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Conserved domains on  [gi|1267345272|ref|NP_001344033|]
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H(+)/Cl(-) exchange transporter 4 isoform 4 [Mus musculus]

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 ...
 58-490 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: 711.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  58 NYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVA 137
Cdd:cd03684    27 NYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 138 CCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPF 217
Cdd:cd03684   107 TCVGNIISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 218 GNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTR 297
Cdd:cd03684   187 GTGRLVLFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTR 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 298 QSTSELISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIP 377
Cdd:cd03684   267 LDMTELLELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVP 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 378 SMAVGAMAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVP 457
Cdd:cd03684   334 SMAVGALFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILP 412

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1267345272 458 LMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFL 490
Cdd:cd03684   413 LMIAVMVSKWVADAIGKEGIYDAHIHLNGYPFL 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 6.38e-45

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: 155.76  E-value: 6.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 501 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 580
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345272 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 ...
 58-490 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: 711.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  58 NYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVA 137
Cdd:cd03684    27 NYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 138 CCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPF 217
Cdd:cd03684   107 TCVGNIISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 218 GNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTR 297
Cdd:cd03684   187 GTGRLVLFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTR 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 298 QSTSELISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIP 377
Cdd:cd03684   267 LDMTELLELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVP 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 378 SMAVGAMAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVP 457
Cdd:cd03684   334 SMAVGALFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILP 412

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1267345272 458 LMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFL 490
Cdd:cd03684   413 LMIAVMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 69-470 1.92e-92

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


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 289.83  E-value: 1.92e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  69 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 148
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 149 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 228
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 229 YHTPWYMAELFPFILLGVFGGLWGTLFTRCNIaWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELF 308
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 309 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRM 388
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 389 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 468
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 1267345272 469 AD 470
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
42-483 2.08e-57

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 199.98  E-value: 2.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  42 SELLLSQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVV 121
Cdd:COG0038    33 THLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 122 SSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:COG0038   111 GSGGSLGREGPSVQIGAAIGSLLGRLL-RLSPED--RRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 202 FAALVAAFTLRSInpFGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCnIAWCRRRkTTRLGRYPVLEVIA 281
Cdd:COG0038   188 IASVVAYLVSRLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAI 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 282 VTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVI 361
Cdd:COG0038   262 GGLLVGLLGLFLPQVLGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 362 TIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:COG0038   308 TALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG---------------LSPGLFALVGMAAVFAAVTRAPLTA 372

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1267345272 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 6.38e-45

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: 155.76  E-value: 6.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 501 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 580
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345272 581 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 651
Cdd:cd04591    61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
39-522 9.15e-28

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 116.53  E-value: 9.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  39 QKWSELLLSQSEGAsaYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLV 118
Cdd:PRK05277   26 QNQRLGLLASVADN--GLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 119 LVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKT 196
Cdd:PRK05277  102 GTLGSGMVLGREGPTVQMGGNIGRMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLIS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 197 LWRSFFAALVAAFTLRSINpfGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIA---WCRRRKTTRLGR 273
Cdd:PRK05277  180 IKAVFIGVIMATIVFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKR 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 274 YpVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLAL 353
Cdd:PRK05277  256 W-VLMGGAVGGLCGLLGLLAPAAVGGGFNLIPIALA---------------------------------GNF-SIGMLLF 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 354 ALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGG 433
Cdd:PRK05277  301 IFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAA 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 434 VTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEP 513
Cdd:PRK05277  366 TVRAPLTGIVLVLEMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARS 429


                  ....*....
gi 1267345272 514 PLSVLTQDS 522
Cdd:PRK05277  430 KAAPASENT 438
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
417-652 5.71e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 74.15  E-value: 5.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 417 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 496
Cdd:COG2524     4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 497 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 576
Cdd:COG2524    83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267345272 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 6.31e-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: 49.43  E-value: 6.31e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1267345272  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 1.84e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 48.36  E-value: 1.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345272 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 1267345272 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 ...
 58-490 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: 711.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  58 NYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVA 137
Cdd:cd03684    27 NYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 138 CCCGNFFSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPF 217
Cdd:cd03684   107 TCVGNIISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPF 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 218 GNSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTR 297
Cdd:cd03684   187 GTGRLVLFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTR 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 298 QSTSELISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIP 377
Cdd:cd03684   267 LDMTELLELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVP 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 378 SMAVGAMAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVP 457
Cdd:cd03684   334 SMAVGALFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILP 412

