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Conserved domains on  [gi|1267345244|ref|NP_001344032|]
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H(+)/Cl(-) exchange transporter 4 isoform 1 [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|GO:0055085
PubMed:  11182894|9207144|9046241
SCOP:  4003598

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 65-571 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: 727.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  65 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 144
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 225 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 304
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 305 LFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSEL 384
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 385 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 464
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 465 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 544
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                         490       500
                  ....*....|....*....|....*..
gi 1267345244 545 TSKWVADAFGKEGIYEAHIHLNGYPFL 571
Cdd:cd03684   419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 582-732 1.05e-44

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


:

Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 155.76  E-value: 1.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 582 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 661
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345244 662 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 732
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 ...
 65-571 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: 727.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  65 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 144
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 225 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 304
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 305 LFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSEL 384
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 385 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 464
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 465 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 544
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                         490       500
                  ....*....|....*....|....*..
gi 1267345244 545 TSKWVADAFGKEGIYEAHIHLNGYPFL 571
Cdd:cd03684   419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 150-551 9.56e-93

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


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 292.91  E-value: 9.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 150 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 229
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 230 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 309
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 310 YHTPWYMAELFPFILLGVFGGLWGTLFTRCNIaWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELF 389
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 390 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRM 469
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 470 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 549
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 1267345244 550 AD 551
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
58-564 4.25e-58

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 203.06  E-value: 4.25e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  58 WVVMLLIGLLAGTLAGVIDLAVDWMTDLkegvclsafwysheqccwtsnettfedrdkcplwqkwseLLLSQSEGASAYI 137
Cdd:COG0038     8 LLLAVLVGILAGLAAVLFRLLLELATHL---------------------------------------FLGGLLSAAGSHL 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 138 LNYLmYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:COG0038    49 PPWL-VLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQI 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 218 ACCCGNFFSSLFsKYSKNEgkRREVLSaaaaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInp 297
Cdd:COG0038   126 GAAIGSLLGRLL-RLSPED--RRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL-- 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 298 FGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCnIAWCRRRkTTRLGRYPVLEVIAVTAVTAIVAYPNPYT 377
Cdd:COG0038   201 FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQV 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 378 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVITIFTFGMKIPSGLFI 457
Cdd:COG0038   277 LGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFA 322

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 458 PSMAVGAMAGRMVGIGVEQLAyhhhdwiifrnwcrPGADcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 537
Cdd:COG0038   323 PSLFIGALLGAAFGLLLNLLF--------------PGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLL 387

                         490       500
                  ....*....|....*....|....*..
gi 1267345244 538 PLMAAAVTSKWVADAFGKEGIYEAHIH 564
Cdd:COG0038   388 PLMIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 582-732 1.05e-44

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 155.76  E-value: 1.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 582 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 661
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345244 662 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 732
Cdd:cd04591    61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
63-603 1.79e-29

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 121.92  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  63 LIGLLAGTLAGVIDLAVDWMtdlkegvclsafwysheqccwtsnettfedrdkcplwQKWSELLLSQSEGAsaYILNYLM 142
Cdd:PRK05277    6 VVGTLTGLVGVAFELAVDWV-------------------------------------QNQRLGLLASVADN--GLLLWIV 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 143 YILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCG 222
Cdd:PRK05277   47 AFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIG 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 223 NFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFTLRSINpfGN 300
Cdd:PRK05277  125 RMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN--GE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 301 SrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIA---WCRRRKTTRLGRYpVLEVIAVTAVTAIVAYPNPYT 377
Cdd:PRK05277  201 Q--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRW-VLMGGAVGGLCGLLGLLAPAA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 378 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVITIFTFGMKIPSGLFI 457
Cdd:PRK05277  278 VGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCFGSGAPGGIFA 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 458 PSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 537
Cdd:PRK05277  324 PMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLIL 388

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 538 PLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 603
Cdd:PRK05277  389 PLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
498-733 9.72e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 73.76  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 498 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 577
Cdd:COG2524     4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 578 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 657
Cdd:COG2524    83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267345244 658 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 733
Cdd:COG2524   154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 688-731 8.62e-08

