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Conserved domains on  [gi|76563948|ref|NP_071534|]
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H(+)/Cl(-) exchange transporter 4 [Rattus norvegicus]

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 ...
 72-578 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: 729.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  72 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 151
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 152 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 231
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 232 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 311
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 312 LFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCNIAWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSEL 391
Cdd:cd03684 193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 392 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 471
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 472 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 551
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 76563948 552 TSKWVADAFGKEGIYEAHIHLNGYPFL 578
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 ...
 589-739 7.93e-46

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


:

Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 159.22  E-value: 7.93e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 589 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 668
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76563948 669 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 739
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 ...
 72-578 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: 729.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  72 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 151
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 152 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 231
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 232 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 311
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 312 LFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCNIAWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSEL 391
Cdd:cd03684 193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 392 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 471
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 472 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 551
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 76563948 552 TSKWVADAFGKEGIYEAHIHLNGYPFL 578
Cdd:cd03684 419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 157-558 2.23e-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: 294.84  E-value: 2.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   157 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 236
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   237 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 316
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   317 YHTPWYMAELFPFILLGVFGGLWGTVFTRCNIaWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELF 396
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   397 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRM 476
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   477 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 556
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 76563948   557 AD 558
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
65-571 1.97e-58

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 204.22  E-value: 1.97e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  65 WVVMLLIGLLAGTLAGVIDLAVDWMTDLkegvclsafwysheqccwtsnettfedrdkcplwqkwseLLLSQSEGASAYI 144
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHL---------------------------------------FLGGLLSAAGSHL 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 145 LNYLmYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 224
Cdd:COG0038  49 PPWL-VLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQI 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 225 ACCCGNFFSSLFsKYSKNEgkRREVLSaaaaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInp 304
Cdd:COG0038 126 GAAIGSLLGRLL-RLSPED--RRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL-- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 305 FGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCnIAWCRRRkTTRLGKYPVLEVIVVTAITAIIAYPNPYT 384
Cdd:COG0038 201 FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQV 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 385 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVITIFTFGMKIPSGLFI 464
Cdd:COG0038 277 LGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFA 322

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 465 PSMAVGAMAGRMVGIGVEQLAyhhhdwiifrnwcrPGADcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 544
Cdd:COG0038 323 PSLFIGALLGAAFGLLLNLLF--------------PGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLL 387

                       490       500
                ....*....|....*....|....*..
gi 76563948 545 PLMAAAVTSKWVADAFGKEGIYEAHIH 571
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 ...
 589-739 7.93e-46

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


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 159.22  E-value: 7.93e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 589 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 668
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76563948 669 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 739
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
70-610 7.80e-29

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 120.38  E-value: 7.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   70 LIGLLAGTLAGVIDLAVDWMtdlkegvclsafwysheqccwtsnettfedrdkcplwQKWSELLLSQSEGAsaYILNYLM 149
Cdd:PRK05277   6 VVGTLTGLVGVAFELAVDWV-------------------------------------QNQRLGLLASVADN--GLLLWIV 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  150 YILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCG 229
Cdd:PRK05277  47 AFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIG 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  230 NFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFTLRSINpfGN 307
Cdd:PRK05277 125 RMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN--GE 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  308 SrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCNIA---WCRRRKTTRLGKYpVLEVIVVTAITAIIAYPNPYT 384
Cdd:PRK05277 201 Q--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRW-VLMGGAVGGLCGLLGLLAPAA 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  385 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVITIFTFGMKIPSGLFI 464
Cdd:PRK05277 278 VGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCFGSGAPGGIFA 323

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  465 PSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 544
Cdd:PRK05277 324 PMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLIL 388

