAFTLRSINPFGNSR---------LVLFYVeYHTP--WYMAELFPFILLGVFGGLWGTLFIR 257
Cdd:cd03685  218 ASFWNQALTWRTFFSSMIVTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNH 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 258 CN--IAWCRRRKTTRLGKYPVLEVIVVTAITAIIAYpnpytrqstseliselfndcgalessqlcdyindpnmtrpvddi 335
Cdd:cd03685  297 LNhkVTRFRKRINHKGKLLKVLEALLVSLVTSVVAF-------------------------------------------- 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 336 pdrpagvgvytaMWQLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLayhhhdwiifrnwcrPGAD 415
Cdd:cd03685  333 ------------PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSY---------------FGFT 385

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379643013 416 CVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFgKEGIYEAHIHLNGYPFL 490
Cdd:cd03685  386 SIDPGLYALLGAAAFLGGVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 54-490 5.44e-80

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: 260.26  E-value: 5.44e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  54 AYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPL 133
Cdd:cd03683   40 NSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPF 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 134 VHVACCCGNFFSSL---FSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFT 210
Cdd:cd03683  120 VHISSIVAALLSKLttfFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFT 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 211 LRSINPF---GNSRLVLFYVEYHT--PWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKTTR-----LGKYPVLEVI 280
Cdd:cd03683  200 FRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRlfskfLKRSPLLYPA 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 281 VVTAITAIIAYPnpytrqstseliselfndcgalessqlcdYINdpnmtrpvddipdrpagvgvytamwqLALALIFKIV 360
Cdd:cd03683  280 IVALLTAVLTFP-----------------------------FLT--------------------------LFLFIVVKFV 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 361 VTIFTFGMKIPSGLFIPSMAVGAIAGRMVGigvEQLAYHHHDWIifrnwCRPGADCVTPGLYAMVGAAACLGGVTRmTVS 440
Cdd:cd03683  305 LTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAVLFPEGI-----RGGISNPIGPGGYAVVGAAAFSGAVTH-TVS 375

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 379643013 441 LVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYEAHIHLNGYPFL 490
Cdd:cd03683  376 VAVIIFELTGQISHLLPVLIAVLISNAVAQFLQ-PSIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 61-465 3.27e-60

CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function.


Pssm-ID: 238233 [Multi-domain]  Cd Length: 383  Bit Score: 206.26  E-value: 3.27e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  61 MYILWALLFAFLAVSLVRVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACC 139
Cdd:cd00400   38 LYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 140 CGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGN 219
Cdd:cd00400  115 IGSWLGRRL-RLSRND--RRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEP 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 220 srlvLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAWCRRRKttRLGKYPVLEVIVVTAITAIIAYPNPYTRQS 299
Cdd:cd00400  192 ----AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPALGGLLLGLLGLFLPQVLGS 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 300 TSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvgVYTAMWQLALALIFKIVVTIFTFGMKIPSGLFIPSM 379
Cdd:cd00400  266 GYGAILLALA----------------------------------GELSLLLLLLLLLLKLLATALTLGSGFPGGVFAPSL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 380 AVGAIAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLM 459
Cdd:cd00400  312 FIGAALGAAFGLLLPALFPGLV---------------ASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLM 376


                 ....*.
gi 379643013 460 AAAVTS 465
Cdd:cd00400  377 LAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
42-483 1.58e-57

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 199.98  E-value: 1.58e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  42 SELLVNQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVV 121
Cdd:COG0038   33 THLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 122 SSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:COG0038  111 GSGGSLGREGPSVQIGAAIGSLLGRLL-RLSPED--RRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVL 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 202 FAALVAAFTLRSInpFGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCnIAWCRRRkTTRLGKYPVLEVIV 281
Cdd:COG0038  188 IASVVAYLVSRLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAI 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 282 VTAITAIIAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVV 361
Cdd:COG0038  262 GGLLVGLLGLFLPQVLGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLA 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 362 TIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:COG0038  308 TALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG---------------LSPGLFALVGMAAVFAAVTRAPLTA 372