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 49.05  E-value: 8.62e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1267345244  688 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 731
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 680-734 2.77e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 47.98  E-value: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 680 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 734
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 687-729 8.79e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 8.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1267345244 687 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 729
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 ...
 65-571 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: 727.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  65 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 144
Cdd:cd03684     1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd03684    33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 225 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 304
Cdd:cd03684   113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 305 LFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSEL 384
Cdd:cd03684   193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 385 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 464
Cdd:cd03684   273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 465 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 544
Cdd:cd03684   340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                         490       500
                  ....*....|....*....|....*..
gi 1267345244 545 TSKWVADAFGKEGIYEAHIHLNGYPFL 571
Cdd:cd03684   419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 65-560 3.86e-138

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: 413.28  E-value: 3.86e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  65 GLLAGTLAGVIDLAVDWMTDLKEGVCLSAFwysheqccwtsnettfedrdkcplwqkwselllsqsegaSAYILNYLMYI 144
Cdd:cd01036     1 GLLMGLVAVVLDYAVESSLDAGQWLLRRIP---------------------------------------GSYLLGYLMWV 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd01036    42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 225 FSSLFSKYS----------KNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRS 294
Cdd:cd01036   122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 295 INPFGNSR----------LVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRR---KTTRLGRYPVLEVI 361
Cdd:cd01036   202 YNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRrrlLFRKTARYRVLEPV 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 362 AVTAVTAIVAYPnpytrqstseliselfndcgalessqlcdyindpnmtrpvddipdrpagvgvytamWQLALALIFKIV 441
Cdd:cd01036   282 LFTLIYSTIHYA--------------------------------------------------------PTLLLFLLIYFW 305

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 442 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHDwiifrnwCRPGADCVTPGLYAMVGAAACLGGVTRMTVS 521
Cdd:cd01036   306 MSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRLTFS 378

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1267345244 522 LVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYE 560
Cdd:cd01036   379 ICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 58-571 2.81e-94

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: 301.11  E-value: 2.81e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  58 WVVMLLIGLLAGTLAGVIDLAVDWMTDLKegvcLSAFWYSHEQCCwtsnettfedrdkcplwqkwselllsqsegasaYI 137
Cdd:cd03685    33 WIICLLIGIFTGLVAYFIDLAVENLAGLK----FLVVKNYIEKGR---------------------------------LF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 138 LNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:cd03685    76 TAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 218 ACCCGNFFSSLFSK----------YSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALV 287
Cdd:cd03685   156 GACIAAGLSQGGSTslrldfrwfrYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 288 AAFTLRSINPFGNSR---------LVLFYVeYHTP--WYMAELFPFILLGVFGGLWGTLFTRCN--IAWCRRRKTTRLGR 354
Cdd:cd03685   236 VTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNhkVTRFRKRINHKGKL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 355 YPVLEVIAVTAVTAIVAYpnpytrqstseliselfndcgalessqlcdyindpnmtrpvddipdrpagvgvytaMWQLAL 434
Cdd:cd03685   315 LKVLEALLVSLVTSVVAF--------------------------------------------------------PQTLLI 338

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 435 ALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLayhhhdwiifrnwcrPGADCVTPGLYAMVGAAACLGG 514
Cdd:cd03685   339 FFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSY---------------FGFTSIDPGLYALLGAAAFLGG 403

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1267345244 515 VTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFgKEGIYEAHIHLNGYPFL 571
Cdd:cd03685   404 VMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 150-551 9.56e-93