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948  545 PLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 610
Cdd:PRK05277 389 PLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
505-740 2.49e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 75.31  E-value: 2.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 505 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 584
Cdd:COG2524   4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 585 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 664
Cdd:COG2524  83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76563948 665 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 740
Cdd:COG2524 154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 695-738 8.96e-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: 8.96e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 76563948    695 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 738
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 687-741 3.00e-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: 47.59  E-value: 3.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948   687 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 741
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 694-736 8.90e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 8.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 76563948  694 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 736
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 ...
 72-578 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: 729.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  72 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 151
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 152 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 231
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 232 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 311
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 312 LFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCNIAWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSEL 391
Cdd:cd03684 193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 392 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 471
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 472 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 551
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 76563948 552 TSKWVADAFGKEGIYEAHIHLNGYPFL 578
Cdd:cd03684 419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 72-567 2.39e-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: 414.05  E-value: 2.39e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  72 GLLAGTLAGVIDLAVDWMTDLKEGVCLSAFwysheqccwtsnettfedrdkcplwqkwselllsqsegaSAYILNYLMYI 151
Cdd:cd01036   1 GLLMGLVAVVLDYAVESSLDAGQWLLRRIP---------------------------------------GSYLLGYLMWV 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 152 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 231
Cdd:cd01036  42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 232 FSSLFSKYS----------KNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRS 301
Cdd:cd01036 122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 302 INPFGNSR----------LVLFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCNIAWCRRR---KTTRLGKYPVLEVI 368
Cdd:cd01036 202 YNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRrrlLFRKTARYRVLEPV 281

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 369 VVTAITAIIAYPnpytrqstseliselfndcgalessqlcdyindpnmtrpvddipdrpagvgvytamWQLALALIFKIV 448
Cdd:cd01036 282 LFTLIYSTIHYA--------------------------------------------------------PTLLLFLLIYFW 305

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 449 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHDwiifrnwCRPGADCVTPGLYAMVGAAACLGGVTRMTVS 528
Cdd:cd01036 306 MSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRLTFS 378

                       490       500       510
                ....*....|....*....|....*....|....*....
gi 76563948 529 LVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYE 567
Cdd:cd01036 379 ICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 157-558 2.23e-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: 294.84  E-value: 2.23e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   157 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 236
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   237 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 316
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   317 YHTPWYMAELFPFILLGVFGGLWGTVFTRCNIaWCRRRKTTRLGKYPVLEVIVVTAITAIIAYPNPYTRQSTSELISELF 396
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   397 NDCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRM 476
Cdd:pfam00654 232 NGN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   477 VGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWV 556
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 76563948   557 AD 558
Cdd:pfam00654 343 SR 344
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 65-578 6.61e-93

ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. Proteins in this family are ubiquitous in eukarotes and their functions are unclear. They are expressed in intracellular organelles membranes. This family belongs to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. ClC chloride ion channel superfamily perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, and transepithelial transport in animals.


Pssm-ID: 239657 [Multi-domain]  Cd Length: 466  Bit Score: 298.03  E-value: 6.61e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  65 WVVMLLIGLLAGTLAGVIDLAVDWMTDLKegvcLSAFWYSHEQCCwtsnettfedrdkcplwqkwselllsqsegasaYI 144
Cdd:cd03685  33 WIICLLIGIFTGLVAYFIDLAVENLAGLK----FLVVKNYIEKGR---------------------------------LF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 145 LNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 224
Cdd:cd03685  76 TAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 225 ACCCGNFFSSLFSK----------YSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALV 294
Cdd:cd03685 156 GACIAAGLSQGGSTslrldfrwfrYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMI 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 295 AAFTLRSINPFGNSR---------LVLFYVeYHTP--WYMAELFPFILLGVFGGLWGTVFTRCN--IAWCRRRKTTRLGK 361
Cdd:cd03685 236 VTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNhkVTRFRKRINHKGKL 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 362 YPVLEVIVVTAITAIIAYpnpytrqstseliselfndcgalessqlcdyindpnmtrpvddipdrpagvgvytaMWQLAL 441
Cdd:cd03685 315 LKVLEALLVSLVTSVVAF--------------------------------------------------------PQTLLI 338

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 442 ALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLayhhhdwiifrnwcrPGADCVTPGLYAMVGAAACLGG 521
Cdd:cd03685 339 FFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSY---------------FGFTSIDPGLYALLGAAAFLGG 403

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 76563948 522 VTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFgKEGIYEAHIHLNGYPFL 578
Cdd:cd03685 404 VMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 142-578 1.15e-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: 261.41  E-value: 1.15e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 142 AYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPL 221
Cdd:cd03683  40 NSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPF 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 222 VHVACCCGNFFSSL---FSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFT 298
Cdd:cd03683 120 VHISSIVAALLSKLttfFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFT 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 299 LRSINPF---GNSRLVLFYVEYHT--PWYMAELFPFILLGVFGGLWGTVFTRCNIAWCRRRKTTR-----LGKYPVLEVI 368
Cdd:cd03683 200 FRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRlfskfLKRSPLLYPA 279