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 379643013 442 VVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAHIH 483
Cdd:COG0038  373 ILLVLEMTGSYSLLLPLMIACVIAYLVSRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 57-480 7.71e-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: 173.50  E-value: 7.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  57 LNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 136
Cdd:cd01031   35 PLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 137 ACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINP 216
Cdd:cd01031  113 GAAIGQGVSKWF-KTSPEE--RRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 217 FGnsrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIR--CNIAWCRRRkttRLGKYPVLEVIVVTAITAIIAYPNP 294
Cdd:cd01031  190 LG----PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRslLKSQDLYRK---LKKLPRELRVLLPGLLIGPLGLLLP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 295 YTRQSTSELISELFndcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWQLALALIFKIVVTIFTFGMKIPSGL 374
Cdd:cd01031  263 EALGGGHGLILSLA----------------------------------GGNFSISLLLLIFVLRFIFTMLSYGSGAPGGI 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 375 FIPSMAVGAIAGRMVGIGVEQLAyhhHDWIIFrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEY 454
Cdd:cd01031  309 FAPMLALGALLGLLFGTILVQLG---PIPISA------------PATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNL 373

                        410       420
                 ....*....|....*....|....*.
gi 379643013 455 IVPLMAAAVTSKWVADAFGKEGIYEA 480
Cdd:cd01031  374 LLPLMVVCLVAYLVADLLGGKPIYEA 399
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 501-651 5.47e-46

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: 158.84  E-value: 5.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 501 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 580
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379643013 581 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 651
Cdd:cd04591   61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 62-478 8.98e-28

ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, are putative halogen ion (Cl-, Br- and I-) transport proteins found in eubacteria. They belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge.


Pssm-ID: 238506 [Multi-domain]  Cd Length: 390  Bit Score: 115.79  E-value: 8.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  62 YILWALLFA--FLAVSLVRVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 136
Cdd:cd01034   27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 137 ACCCGNFFSSLFSKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFTLR 212
Cdd:cd01034  107 GAAVMLAIGRRLPK--WGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 213 SINPFGNSRLvlfyveyHTPWyMAELFPFILLGVFGGLWGTLFIRCNIA---WCRRRKTTRLGKYPVLEVIVVTAITAII 289
Cdd:cd01034  185 NYPYFGVAAV-------ALPL-GEAWLLVLVCGVVGGLAGGLFARLLVAlssGLPGWVRRFRRRRPVLFAALCGLALALI 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 290 AYpnpytrqSTSELIselFNDcGALESSQlcdyindpnmtrpvddipdrpAGVGVYTAMWQLALAlifKIVVTIFTFGMK 369
Cdd:cd01034  257 GL-------VSGGLT---FGT-GYLQARA---------------------ALEGGGGLPLWFGLL---KFLATLLSYWSG 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 370 IPSGLFIPSMAVGAiagrmvGIG--VEQLAYHHHdwiifrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFE 447
Cdd:cd01034  302 IPGGLFAPSLAVGA------GLGslLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVME 358

                        410       420       430
                 ....*....|....*....|....*....|.
gi 379643013 448 LTGGLEYIVPLMAAAVTSKWVADAFGKEGIY 478
Cdd:cd01034  359 MTGDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
52-522 4.03e-27

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 114.60  E-value: 4.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013  52 ASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEG 131
Cdd:PRK05277  37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 132 PLVHVACCCGNFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 209
Cdd:PRK05277 115 PTVQMGGNIGRMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 210 TLRSINpfGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIA---WCRRRKTTRLGKYpVLEVIVVTAIT 286
Cdd:PRK05277 193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRW-VLMGGAVGGLC 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 287 AIIAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVVTIFTF 366
Cdd:PRK05277 268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCF 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 367 GMKIPSGLFIPSMAVGAIAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMF 446
Cdd:PRK05277 314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVL 378

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013 447 ELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 522
Cdd:PRK05277 379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
111-479 1.18e-20