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


Pssm-ID: 425802 [Multi-domain]  Cd Length: 344  Bit Score: 292.91  E-value: 9.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 150 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 229
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 230 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 309
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 310 YHTPWYMAELFPFILLGVFGGLWGTLFTRCNIaWCRRRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELF 389
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 390 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRM 469
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 470 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 549
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 1267345244 550 AD 551
Cdd:pfam00654 343 SR 344
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 135-571 1.89e-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: 261.03  E-value: 1.89e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 135 AYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPL 214
Cdd:cd03683    40 NSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 215 VHVACCCGNFFSSL---FSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFT 291
Cdd:cd03683   120 VHISSIVAALLSKLttfFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFT 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 292 LRSINPF---GNSRLVLFYVEYHT--PWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKTTR-----LGRYPVLEVI 361
Cdd:cd03683   200 FRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRlfskfLKRSPLLYPA 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 362 AVTAVTAIVAYPnpytrqstseliselfndcgalessqlcdYINdpnmtrpvddipdrpagvgvytamwqLALALIFKIV 441
Cdd:cd03683   280 IVALLTAVLTFP-----------------------------FLT--------------------------LFLFIVVKFV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 442 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGigvEQLAYHHHDWIIfrnwcRPGADCVTPGLYAMVGAAACLGGVTRmTVS 521
Cdd:cd03683   305 LTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAVLFPEGIR-----GGISNPIGPGGYAVVGAAAFSGAVTH-TVS 375

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267345244 522 LVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYEAHIHLNGYPFL 571
Cdd:cd03683   376 VAVIIFELTGQISHLLPVLIAVLISNAVAQFLQ-PSIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 118-546 7.41e-60

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


Pssm-ID: 238233 [Multi-domain]  Cd Length: 383  Bit Score: 207.03  E-value: 7.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 118 LWQKWSELLLSQSEGASAYILNYL-MYILWALLFAFLAVSLVRVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLLIKT 195
Cdd:cd00400    13 LLIELLQNLLFGGLPGELAAGSLSpLYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 196 VTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPL 275
Cdd:cd00400    90 LASALTLGSGGSVGREGPIVQIGAAIGSWLGRRL-RLSRND--RRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 276 KTLWRSFFAALVAAFTLRSINPFGNsrlvLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIAWCRRRKttRLGRY 355
Cdd:cd00400   167 ASLIPVLLASVAAALVSRLLFGAEP----AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 356 PVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvgVYTAMWQLALA 435
Cdd:cd00400   241 PWLRPALGGLLLGLLGLFLPQVLGSGYGAILLALA----------------------------------GELSLLLLLLL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 436 LIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGV 515
Cdd:cd00400   287 LLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALFPGLV---------------ASPGAYALVGMAALLAAV 351

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1267345244 516 TRMTVSLVVIMFELTGGLEYIVPLMAAAVTS 546
Cdd:cd00400   352 LRAPLTAILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
58-564 4.25e-58

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 203.06  E-value: 4.25e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  58 WVVMLLIGLLAGTLAGVIDLAVDWMTDLkegvclsafwysheqccwtsnettfedrdkcplwqkwseLLLSQSEGASAYI 137
Cdd:COG0038     8 LLLAVLVGILAGLAAVLFRLLLELATHL---------------------------------------FLGGLLSAAGSHL 48

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 138 LNYLmYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:COG0038    49 PPWL-VLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQI 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 218 ACCCGNFFSSLFsKYSKNEgkRREVLSaaaaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInp 297
Cdd:COG0038   126 GAAIGSLLGRLL-RLSPED--RRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL-- 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 298 FGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCnIAWCRRRkTTRLGRYPVLEVIAVTAVTAIVAYPNPYT 377
Cdd:COG0038   201 FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQV 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 378 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVITIFTFGMKIPSGLFI 457
Cdd:COG0038   277 LGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFA 322

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 458 PSMAVGAMAGRMVGIGVEQLAyhhhdwiifrnwcrPGADcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 537
Cdd:COG0038   323 PSLFIGALLGAAFGLLLNLLF--------------PGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLL 387

                         490       500
                  ....*....|....*....|....*..
gi 1267345244 538 PLMAAAVTSKWVADAFGKEGIYEAHIH 564
Cdd:COG0038   388 PLMIACVIAYLVSRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 64-561 1.22e-48

ClC chloride channel EriC. This domain is found in the EriC chloride transporters that mediate the extreme acid resistance response in eubacteria and archaea. This response allows bacteria to survive in the acidic environments by decarboxylation-linked proton utilization. As shown for Escherichia coli EriC, these channels can counterbalance the electric current produced by the outwardly directed virtual proton pump linked to amino acid decarboxylation. The EriC proteins belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge. In Escherichia coli EriC, a glutamate residue that protrudes into the pore is thought to participate in gating by binding to a Cl- ion site within the selectivity filter.