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 369 VVTAITAIIAYPnpytrqstseliselfndcgalessqlcdYINdpnmtrpvddipdrpagvgvytamwqLALALIFKIV 448
Cdd:cd03683 280 IVALLTAVLTFP-----------------------------FLT--------------------------LFLFIVVKFV 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 449 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGigvEQLAYHHHDWIIfrnwcRPGADCVTPGLYAMVGAAACLGGVTRmTVS 528
Cdd:cd03683 305 LTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAVLFPEGIR-----GGISNPIGPGGYAVVGAAAFSGAVTH-TVS 375

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 76563948 529 LVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYEAHIHLNGYPFL 578
Cdd:cd03683 376 VAVIIFELTGQISHLLPVLIAVLISNAVAQFLQ-PSIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 125-553 2.21e-60

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


Pssm-ID: 238233 [Multi-domain]  Cd Length: 383  Bit Score: 208.57  E-value: 2.21e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 125 LWQKWSELLLSQSEGASAYILNYL-MYILWALLFAFLAVSLVRVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLLIKT 202
Cdd:cd00400  13 LLIELLQNLLFGGLPGELAAGSLSpLYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKF 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 203 VTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPL 282
Cdd:cd00400  90 LASALTLGSGGSVGREGPIVQIGAAIGSWLGRRL-RLSRND--RRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSV 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 283 KTLWRSFFAALVAAFTLRSINPFGNsrlvLFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCNIAWCRRRKttRLGKY 362
Cdd:cd00400 167 ASLIPVLLASVAAALVSRLLFGAEP----AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIP 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 363 PVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvgVYTAMWQLALA 442
Cdd:cd00400 241 PWLRPALGGLLLGLLGLFLPQVLGSGYGAILLALA----------------------------------GELSLLLLLLL 286

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 443 LIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGV 522
Cdd:cd00400 287 LLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALFPGLV---------------ASPGAYALVGMAALLAAV 351

                       410       420       430
                ....*....|....*....|....*....|.
gi 76563948 523 TRMTVSLVVIMFELTGGLEYIVPLMAAAVTS 553
Cdd:cd00400 352 LRAPLTAILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
65-571 1.97e-58

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 204.22  E-value: 1.97e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  65 WVVMLLIGLLAGTLAGVIDLAVDWMTDLkegvclsafwysheqccwtsnettfedrdkcplwqkwseLLLSQSEGASAYI 144
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHL---------------------------------------FLGGLLSAAGSHL 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 145 LNYLmYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 224
Cdd:COG0038  49 PPWL-VLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQI 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 225 ACCCGNFFSSLFsKYSKNEgkRREVLSaaaaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInp 304
Cdd:COG0038 126 GAAIGSLLGRLL-RLSPED--RRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL-- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 305 FGNSrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCnIAWCRRRkTTRLGKYPVLEVIVVTAITAIIAYPNPYT 384
Cdd:COG0038 201 FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQV 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 385 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVITIFTFGMKIPSGLFI 464
Cdd:COG0038 277 LGSGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFA 322

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 465 PSMAVGAMAGRMVGIGVEQLAyhhhdwiifrnwcrPGADcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 544
Cdd:COG0038 323 PSLFIGALLGAAFGLLLNLLF--------------PGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLL 387

                       490       500
                ....*....|....*....|....*..
gi 76563948 545 PLMAAAVTSKWVADAFGKEGIYEAHIH 571
Cdd:COG0038 388 PLMIACVIAYLVSRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 71-568 6.57e-49

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: 177.35  E-value: 6.57e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  71 IGLLAGTLAGVIDLAVDWMTDLKEgvclsaFWYSHeqccwtsnettfedrdkcplwqkwselllsqsegASAYILNYLMY 150
Cdd:cd01031   1 IGLLAGLVAVLFRLGIDKLGNLRL------SLYDF----------------------------------AANNPPLLLVL 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 151 ILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGN 230
Cdd:cd01031  41 PLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQ 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 231 FFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGnsrl 310
Cdd:cd01031 119 GVSKWF-KTSPEE--RRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG---- 191

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 311 VLFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTR--CNIAWCRRRkttRLGKYPVLEVIVVTAITAIIAYPNPYTRQST 388
Cdd:cd01031 192 PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRslLKSQDLYRK---LKKLPRELRVLLPGLLIGPLGLLLPEALGGG 268