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 96.35  E-value: 1.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 111 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGnffsSLFSKYSKNEGKR-REVLSAAAAAGVSVAFGAPIGGVLFSLEEVS 189
Cdd:PRK01862 119 LWRSASSLLTIGSGGSIGREGPMVQLAALAA----SLVGRFAHFDPPRlRLLVACGAAAGITSAYNAPIAGAFFVAEIVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 190 YYFPLKTLWRSFFAALVAAFTLRSinpFGNSRlVLFYVEYH---TPWymaELFPFILLGVFGGLWGTLFIRCNIAWCRRR 266
Cdd:PRK01862 195 GSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRLLDASKNQF 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 267 KTTRLGkyPVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmTRPVddipdrpagvgvyt 346
Cdd:PRK01862 268 KRLPVP--LPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILH-------------------APWT-------------- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 347 amWQ-LALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHHhdwiifrnwcrpgadCVTPGLYAMV 425
Cdd:PRK01862 313 --WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHALWPGH---------------TSAPFAYAMV 375

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 379643013 426 GAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYE 479
Cdd:PRK01862 376 GMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYE 429
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
417-652 1.53e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 75.69  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 417 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 496
Cdd:COG2524    4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 497 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 576
Cdd:COG2524   83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379643013 577 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 652
Cdd:COG2524  154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
504-657 5.82e-14

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 69.12  E-value: 5.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 504 DVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGFAQRRELILAIKNARQRQegivsnsimyft 583
Cdd:COG3448    6 DIMTR----DVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE------------ 65

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013 584 eeppelPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRqCL--VTRSGRLLGIITKKDVLRHMAQMAN 657
Cdd:COG3448   66 ------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
494-655 2.24e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 67.63  E-value: 2.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 494 DEFTHRTLATDVMRprrgEPPLSVLTQDsMTVEDVETLIKETDYNGFPVVvsRDSERLIGfaqrrelILAIKNARQRQEG 573
Cdd:COG4109   10 DTFKEILLVEDIMT----LEDVATLSED-DTVEDALELLEKTGHSRFPVV--DENGRLVG-------IVTSKDILGKDDD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 574 ivsnsimyfteeppelpansphpLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHM 652
Cdd:COG4109   76 -----------------------TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKAL 132


                 ...
gi 379643013 653 AQM 655
Cdd:COG4109  133 QKI 135
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 108-465 6.62e-12

Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) transporters found in eubacteria. They belong to the ClC superfamily of halogen ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge.


Pssm-ID: 238505 [Multi-domain]  Cd Length: 388  Bit Score: 67.70  E-value: 6.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 108 WTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNegkRREVLSAAAAAGVSVAFGAPIGGVLFSLE- 186
Cdd:cd01033   83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVAD---RRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 187 ---EVSyyfplktlWRSFFAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYmaELFPF-ILLGVFGGLWGTLFIRCNiAW 262
Cdd:cd01033  160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLST--PLLIWaLLAGPVLGVVAAGFRRLS-QA 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 263 CRRRKTTrlGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNDCGALESsqlcdyindpnmtrpvddipdrpagv 342
Cdd:cd01033  229 ARAKRPK--GKRILWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSL-------------------------- 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 343 gvytamwqLALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGIGVEQLAYHhhdwiifrnwcrpgadcVTPGLY 422
Cdd:cd01033  281 --------LLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGIVWNALLPP-----------------LSIAAF 335

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 379643013 423 AMVGAAACLGGVTRMTVSLVVIMFELTG-GLEYIVPLMAAAVTS 465
Cdd:cd01033  336 ALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS COG0517
CBS domain [Signal transduction mechanisms];
501-654 7.26e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 62.96  E-value: 7.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 501 LATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGfaqrrelilaiknarqrqegIVSNS-I 579
Cdd:COG0517    2 KVKDIMTT----DVVTV--SPDATVREALELMSEKRIGGLPVV--DEDGKLVG--------------------IVTDRdL 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013 580 MYFTEEPPELPANSPhplkLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLV-TRSGRLLGIITKKDVLRHMAQ 654
Cdd:COG0517   54 RRALAAEGKDLLDTP----VSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 512-650 2.75e-11