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1267345272 458 LMAAAVTSKWVADAFGKEGIYEAHIHLNGYPFL 490
Cdd:cd03684   413 LMIAVMVSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 39-479 1.15e-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: 1.15e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  39 QKWSELLLSQSEGasaYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLV 118
Cdd:cd01036    20 DAGQWLLRRIPGS---YLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 119 LVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYS----------KNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV 188
Cdd:cd01036    97 CAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEV 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 189 SYYFPLKTLWRSFFAALVAAFTLRSINPFGNSR----------LVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRC 258
Cdd:cd01036   177 STFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRL 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 259 NIAWCRRR---KTTRLGRYPVLEVIAVTAVTAIVAYPnpytrqstseliselfndcgalessqlcdyindpnmtrpvddi 335
Cdd:cd01036   257 SIIFLRWRrrlLFRKTARYRVLEPVLFTLIYSTIHYA------------------------------------------- 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 336 pdrpagvgvytamWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHDwiifrnwCRPGAD 415
Cdd:cd01036   294 -------------PTLLLFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATL 353

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267345272 416 CVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYE 479
Cdd:cd01036   354 WADPGVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 69-470 1.92e-92

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


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 289.83  E-value: 1.92e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  69 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 148
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 149 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 228
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 229 YHTPWYMAELFPFILLGVFGGLWGTLFTRCNIaWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELF 308
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 309 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRM 388
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 389 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 468
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 1267345272 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. ...
 55-490 1.25e-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: 289.55  E-value: 1.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  55 YILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLV 134
Cdd:cd03685    74 LFTAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 135 HVACCCGNFFSSLFSK----------YSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAA 204
Cdd:cd03685   154 HIGACIAAGLSQGGSTslrldfrwfrYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSS 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 205 LVAAFTLRSINPFGNSR---------LVLFYVeYHTP--WYMAELFPFILLGVFGGLWGTLFTRCN--IAWCRRRKTTRL 271
Cdd:cd03685   234 MIVTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNhkVTRFRKRINHKG 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 272 GRYPVLEVIAVTAVTAIVAYpnpytrqstseliselfndcgalessqlcdyindpnmtrpvddipdrpagvgvytaMWQL 351
Cdd:cd03685   313 KLLKVLEALLVSLVTSVVAF--------------------------------------------------------PQTL 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 352 ALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLayhhhdwiifrnwcrPGADCVTPGLYAMVGAAACL 431
Cdd:cd03685   337 LIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSY---------------FGFTSIDPGLYALLGAAAFL 401

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267345272 432 GGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFgKEGIYEAHIHLNGYPFL 490
Cdd:cd03685   402 GGVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-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 2.96e-79

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: 258.33  E-value: 2.96e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  54 AYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPL 133
Cdd:cd03683    40 NSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 134 VHVACCCGNFFSSL---FSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFT 210
Cdd:cd03683   120 VHISSIVAALLSKLttfFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFT 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 211 LRSINPF---GNSRLVLFYVEYHT--PWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTR-----LGRYPVLEVI 280
Cdd:cd03683   200 FRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRlfskfLKRSPLLYPA 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 281 AVTAVTAIVAYPnpytrqstseliselfndcgalessqlcdYINdpnmtrpvddipdrpagvgvytamwqLALALIFKIV 360
Cdd:cd03683   280 IVALLTAVLTFP-----------------------------FLT--------------------------LFLFIVVKFV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 361 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGigvEQLAYHHHDWIIfrnwcRPGADCVTPGLYAMVGAAACLGGVTRmTVS 440
Cdd:cd03683   305 LTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAVLFPEGIR-----GGISNPIGPGGYAVVGAAAFSGAVTH-TVS 375

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267345272 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 ...
 43-465 1.05e-59