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 389 SELISELFndcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMA 468
Cdd:cd01031 269 HGLILSLA----------------------------------GGNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLA 314

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 469 VGAMAGRMVGIGVEQLAyhhHDWIIFrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMA 548
Cdd:cd01031 315 LGALLGLLFGTILVQLG---PIPISA------------PATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMV 379

                       490       500
                ....*....|....*....|
gi 76563948 549 AAVTSKWVADAFGKEGIYEA 568
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 ...
 589-739 7.93e-46

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


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 159.22  E-value: 7.93e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 589 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVVVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 668
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76563948 669 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 739
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
70-610 7.80e-29

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 120.38  E-value: 7.80e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948   70 LIGLLAGTLAGVIDLAVDWMtdlkegvclsafwysheqccwtsnettfedrdkcplwQKWSELLLSQSEGAsaYILNYLM 149
Cdd:PRK05277   6 VVGTLTGLVGVAFELAVDWV-------------------------------------QNQRLGLLASVADN--GLLLWIV 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  150 YILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCG 229
Cdd:PRK05277  47 AFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIG 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  230 NFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFTLRSINpfGN 307
Cdd:PRK05277 125 RMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN--GE 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  308 SrlVLFYVEYHTPWYMAELFPFILLGVFGGLWGTVFTRCNIA---WCRRRKTTRLGKYpVLEVIVVTAITAIIAYPNPYT 384
Cdd:PRK05277 201 Q--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRW-VLMGGAVGGLCGLLGLLAPAA 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  385 RQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVITIFTFGMKIPSGLFI 464
Cdd:PRK05277 278 VGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCFGSGAPGGIFA 323

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  465 PSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 544
Cdd:PRK05277 324 PMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLIL 388

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948  545 PLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 610
Cdd:PRK05277 389 PLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 150-566 2.65e-27

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: 114.63  E-value: 2.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 150 YILWALLFA--FLAVSLVRVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 224
Cdd:cd01034  27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 225 ACCCGNFFSSLFSKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFTLR 300
Cdd:cd01034 107 GAAVMLAIGRRLPK--WGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 301 SINPFGNSRLvlfyveyHTPWyMAELFPFILLGVFGGLWGTVFTRCNIA---WCRRRKTTRLGKYPVLEVIVVTAITAII 377
Cdd:cd01034 185 NYPYFGVAAV-------ALPL-GEAWLLVLVCGVVGGLAGGLFARLLVAlssGLPGWVRRFRRRRPVLFAALCGLALALI 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 378 AYpnpytrqSTSELIselFNDcGALESSQlcdyindpnmtrpvddipdrpAGVGVYTAMWQLALAlifKIVITIFTFGMK 457
Cdd:cd01034 257 GL-------VSGGLT---FGT-GYLQARA---------------------ALEGGGGLPLWFGLL---KFLATLLSYWSG 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 458 IPSGLFIPSMAVGAmagrmvGIG--VEQLAYHHHdwiifrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFE 535
Cdd:cd01034 302 IPGGLFAPSLAVGA------GLGslLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVME 358

                       410       420       430
                ....*....|....*....|....*....|.
gi 76563948 536 LTGGLEYIVPLMAAAVTSKWVADAFGKEGIY 566
Cdd:cd01034 359 MTGDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
199-567 1.60e-19

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 92.89  E-value: 1.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  199 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGnffsSLFSKYSKNEGKR-REVLSAAAAAGVSVAFGAPIGGVLFSLEEVS 277
Cdd:PRK01862 119 LWRSASSLLTIGSGGSIGREGPMVQLAALAA----SLVGRFAHFDPPRlRLLVACGAAAGITSAYNAPIAGAFFVAEIVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  278 YYFPLKTLWRSFFAALVAAFTLRSinpFGNSRlVLFYVEYH---TPWymaELFPFILLGVFGGLWGTVFTRCNIAWCRRR 354
Cdd:PRK01862 195 GSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRLLDASKNQF 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  355 KTTRLGkyPVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmTRPVddipdrpagvgvyt 434
Cdd:PRK01862 268 KRLPVP--LPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILH-------------------APWT-------------- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  435 amWQ-LALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHhdwiifrnwcrpgadCVTPGLYAMV 513
Cdd:PRK01862 313 --WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHALWPGH---------------TSAPFAYAMV 375