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: 60.72  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 512 EPPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppeLPA 591
Cdd:cd02205    2 RDVVTV--DPDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRAL------------------------VEG 53

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 592 NSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLR 650
Cdd:cd02205   54 GLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 504-655 1.05e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 56.76  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 504 DVMRprrgEPPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGFAQRRELILAIKNARqrqegivsnsimyft 583
Cdd:COG2905    3 DIMS----RDVVTV--SPDATVREAARLMTEKGVGSLVVV--DDDGRLVGIITDRDLRRRVLAEG--------------- 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 379643013 584 EEPPELPAnsphplklRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQM 655
Cdd:COG2905   60 LDPLDTPV--------SEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 522-650 1.64e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. 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: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 55.79  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 522 SMTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppelpansPHPlKLRR 601
Cdd:cd04610   11 DDTVKDVIKLIKETGHDGFPVV---DDGKVVGYVTAKDLLGKD-----------------------------DDE-KVSE 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 379643013 602 IlnLSPFTVTDHTPMeTVVDIFRKLgLRQCL-----VTRSGRLLGIITKKDVLR 650
Cdd:cd04610   58 I--MSRDTVVADPDM-DITDAARVI-FRSGIsklpvVDDEGNLVGIITNMDVIR 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 607-650 8.55e-08

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: 49.05  E-value: 8.55e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 379643013   607 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 650
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
597-653 2.03e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 50.25  E-value: 2.03e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 379643013 597 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLRHMA 653
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEdGKLVGIVTDRDLRRALA 58
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 599-653 2.44e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 47.98  E-value: 2.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013  599 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 653
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 513-650 3.20e-07

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: 49.74  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 513 PPLSVltQDSMTVEDVETLIKETDYNGFPVVvsrDSE-RLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPA 591
Cdd:cd04586    4 DVVTV--TPDTSVREAARLLLEHRISGLPVV---DDDgKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLAEEYV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 379643013 592 NSpHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 650
Cdd:cd04586   79 KA-HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
597-653 9.64e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 48.32  E-value: 9.64e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 379643013 597 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMA 653
Cdd:COG3448    2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALL 59
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 523-650 3.94e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 46.65  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 523 MTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAiknarqrqegivSNSImyFTEEPPELPANSPHPLKLRRI 602
Cdd:cd04584   17 TSLAEARELMKEHKIRHLPVV---DDGKLVGIVTDRDLLRA------------SPSK--ATSLSIYELNYLLSKIPVKDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 379643013 603 LNLSPFTVTDHTPMETVVDIFR--KLGlrqCL-VTRSGRLLGIITKKDVLR 650
Cdd:cd04584   80 MTKDVITVSPDDTVEEAALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 520-650 5.33e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 45.54  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 520 QDSMTVEDVETLIKETDYNGFPVVvsrDSE-RLIGfaqrrelILAIKNArqrqegivsnsimyfTEEPPELPansphplk 598
Cdd:cd04596    8 RETDTVRDYKQLSEETGHSRFPVV---DEEnRVVG-------IVTAKDV---------------IGKEDDTP-------- 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013 599 LRRILNLSPFTVTDHTpmeTVVDIFRKL---GLRQCLVTRSGR-LLGIITKKDVLR 650
Cdd:cd04596   55 IEKVMTKNPITVKPKT---SVASAAHMMiweGIELLPVVDENRkLLGVISRQDVLK 107
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 522-652 7.37e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 45.40  E-value: 7.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 522 SMTVEDV------ETLIKETDYNGFpvVVSRDsERLIGFAQRRELILAiknarqrqegivsnsimyfteePPELpansph 595
Cdd:cd04606   17 DWTVEEAleylrrLAPDPETIYYIY--VVDED-RRLLGVVSLRDLLLA----------------------DPDT------ 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379643013 596 plKLRRILNLSPFTVTDHTPMETVVDIFRKLGLrqcL----VTRSGRLLGIITKKDVLRHM 652
Cdd:cd04606   66 --KVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 607-656 8.36e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 45.49  E-value: 8.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 379643013 607 PFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMA 656
Cdd:cd04584   10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
595-654 2.21e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.03  E-value: 2.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 595 HPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQ 654
Cdd:COG2524   84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 124-390 4.76e-05