Pssm-ID: 238504 [Multi-domain]  Cd Length: 402  Bit Score: 176.58  E-value: 1.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  64 IGLLAGTLAGVIDLAVDWMTDLKEgvclsaFWYSHeqccwtsnettfedrdkcplwqkwselllsqsegASAYILNYLMY 143
Cdd:cd01031     1 IGLLAGLVAVLFRLGIDKLGNLRL------SLYDF----------------------------------AANNPPLLLVL 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 144 ILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGN 223
Cdd:cd01031    41 PLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQ 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 224 FFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGnsrl 303
Cdd:cd01031   119 GVSKWF-KTSPEE--RRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG---- 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 304 VLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRcNIAWCRR--RKTTRLGRYpvLEVIAVTAVTAIVAYPNPYTRQST 381
Cdd:cd01031   192 PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNR-SLLKSQDlyRKLKKLPRE--LRVLLPGLLIGPLGLLLPEALGGG 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 382 SELISELFndcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMA 461
Cdd:cd01031   269 HGLILSLA----------------------------------GGNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLA 314

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 462 VGAMAGRMVGIGVEQLAyhhHDWIIFrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMA 541
Cdd:cd01031   315 LGALLGLLFGTILVQLG---PIPISA------------PATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMV 379

                         490       500
                  ....*....|....*....|
gi 1267345244 542 AAVTSKWVADAFGKEGIYEA 561
Cdd:cd01031   380 VCLVAYLVADLLGGKPIYEA 399
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 582-732 1.05e-44

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 155.76  E-value: 1.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 582 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 661
Cdd:cd04591     1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345244 662 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 732
Cdd:cd04591    61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
63-603 1.79e-29

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 121.92  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244  63 LIGLLAGTLAGVIDLAVDWMtdlkegvclsafwysheqccwtsnettfedrdkcplwQKWSELLLSQSEGAsaYILNYLM 142
Cdd:PRK05277    6 VVGTLTGLVGVAFELAVDWV-------------------------------------QNQRLGLLASVADN--GLLLWIV 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 143 YILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCG 222
Cdd:PRK05277   47 AFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIG 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 223 NFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFTLRSINpfGN 300
Cdd:PRK05277  125 RMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN--GE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 301 SrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLFTRCNIA---WCRRRKTTRLGRYpVLEVIAVTAVTAIVAYPNPYT 377
Cdd:PRK05277  201 Q--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRW-VLMGGAVGGLCGLLGLLAPAA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 378 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVITIFTFGMKIPSGLFI 457
Cdd:PRK05277  278 VGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCFGSGAPGGIFA 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 458 PSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 537
Cdd:PRK05277  324 PMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLIL 388

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 538 PLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 603
Cdd:PRK05277  389 PLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 143-559 3.93e-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: 117.33  E-value: 3.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 143 YILWALLFA--FLAVSLVRVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:cd01034    27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 218 ACCCGNFFSSLFSKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFTLR 293
Cdd:cd01034   107 GAAVMLAIGRRLPK--WGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 294 SINPFGNSRLvlfyveyHTPWyMAELFPFILLGVFGGLWGTLFTRCNIA---WCRRRKTTRLGRYPVLEVIAVTAVTAIV 370
Cdd:cd01034   185 NYPYFGVAAV-------ALPL-GEAWLLVLVCGVVGGLAGGLFARLLVAlssGLPGWVRRFRRRRPVLFAALCGLALALI 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 371 AYpnpytrqSTSELIselFNDcGALESSQlcdyindpnmtrpvddipdrpAGVGVYTAMWQLALAlifKIVITIFTFGMK 450
Cdd:cd01034   257 GL-------VSGGLT---FGT-GYLQARA---------------------ALEGGGGLPLWFGLL---KFLATLLSYWSG 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 451 IPSGLFIPSMAVGAmagrmvGIG--VEQLAYHHHdwiifrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFE 528
Cdd:cd01034   302 IPGGLFAPSLAVGA------GLGslLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVME 358