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 76563948  514 GAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYE 567
Cdd:PRK01862 376 GMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYE 429
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
505-740 2.49e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 75.31  E-value: 2.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 505 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 584
Cdd:COG2524   4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 585 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 664
Cdd:COG2524  83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76563948 665 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 740
Cdd:COG2524 154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
592-745 1.00e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 68.74  E-value: 1.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 592 DVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGFAQRRELILAIKNARQRQegivsnsimyft 671
Cdd:COG3448   6 DIMTR----DVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE------------ 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948 672 eeppelPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRqCL--VTRSGRLLGIITKKDVLRHMAQMAN 745
Cdd:COG3448  66 ------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
582-743 3.79e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 66.86  E-value: 3.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 582 DEFTHRTLATDVMRprrgEPPLSVLTQDsMTVEDVETLIKETDYNGFPVVvsRDSERLIGfaqrrelILAIKNARQRQEG 661
Cdd:COG4109  10 DTFKEILLVEDIMT----LEDVATLSED-DTVEDALELLEKTGHSRFPVV--DENGRLVG-------IVTSKDILGKDDD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 662 ivsnsimyfteeppelpansphpLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHM 740
Cdd:COG4109  76 -----------------------TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKAL 132


                ...
gi 76563948 741 AQM 743
Cdd:COG4109 133 QKI 135
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 196-553 4.38e-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: 4.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 196 WTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNegkRREVLSAAAAAGVSVAFGAPIGGVLFSLE- 274
Cdd:cd01033  83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVAD---RRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 275 ---EVSyyfplktlWRSFFAALVAAFTLRSINPFGNSRLVLFYVEYHTPWYMAELFPFI---LLGVFGGLWGTVFTRcni 348
Cdd:cd01033 160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTPLLIWALLagpVLGVVAAGFRRLSQA--- 228

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 349 AWCRRRKTTRLgkypVLEVIVVTAITAIIAYPNPYTRQSTSELISELFNDCGALESsqlcdyindpnmtrpvddipdrpa 428
Cdd:cd01033 229 ARAKRPKGKRI----LWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFSTTLTLSL------------------------ 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 429 gvgvytamwqLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHhhdwiifrnwcrpgadcVTPG 508
Cdd:cd01033 281 ----------LLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGIVWNALLPP-----------------LSIA 333

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 76563948 509 LYAMVGAAACLGGVTRMTVSLVVIMFELTG-GLEYIVPLMAAAVTS 553
Cdd:cd01033 334 AFALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS COG0517
CBS domain [Signal transduction mechanisms];
589-742 1.23e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 62.58  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 589 LATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGfaqrrelilaiknarqrqegIVSNS-I 667
Cdd:COG0517   2 KVKDIMTT----DVVTV--SPDATVREALELMSEKRIGGLPVV--DEDGKLVG--------------------IVTDRdL 53

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948 668 MYFTEEPPELPANSPhplkLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLV-TRSGRLLGIITKKDVLRHMAQ 742
Cdd:COG0517  54 RRALAAEGKDLLDTP----VSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 600-738 4.25e-11

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 60.34  E-value: 4.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 600 EPPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppeLPA 679
Cdd:cd02205   2 RDVVTV--DPDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRAL------------------------VEG 53

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 680 NSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLR 738
Cdd:cd02205  54 GLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 592-743 1.64e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 56.38  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 592 DVMRprrgEPPLSVltQDSMTVEDVETLIKETDYNGFPVVvsRDSERLIGFAQRRELILAIKNARqrqegivsnsimyft 671
Cdd:COG2905   3 DIMS----RDVVTV--SPDATVREAARLMTEKGVGSLVVV--DDDGRLVGIITDRDLRRRVLAEG--------------- 59

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76563948 672 EEPPELPAnsphplklRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQM 743
Cdd:COG2905  60 LDPLDTPV--------SEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 610-738 1.87e-09

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 55.79  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 610 SMTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppelpansPHPlKLRR 689
Cdd:cd04610  11 DDTVKDVIKLIKETGHDGFPVV---DDGKVVGYVTAKDLLGKD-----------------------------DDE-KVSE 57

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 76563948 690 IlnLSPFTVTDHTPMeTVVDIFRKLgLRQCL-----VTRSGRLLGIITKKDVLR 738
Cdd:cd04610  58 I--MSRDTVVADPDM-DITDAARVI-FRSGIsklpvVDDEGNLVGIITNMDVIR 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 695-738 8.96e-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: 8.96e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 76563948    695 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 738
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
685-741 2.69e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 49.86  E-value: 2.69e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 76563948 685 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLRHMA 741
Cdd:COG0517   1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEdGKLVGIVTDRDLRRALA 58
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 687-741 3.00e-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: 47.59  E-value: 3.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948   687 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 741
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 601-738 4.54e-07