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: 46.03  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 124 GLSLGKEGPLVHVacccGNFFSSLFSKYSK-NEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlk 195
Cdd:cd03682   92 GGSAGREGTAVQM----GGSLADAFGRVFKlPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP-- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 196 tlwrSFFAALVAAFTLRSINPFGNSRLVLFYVEYhTPWYMAELfpfILLGVFGGLWGTLFIRCnIAWCrRRKTTRLGKYP 275
Cdd:cd03682  166 ----CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNP 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 276 VLEVIVVTAITAIIAYpnpytrqstseliselfndcgaLESSQlcDYINdpnmtRPVDDIPDRPAGVGVYTAMWqlalal 355
Cdd:cd03682  236 YLRPFVGGLLIILLVY----------------------LLGSR--RYLG-----LGTPLIEDSFFGGTVYPYDW------ 280

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 379643013 356 IFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVG 390
Cdd:cd03682  281 LLKLIFTVITLGAGFKGGEVTPLFFIGATLGNALA 315
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 502-649 7.08e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. 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: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 42.87  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 502 ATDVMRPRRgepplSVLTQD-SMTVEDVETLIKETDYNGFPvVVSRDSERLIGFAQRRELILAIKNARQrqegivsnsim 580
Cdd:cd04590    2 VREVMTPRT-----DVVALDaDATLEELLELILESGYSRFP-VYEGDLDNIIGVLHVKDLLAALLEGRE----------- 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 581 yfteeppelpansphPLKLRRILNlSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVL 649
Cdd:cd04590   65 ---------------KLDLRALLR-PPLFVPETTPLDDLLEEFRKERSHMAIVVDEyGGTAGIVTLEDIL 118
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 607-663 9.98e-05

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: 42.23  E-value: 9.98e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 379643013 607 PFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMAQMANQDPESI 663
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVdDDGKLVGIVTERDILRALVEGGLALDTPV 61
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 513-651 1.33e-04

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: 41.75  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 513 PPLSVLTQDsmTVEDVETLIKETDYNGFPVVVsrDSERLIGFAQRRELILAIKNARQRQEGIVSnSIMYftEEPPELPAN 592
Cdd:cd04608   11 APVTVLPDD--TLGEAIEIMREYGVDQLPVVD--EDGRVVGMVTEGNLLSSLLAGRAQPSDPVS-KAMY--KQFKQVDLD 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 379643013 593 SPHPlKLRRILNlspftvTDHTPMetVVDifrklglrqclvtRSGRLLGIITKKDVLRH 651
Cdd:cd04608   84 TPLG-ALSRILE------RDHFAL--VVD-------------GQGKVLGIVTRIDLLNY 120
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 111-481 6.91e-04

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 42.46  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 111 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKysKNEGKRRevLSAAAAAGVSVAFGAPIGGVLFSLEEVSY 190
Cdd:PRK01610 101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTP--RQEWKLW--IACGAAAGMASAYHAPLAGSLFIAEILFG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 191 YFPLKTLWRSFFAALVAAFTLRSINPfgnSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFIRCNIAwcRRRKTTR 270
Cdd:PRK01610 177 TLMLASLGPVVISAVVALLTTNLLNG---SDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLLLTLMNA--SHRGFVS 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 271 LGKYPVLEVIVVTAITAIIaypnpytrqstSELISELFNDCGALESSQLCDyindpnmtrpvddipdrPAGVGVytamwq 350
Cdd:PRK01610 252 LKLAPPWQLALGGLIVGLL-----------SLFTPAVWGNGYSVVQSFLTA-----------------PPLLML------ 297