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1267345244 529 LTGGLEYIVPLMAAAVTSKWVADAFGKEGIY 559
Cdd:cd01034   359 MTGDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
192-560 1.69e-19

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 92.89  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 192 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGnffsSLFSKYSKNEGKR-REVLSAAAAAGVSVAFGAPIGGVLFSLEEVS 270
Cdd:PRK01862  119 LWRSASSLLTIGSGGSIGREGPMVQLAALAA----SLVGRFAHFDPPRlRLLVACGAAAGITSAYNAPIAGAFFVAEIVL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 271 YYFPLKTLWRSFFAALVAAFTLRSinpFGNSRlVLFYVEYH---TPWymaELFPFILLGVFGGLWGTLFTRCNIAWCRRR 347
Cdd:PRK01862  195 GSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRLLDASKNQF 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 348 KTTRLGryPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmTRPVddipdrpagvgvyt 427
Cdd:PRK01862  268 KRLPVP--LPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILH-------------------APWT-------------- 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 428 amWQ-LALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHhdwiifrnwcrpgadCVTPGLYAMV 506
Cdd:PRK01862  313 --WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHALWPGH---------------TSAPFAYAMV 375

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267345244 507 GAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYE 560
Cdd:PRK01862  376 GMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYE 429
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
498-733 9.72e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 73.76  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 498 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 577
Cdd:COG2524     4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 578 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 657
Cdd:COG2524    83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267345244 658 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 733
Cdd:COG2524   154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
585-738 2.91e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.20  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 585 DVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGFAQRRELILAIKNARQRQegivsnsimyft 664
Cdd:COG3448     6 DIMTR----DVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE------------ 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 665 eeppelPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRqCL--VTRSGRLLGIITKKDVLRHMAQMAN 738
Cdd:COG3448    66 ------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
575-736 1.09e-12

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 65.70  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 575 DEFTHRTLATDVMRprrgEPPLSVLTQDsMTVEDVETLIKETDYNGFPVLvsRDSERLIGfaqrrelILAIKNARQRQEG 654
Cdd:COG4109    10 DTFKEILLVEDIMT----LEDVATLSED-DTVEDALELLEKTGHSRFPVV--DENGRLVG-------IVTSKDILGKDDD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 655 ivsnsimyfteeppelpansphpLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHM 733
Cdd:COG4109    76 -----------------------TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKAL 132


                  ...
gi 1267345244 734 AQM 736
Cdd:COG4109   133 QKI 135
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 189-546 4.64e-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: 68.47  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 189 WTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNegkRREVLSAAAAAGVSVAFGAPIGGVLFSLE- 267
Cdd:cd01033    83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVAD---RRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 268 ---EVSyyfplktlWRSFFAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFI---LLGVFGGLWGTLFTRcni 341
Cdd:cd01033   160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTPLLIWALLagpVLGVVAAGFRRLSQA--- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 342 AWCRRRKTTRLgrypVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFNDCGALESsqlcdyindpnmtrpvddipdrpa 421
Cdd:cd01033   229 ARAKRPKGKRI----LWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSL------------------------ 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 422 gvgvytamwqLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHhhdwiifrnwcrpgadcVTPG 501
Cdd:cd01033   281 ----------LLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGIVWNALLPP-----------------LSIA 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1267345244 502 LYAMVGAAACLGGVTRMTVSLVVIMFELTG-GLEYIVPLMAAAVTS 546
Cdd:cd01033   334 AFALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS COG0517
CBS domain [Signal transduction mechanisms];
582-735 6.68e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 60.26  E-value: 6.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 582 LATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGfaqrrelilaiknarqrqegIVSNS-I 660
Cdd:COG0517     2 KVKDIMTT----DVVTV--SPDATVREALELMSEKRIGGLPVV--DEDGKLVG--------------------IVTDRdL 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 661 MYFTEEPPELPANSPhplkLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLV-TRSGRLLGIITKKDVLRHMAQ 735
Cdd:COG0517    54 RRALAAEGKDLLDTP----VSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 593-731 2.17e-10