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


Pssm-ID: 238233 [Multi-domain]  Cd Length: 383  Bit Score: 205.11  E-value: 1.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  43 ELLLSQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLLIKTVTLVLVV 121
Cdd:cd00400    20 NLLFGGLPGELAAGSLSPLYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 122 SSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:cd00400    97 GSGGSVGREGPIVQIGAAIGSWLGRRL-RLSRND--RRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 202 FAALVAAFTLRSINPFGNsrlvLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKttRLGRYPVLEVIA 281
Cdd:cd00400   174 LASVAAALVSRLLFGAEP----AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPAL 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 282 VTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvgVYTAMWQLALALIFKIVI 361
Cdd:cd00400   248 GGLLLGLLGLFLPQVLGSGYGAILLALA----------------------------------GELSLLLLLLLLLLKLLA 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 362 TIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:cd00400   294 TALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALFPGLV---------------ASPGAYALVGMAALLAAVLRAPLTA 358

                         410       420
                  ....*....|....*....|....
gi 1267345272 442 VVIMFELTGGLEYIVPLMAAAVTS 465
Cdd:cd00400   359 ILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
42-483 2.08e-57

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 199.98  E-value: 2.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  42 SELLLSQSEGASAYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVV 121
Cdd:COG0038    33 THLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 122 SSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSF 201
Cdd:COG0038   111 GSGGSLGREGPSVQIGAAIGSLLGRLL-RLSPED--RRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 202 FAALVAAFTLRSInpFGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCnIAWCRRRkTTRLGRYPVLEVIA 281
Cdd:COG0038   188 IASVVAYLVSRLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAI 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 282 VTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVI 361
Cdd:COG0038   262 GGLLVGLLGLFLPQVLGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 362 TIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSL 441
Cdd:COG0038   308 TALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG---------------LSPGLFALVGMAAVFAAVTRAPLTA 372

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1267345272 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 1.08e-46

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: 170.03  E-value: 1.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  57 LNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 136
Cdd:cd01031    35 PLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQI 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 137 ACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINP 216
Cdd:cd01031   113 GAAIGQGVSKWF-KTSPEE--RRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 217 FGnsrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRcNIAWCRR--RKTTRLGRYpvLEVIAVTAVTAIVAYPNP 294
Cdd:cd01031   190 LG----PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNR-SLLKSQDlyRKLKKLPRE--LRVLLPGLLIGPLGLLLP 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 295 YTRQSTSELISELFndcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWQLALALIFKIVITIFTFGMKIPSGL 374
Cdd:cd01031   263 EALGGGHGLILSLA----------------------------------GGNFSISLLLLIFVLRFIFTMLSYGSGAPGGI 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 375 FIPSMAVGAMAGRMVGIGVEQLAyhhHDWIIFrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEY 454
Cdd:cd01031   309 FAPMLALGALLGLLFGTILVQLG---PIPISA------------PATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNL 373

                         410       420
                  ....*....|....*....|....*.
gi 1267345272 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 6.38e-45

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: 155.76  E-value: 6.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 501 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 580
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345272 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 6.00e-28

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


Pssm-ID: 238506 [Multi-domain]  Cd Length: 390  Bit Score: 116.17  E-value: 6.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  62 YILWALLFA--FLAVSLVRVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 136
Cdd:cd01034    27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 137 ACCCGNFFSSLFSKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFTLR 212
Cdd:cd01034   107 GAAVMLAIGRRLPK--WGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 213 SINPFGNSRLvlfyveyHTPWyMAELFPFILLGVFGGLWGTLFTRCNIA---WCRRRKTTRLGRYPVLEVIAVTAVTAIV 289
Cdd:cd01034   185 NYPYFGVAAV-------ALPL-GEAWLLVLVCGVVGGLAGGLFARLLVAlssGLPGWVRRFRRRRPVLFAALCGLALALI 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 290 AYpnpytrqSTSELIselFNDcGALESSQlcdyindpnmtrpvddipdrpAGVGVYTAMWQLALAlifKIVITIFTFGMK 369
Cdd:cd01034   257 GL-------VSGGLT---FGT-GYLQARA---------------------ALEGGGGLPLWFGLL---KFLATLLSYWSG 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 370 IPSGLFIPSMAVGAmagrmvGIG--VEQLAYHHHdwiifrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFE 447
Cdd:cd01034   302 IPGGLFAPSLAVGA------GLGslLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVME 358

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1267345272 448 LTGGLEYIVPLMAAAVTSKWVADAFGKEGIY 478
Cdd:cd01034   359 MTGDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
39-522 9.15e-28