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 351 LALALIFKIVVTIFTFGMKIPSGLFIPSMAVGAIAGRMVGigveqlayhhhdwIIFRNWCrPGADCVTPgLYAMVGAAAC 430
Cdd:PRK01610 298 IAGIFLCKLLAVLASSGSGAPGGVFTPTLFVGLAIGMLYG-------------RSLGLWL-PDGEEITL-LLGLTGMATL 362

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 379643013 431 LGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAH 481
Cdd:PRK01610 363 LAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLRRDSIYRQH 413
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 606-648 7.59e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 7.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 379643013 606 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 648
Cdd:PTZ00314 105 DPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 606-648 7.88e-04

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: 39.40  E-value: 7.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 379643013 606 SP-FTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDV 648
Cdd:cd04595    2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 45
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 599-663 9.63e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.43  E-value: 9.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 379643013 599 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTR-SGRLLGIITKKDVLRHMAQmANQDPESI 663
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDdDGRLVGIITDRDLRRRVLA-EGLDPLDT 65
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
581-650 1.11e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 42.13  E-value: 1.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 379643013 581 YFTEEPPELPANSpHPlKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLR 650
Cdd:PRK14869  54 YFGVEAPELIEDV-KP-QVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTlPVVDEEGKLLGLVSLSDLAR 122
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
523-659 2.67e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 40.82  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 523 MTVEDV------ETLIKETDYNGFpvVVSRDsERLIGFAQRRELILAiknarqrqegivsnsimyfteePPElpansphp 596
Cdd:COG2239  146 WTVGEAlrylrrQAEDPETIYYIY--VVDDD-GRLVGVVSLRDLLLA----------------------DPD-------- 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379643013 597 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRqCL--VTRSGRLLGIITKKDVLRHMAQMANQD 659
Cdd:COG2239  193 TKVSDIMDTDVISVPADDDQEEVARLFERYDLL-ALpvVDEEGRLVGIITVDDVVDVIEEEATED 256
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 517-565 3.58e-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: 35.95  E-value: 3.58e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 379643013   517 VLTQDSMTVEDVETLIKETDYNGFPVVVSRDseRLIGFAQRRELILAIK 565
Cdd:smart00116   3 VTVSPDTTLEEALELLRENGIRRLPVVDEEG--RLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 502-566 3.83e-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: 3.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379643013  502 ATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVVsrDSERLIGFAQRRELILAIKN 566
Cdd:pfam00571   1 VKDIMTK----DVVTV--SPDTTLEEALELMREHGISRLPVVD--EDGKLVGIVTLKDLLRALLG 57
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 599-663 6.29e-03

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 37.52  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 599 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQC----------------LVTRSGRLLGIITKKDVLRHMAQMANQDPES 662
Cdd:cd04620    1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                 .
gi 379643013 663 I 663
Cdd:cd04620   81 I 81
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 513-650 8.30e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; 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: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 36.73  E-value: 8.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379643013 513 PPLSVltQDSMTVEDVETLIKEtdYNGFPVVVSRDSERLIGFAQRRELILAIknARQRqegivsnsimyfteePPELPAn 592
Cdd:cd09836    4 PVVTV--PPETTIREAAKLMAE--NNIGSVVVVDDDGKPVGIVTERDIVRAV--AEGI---------------DLDTPV- 61

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 379643013 593 sphplklRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLR 650
Cdd:cd09836   62 -------EEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVdGGGKLVGVISIRDLAR 113
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 598-650 8.48e-03

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 36.82  E-value: 8.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 379643013 598 KLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 650
Cdd:cd04631    1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMR 53
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 616-650 9.23e-03

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 36.15  E-value: 9.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 379643013 616 METVVDIFRKLG--LRQCLVTRSGRLLGIITKKDVLR 650
Cdd:COG3620   59 VSTLEKIAEALGkeLSAVLVVDDGKLVGIITRRDLLK 95
 
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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