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 58.41  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 593 EPPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppeLPA 672
Cdd:cd02205     2 RDVVTV--DPDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRAL------------------------VEG 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 673 NSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLR 731
Cdd:cd02205    54 GLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 603-731 3.42e-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: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 603 SMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppelpansPHPlKLRR 682
Cdd:cd04610    11 DDTVKDVIKLIKETGHDGFPVV---DDGKVVGYVTAKDLLGKD-----------------------------DDE-KVSE 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1267345244 683 IlnLSPFTVTDHTPMeTVVDIFRKLgLRQCL-----VTRSGRLLGIITKKDVLR 731
Cdd:cd04610    58 I--MSRDTVVADPDM-DITDAARVI-FRSGIsklpvVDDEGNLVGIITNMDVIR 107
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 585-736 3.78e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 55.22  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 585 DVMRprrgEPPLSVltQDSMTVEDVETLIKETDYNGfpVLVSRDSERLIGFAQRRELILAIKNARqrqegivsnsimyft 664
Cdd:COG2905     3 DIMS----RDVVTV--SPDATVREAARLMTEKGVGS--LVVVDDDGRLVGIITDRDLRRRVLAEG--------------- 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267345244 665 EEPPELPAnsphplklRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQM 736
Cdd:COG2905    60 LDPLDTPV--------SEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 688-731 8.62e-08

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 49.05  E-value: 8.62e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1267345244  688 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 731
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
678-734 2.54e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 50.25  E-value: 2.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267345244 678 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLRHMA 734
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEdGKLVGIVTDRDLRRALA 58
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 680-734 2.77e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 47.98  E-value: 2.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 680 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 734
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
678-742 1.24e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 48.32  E-value: 1.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 678 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMAQMANQDPE 742
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLPDRLDELE 67
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 594-731 1.78e-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: 47.81  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 594 PPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSE-RLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPA 672
Cdd:cd04586     4 DVVTV--TPDTSVREAARLLLEHRISGLPVV---DDDgKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLAEEYV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267345244 673 NSpHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 731
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 ...
 688-737 1.07e-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: 45.49  E-value: 1.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1267345244 688 PFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMA 737
Cdd:cd04584    10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 604-731 2.28e-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: 44.33  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 604 MTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAiknarqrqegivSNSImyFTEEPPELPANSPHPLKLRRI 683
Cdd:cd04584    17 TSLAEARELMKEHKIRHLPVV---DDGKLVGIVTDRDLLRA------------SPSK--ATSLSIYELNYLLSKIPVKDI 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1267345244 684 LNLSPFTVTDHTPMETVVDIFR--KLGlrqCL-VTRSGRLLGIITKKDVLR 731
Cdd:cd04584    80 MTKDVITVSPDDTVEEAALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
676-735 2.56e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.03  E-value: 2.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 676 HPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQ 735
Cdd:COG2524    84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 601-731 4.29e-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: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 601 QDSMTVEDVETLIKETDYNGFPVLvsrDSE-RLIGfaqrrelILAIKNArqrqegivsnsimyfTEEPPELPansphplk 679
Cdd:cd04596     8 RETDTVRDYKQLSEETGHSRFPVV---DEEnRVVG-------IVTAKDV---------------IGKEDDTP-------- 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 680 LRRILNLSPFTVTDHTpmeTVVDIFRKL---GLRQCLVTRSGR-LLGIITKKDVLR 731
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 ...
 583-730 9.94e-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: 42.48  E-value: 9.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 583 ATDVMRPRRgepplSVLTQD-SMTVEDVETLIKETDYNGFPVlVSRDSERLIGFAQRRELILAIKNARQrqegivsnsim 661
Cdd:cd04590     2 VREVMTPRT-----DVVALDaDATLEELLELILESGYSRFPV-YEGDLDNIIGVLHVKDLLAALLEGRE----------- 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 662 yfteeppelpansphPLKLRRILNlSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVL 730
Cdd:cd04590    65 ---------------KLDLRALLR-PPLFVPETTPLDDLLEEFRKERSHMAIVVDEyGGTAGIVTLEDIL 118
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 688-744 1.20e-04