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 116.53  E-value: 9.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272  39 QKWSELLLSQSEGAsaYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLV 118
Cdd:PRK05277   26 QNQRLGLLASVADN--GLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 119 LVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKT 196
Cdd:PRK05277  102 GTLGSGMVLGREGPTVQMGGNIGRMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLIS 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 197 LWRSFFAALVAAFTLRSINpfGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIA---WCRRRKTTRLGR 273
Cdd:PRK05277  180 IKAVFIGVIMATIVFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKR 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 274 YpVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLAL 353
Cdd:PRK05277  256 W-VLMGGAVGGLCGLLGLLAPAAVGGGFNLIPIALA---------------------------------GNF-SIGMLLF 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 354 ALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGG 433
Cdd:PRK05277  301 IFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAA 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 434 VTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEP 513
Cdd:PRK05277  366 TVRAPLTGIVLVLEMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARS 429


                  ....*....
gi 1267345272 514 PLSVLTQDS 522
Cdd:PRK05277  430 KAAPASENT 438
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
111-479 2.33e-19

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 92.12  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 111 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGnffsSLFSKYSKNEGKR-REVLSAAAAAGVSVAFGAPIGGVLFSLEEVS 189
Cdd:PRK01862  119 LWRSASSLLTIGSGGSIGREGPMVQLAALAA----SLVGRFAHFDPPRlRLLVACGAAAGITSAYNAPIAGAFFVAEIVL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 190 YYFPLKTLWRSFFAALVAAFTLRSinpFGNSRlVLFYVEYH---TPWymaELFPFILLGVFGGLWGTLFTRCNIAWCRRR 266
Cdd:PRK01862  195 GSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRLLDASKNQF 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 267 KTTRLGryPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmTRPVddipdrpagvgvyt 346
Cdd:PRK01862  268 KRLPVP--LPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILH-------------------APWT-------------- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 347 amWQ-LALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHhdwiifrnwcrpgadCVTPGLYAMV 425
Cdd:PRK01862  313 --WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHALWPGH---------------TSAPFAYAMV 375

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267345272 426 GAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYE 479
Cdd:PRK01862  376 GMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYE 429
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
417-652 5.71e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 74.15  E-value: 5.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 417 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 496
Cdd:COG2524     4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 497 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 576
Cdd:COG2524    83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267345272 577 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 652
Cdd:COG2524   154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
504-657 1.62e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.97  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 504 DVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGFAQRRELILAIKNARQRQegivsnsimyft 583
Cdd:COG3448     6 DIMTR----DVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE------------ 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345272 584 eeppelPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRqCL--VTRSGRLLGIITKKDVLRHMAQMAN 657
Cdd:COG3448    66 ------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
494-655 6.55e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 66.09  E-value: 6.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 494 DEFTHRTLATDVMRprrgEPPLSVLTQDsMTVEDVETLIKETDYNGFPVLvsRDSERLIGfaqrrelILAIKNARQRQEG 573
Cdd:COG4109    10 DTFKEILLVEDIMT----LEDVATLSED-DTVEDALELLEKTGHSRFPVV--DENGRLVG-------IVTSKDILGKDDD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 574 ivsnsimyfteeppelpansphpLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHM 652
Cdd:COG4109    76 -----------------------TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKAL 132


                  ...
gi 1267345272 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 5.29e-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: 68.09  E-value: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 108 WTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNegkRREVLSAAAAAGVSVAFGAPIGGVLFSLE- 186
Cdd:cd01033    83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVAD---RRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 187 ---EVSyyfplktlWRSFFAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFI---LLGVFGGLWGTLFTRcni 260
Cdd:cd01033   160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTPLLIWALLagpVLGVVAAGFRRLSQA--- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 261 AWCRRRKTTRLgrypVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFNDCGALESsqlcdyindpnmtrpvddipdrpa 340
Cdd:cd01033   229 ARAKRPKGKRI----LWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSL------------------------ 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 341 gvgvytamwqLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHhhdwiifrnwcrpgadcVTPG 420
Cdd:cd01033   281 ----------LLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGIVWNALLPP-----------------LSIA 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1267345272 421 LYAMVGAAACLGGVTRMTVSLVVIMFELTG-GLEYIVPLMAAAVTS 465
Cdd:cd01033   334 AFALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS COG0517
CBS domain [Signal transduction mechanisms];
501-654 3.88e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 61.03  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 501 LATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGfaqrrelilaiknarqrqegIVSNS-I 579
Cdd:COG0517     2 KVKDIMTT----DVVTV--SPDATVREALELMSEKRIGGLPVV--DEDGKLVG--------------------IVTDRdL 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345272 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 1.18e-10

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 59.18  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 512 EPPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppeLPA 591
Cdd:cd02205     2 RDVVTV--DPDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRAL------------------------VEG 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 592 NSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLR 650
Cdd:cd02205    54 GLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 504-655 2.35e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 55.61  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 504 DVMRprrgEPPLSVltQDSMTVEDVETLIKETDYNGfpVLVSRDSERLIGFAQRRELILAIKNARqrqegivsnsimyft 583
Cdd:COG2905     3 DIMS----RDVVTV--SPDATVREAARLMTEKGVGS--LVVVDDDGRLVGIITDRDLRRRVLAEG--------------- 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267345272 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 3.02e-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: 55.02  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 522 SMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppelpansPHPlKLRR 601
Cdd:cd04610    11 DDTVKDVIKLIKETGHDGFPVV---DDGKVVGYVTAKDLLGKD-----------------------------DDE-KVSE 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267345272 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 6.31e-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: 49.43  E-value: 6.31e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1267345272  607 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 650
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
597-653 1.81e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 50.25  E-value: 1.81e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267345272 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 1.84e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 48.36  E-value: 1.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345272 599 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 653
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
597-653 8.84e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 48.71  E-value: 8.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267345272 597 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMA 653
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALL 59
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 513-650 1.23e-06

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: 48.19  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 513 PPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSE-RLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPA 591
Cdd:cd04586     4 DVVTV--TPDTSVREAARLLLEHRISGLPVV---DDDgKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLAEEYV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267345272 592 NSpHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 650
Cdd:cd04586    79 KA-HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 607-656 7.89e-06

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 45.88  E-value: 7.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267345272 607 PFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMA 656
Cdd:cd04584    10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 523-650 1.48e-05

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: 44.72  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 523 MTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAiknarqrqegivSNSImyFTEEPPELPANSPHPLKLRRI 602
Cdd:cd04584    17 TSLAEARELMKEHKIRHLPVV---DDGKLVGIVTDRDLLRA------------SPSK--ATSLSIYELNYLLSKIPVKDI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1267345272 603 LNLSPFTVTDHTPMETVVDIFR--KLGlrqCL-VTRSGRLLGIITKKDVLR 650
Cdd:cd04584    80 MTKDVITVSPDDTVEEAALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
595-654 1.89e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.03  E-value: 1.89e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 595 HPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQ 654
Cdd:COG2524    84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 520-650 3.68e-05

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: 43.23  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 520 QDSMTVEDVETLIKETDYNGFPVLvsrDSE-RLIGfaqrrelILAIKNArqrqegivsnsimyfTEEPPELPansphplk 598
Cdd:cd04596     8 RETDTVRDYKQLSEETGHSRFPVV---DEEnRVVG-------IVTAKDV---------------IGKEDDTP-------- 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345272 599 LRRILNLSPFTVTDHTpmeTVVDIFRKL---GLRQCLVTRSGR-LLGIITKKDVLR 650
Cdd:cd04596    55 IEKVMTKNPITVKPKT---SVASAAHMMiweGIELLPVVDENRkLLGVISRQDVLK 107
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 502-649 5.78e-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: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 502 ATDVMRPRRgepplSVLTQD-SMTVEDVETLIKETDYNGFPVlVSRDSERLIGFAQRRELILAIKNARQrqegivsnsim 580
Cdd:cd04590     2 VREVMTPRT-----DVVALDaDATLEELLELILESGYSRFPV-YEGDLDNIIGVLHVKDLLAALLEGRE----------- 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 581 yfteeppelpansphPLKLRRILNlSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVL 649
Cdd:cd04590    65 ---------------KLDLRALLR-PPLFVPETTPLDDLLEEFRKERSHMAIVVDEyGGTAGIVTLEDIL 118
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 522-652 7.43e-05