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 42.23  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1267345244 688 PFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMAQMANQDPESI 744
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVdDDGKLVGIVTERDILRALVEGGLALDTPV 61
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 603-733 1.30e-04

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: 41.94  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 603 SMTVEDV------ETLIKETDYNGFpvlVSRDSERLIGFAQRRELILAiknarqrqegivsnsimyfteePPELpansph 676
Cdd:cd04606    17 DWTVEEAleylrrLAPDPETIYYIY---VVDEDRRLLGVVSLRDLLLA----------------------DPDT------ 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345244 677 plKLRRILNLSPFTVTDHTPMETVVDIFRKLGLrqcL----VTRSGRLLGIITKKDVLRHM 733
Cdd:cd04606    66 --KVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 594-732 3.57e-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: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 594 PPLSVLTQDsmTVEDVETLIKETDYNGFPVLVsrDSERLIGFAQRRELILAIKNARQRQEGIVSnSIMYftEEPPELPAN 673
Cdd:cd04608    11 APVTVLPDD--TLGEAIEIMREYGVDQLPVVD--EDGRVVGMVTEGNLLSSLLAGRAQPSDPVS-KAMY--KQFKQVDLD 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1267345244 674 SPHPlKLRRILNlspftvTDHTPMetVVDifrklglrqclvtRSGRLLGIITKKDVLRH 732
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 ...
 687-729 8.58e-04

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 39.40  E-value: 8.58e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1267345244 687 SP-FTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDV 729
Cdd:cd04595     2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 45
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 687-729 8.79e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 8.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1267345244 687 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 729
Cdd:PTZ00314  105 DPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 680-744 1.14e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.43  E-value: 1.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1267345244 680 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTR-SGRLLGIITKKDVLRHMAQmANQDPESI 744
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDdDGRLVGIITDRDLRRRVLA-EGLDPLDT 65
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 205-471 1.27e-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: 41.80  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 205 GLSLGKEGPLVHVacccGNFFSSLFSKYSK-NEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlk 276
Cdd:cd03682    92 GGSAGREGTAVQM----GGSLADAFGRVFKlPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP-- 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 277 tlwrSFFAALVAAFTLRSINPFGNSRLVLFYVEYhTPWYMAELfpfILLGVFGGLWGTLFTRCnIAWCrRRKTTRLGRYP 356
Cdd:cd03682   166 ----CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNP 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 357 VLEVIAVTAVTAIVAYpnpytrqstseliselfndcgaLESSQlcDYINdpnmtRPVDDIPDRPAGVGVYTAMWqlalal 436
Cdd:cd03682   236 YLRPFVGGLLIILLVY----------------------LLGSR--RYLG-----LGTPLIEDSFFGGTVYPYDW------ 280

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1267345244 437 IFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVG 471
Cdd:cd03682   281 LLKLIFTVITLGAGFKGGEVTPLFFIGATLGNALA 315
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
662-731 1.28e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 42.13  E-value: 1.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267345244 662 YFTEEPPELPANSpHPlKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLR 731
Cdd:PRK14869   54 YFGVEAPELIEDV-KP-QVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTlPVVDEEGKLLGLVSLSDLAR 122
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 192-336 1.70e-03

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 41.69  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 192 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKysKNEGKRRevLSAAAAAGVSVAFGAPIGGVLFSLEEVSY 271
Cdd:PRK01610  101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTP--RQEWKLW--IACGAAAGMASAYHAPLAGSLFIAEILFG 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267345244 272 YFPLKTLWRSFFAALVAAFTLRSINPfgnSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTLF 336
Cdd:PRK01610  177 TLMLASLGPVVISAVVALLTTNLLNG---SDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLL 238
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 680-744 6.61e-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: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267345244 680 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQC----------------LVTRSGRLLGIITKKDVLRHMAQMANQDPES 743
Cdd:cd04620     1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                  .
gi 1267345244 744 I 744
Cdd:cd04620    81 I 81
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 679-731 9.63e-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: 36.82  E-value: 9.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1267345244 679 KLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 731
Cdd:cd04631     1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMR 53
 
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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