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


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 42.71  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 522 SMTVEDV------ETLIKETDYNGFpvlVSRDSERLIGFAQRRELILAiknarqrqegivsnsimyfteePPELpansph 595
Cdd:cd04606    17 DWTVEEAleylrrLAPDPETIYYIY---VVDEDRRLLGVVSLRDLLLA----------------------DPDT------ 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345272 596 plKLRRILNLSPFTVTDHTPMETVVDIFRKLGLrqcL----VTRSGRLLGIITKKDVLRHM 652
Cdd:cd04606    66 --KVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 607-663 8.23e-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: 8.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267345272 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 2.55e-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: 40.98  E-value: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 513 PPLSVLTQDsmTVEDVETLIKETDYNGFPVLVsrDSERLIGFAQRRELILAIKNARQRQEGIVSnSIMYftEEPPELPAN 592
Cdd:cd04608    11 APVTVLPDD--TLGEAIEIMREYGVDQLPVVD--EDGRVVGMVTEGNLLSSLLAGRAQPSDPVS-KAMY--KQFKQVDLD 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267345272 593 SPHPlKLRRILNlspftvTDHTPMetVVDifrklglrqclvtRSGRLLGIITKKDVLRH 651
Cdd:cd04608    84 TPLG-ALSRILE------RDHFAL--VVD-------------GQGKVLGIVTRIDLLNY 120
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 606-648 6.55e-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: 39.79  E-value: 6.55e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1267345272 606 SP-FTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDV 648
Cdd:cd04595     2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 45
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 1267345272 606 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 648
Cdd:PTZ00314  105 DPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 599-663 8.58e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.81  E-value: 8.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345272 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 1267345272 581 YFTEEPPELPANSpHPlKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLR 650
Cdd:PRK14869   54 YFGVEAPELIEDV-KP-QVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTlPVVDEEGKLLGLVSLSDLAR 122
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 111-255 1.67e-03

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 41.30  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 111 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKysKNEGKRRevLSAAAAAGVSVAFGAPIGGVLFSLEEVSY 190
Cdd:PRK01610  101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTP--RQEWKLW--IACGAAAGMASAYHAPLAGSLFIAEILFG 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267345272 191 YFPLKTLWRSFFAALVAAFTLRSINPfgnSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLF 255
Cdd:PRK01610  177 TLMLASLGPVVISAVVALLTTNLLNG---SDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLL 238
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 124-390 1.69e-03

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


Pssm-ID: 239654 [Multi-domain]  Cd Length: 378  Bit Score: 41.02  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 124 GLSLGKEGPLVHVacccGNFFSSLFSKYSK-NEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlk 195
Cdd:cd03682    92 GGSAGREGTAVQM----GGSLADAFGRVFKlPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP-- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 196 tlwrSFFAALVAAFTLRSINPFGNSRLVLFYVEYhTPWYMAELfpfILLGVFGGLWGTLFTRCnIAWCrRRKTTRLGRYP 275
Cdd:cd03682   166 ----CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNP 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 276 VLEVIAVTAVTAIVAYpnpytrqstseliselfndcgaLESSQlcDYINdpnmtRPVDDIPDRPAGVGVYTAMWqlalal 355
Cdd:cd03682   236 YLRPFVGGLLIILLVY----------------------LLGSR--RYLG-----LGTPLIEDSFFGGTVYPYDW------ 280

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1267345272 356 IFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVG 390
Cdd:cd03682   281 LLKLIFTVITLGAGFKGGEVTPLFFIGATLGNALA 315
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 6.11e-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: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 599 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQC----------------LVTRSGRLLGIITKKDVLRHMAQMANQDPES 662
Cdd:cd04620     1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                  .
gi 1267345272 663 I 663
Cdd:cd04620    81 I 81
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
523-659 7.11e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 39.28  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345272 523 MTVEDVETLIKE-------TDYngfpVLVSRDSERLIGFAQRRELILAiknarqrqegivsnsimyfteePPElpansph 595
Cdd:COG2239   146 WTVGEALRYLRRqaedpetIYY----IYVVDDDGRLVGVVSLRDLLLA----------------------DPD------- 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345272 596 pLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRqCL--VTRSGRLLGIITKKDVLRHMAQMANQD 659
Cdd:COG2239   193 -TKVSDIMDTDVISVPADDDQEEVARLFERYDLL-ALpvVDEEGRLVGIITVDDVVDVIEEEATED 256
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 598-650 7.63e-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: 37.21  E-value: 7.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1267345272 598 KLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 650
Cdd:cd04631     1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMR 53
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 616-650 8.96e-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: 8.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1267345272 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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