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 49.74  E-value: 4.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 601 PPLSVltQDSMTVEDVETLIKETDYNGFPVVvsrDSE-RLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPA 679
Cdd:cd04586   4 DVVTV--TPDTSVREAARLLLEHRISGLPVV---DDDgKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLAEEYV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 76563948 680 NSpHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 738
Cdd:cd04586  79 KA-HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
685-741 1.33e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 48.32  E-value: 1.33e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 76563948 685 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMA 741
Cdd:COG3448   2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALL 59
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 611-738 5.87e-06

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 46.26  E-value: 5.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 611 MTVEDVETLIKETDYNGFPVVvsrDSERLIGFAQRRELILAiknarqrqegivSNSImyFTEEPPELPANSPHPLKLRRI 690
Cdd:cd04584  17 TSLAEARELMKEHKIRHLPVV---DDGKLVGIVTDRDLLRA------------SPSK--ATSLSIYELNYLLSKIPVKDI 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 76563948 691 LNLSPFTVTDHTPMETVVDIFR--KLGlrqCL-VTRSGRLLGIITKKDVLR 738
Cdd:cd04584  80 MTKDVITVSPDDTVEEAALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 608-738 7.47e-06

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 45.15  E-value: 7.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 608 QDSMTVEDVETLIKETDYNGFPVVvsrDSE-RLIGfaqrrelILAIKNArqrqegivsnsimyfTEEPPELPansphplk 686
Cdd:cd04596   8 RETDTVRDYKQLSEETGHSRFPVV---DEEnRVVG-------IVTAKDV---------------IGKEDDTP-------- 54

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948 687 LRRILNLSPFTVTDHTpmeTVVDIFRKL---GLRQCLVTRSGR-LLGIITKKDVLR 738
Cdd:cd04596  55 IEKVMTKNPITVKPKT---SVASAAHMMiweGIELLPVVDENRkLLGVISRQDVLK 107
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 695-744 1.14e-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: 1.14e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 76563948 695 PFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMA 744
Cdd:cd04584  10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 610-740 1.27e-05

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


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 45.02  E-value: 1.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 610 SMTVEDV------ETLIKETDYNGFpvVVSRDsERLIGFAQRRELILAiknarqrqegivsnsimyfteePPELpansph 683
Cdd:cd04606  17 DWTVEEAleylrrLAPDPETIYYIY--VVDED-RRLLGVVSLRDLLLA----------------------DPDT------ 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76563948 684 plKLRRILNLSPFTVTDHTPMETVVDIFRKLGLrqcL----VTRSGRLLGIITKKDVLRHM 740
Cdd:cd04606  66 --KVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
683-742 2.79e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 45.64  E-value: 2.79e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 683 HPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQ 742
Cdd:COG2524  84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 590-737 1.01e-04

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: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 590 ATDVMRPRRgepplSVLTQD-SMTVEDVETLIKETDYNGFPvVVSRDSERLIGFAQRRELILAIKNARQrqegivsnsim 668
Cdd:cd04590   2 VREVMTPRT-----DVVALDaDATLEELLELILESGYSRFP-VYEGDLDNIIGVLHVKDLLAALLEGRE----------- 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 669 yfteeppelpansphPLKLRRILNlSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVL 737
Cdd:cd04590  65 ---------------KLDLRALLR-PPLFVPETTPLDDLLEEFRKERSHMAIVVDEyGGTAGIVTLEDIL 118
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 212-478 1.25e-04

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: 44.88  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 212 GLSLGKEGPLVHVacccGNFFSSLFSKYSK-NEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlk 283
Cdd:cd03682  92 GGSAGREGTAVQM----GGSLADAFGRVFKlPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP-- 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 284 tlwrSFFAALVAAFTLRSINPFGNSRLVLFYVEYhTPWYMAELfpfILLGVFGGLWGTVFTRCnIAWCrRRKTTRLGKYP 363
Cdd:cd03682 166 ----CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNP 235

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 364 VLEVIVVTAITAIIAYpnpytrqstseliselfndcgaLESSQlcDYINdpnmtRPVDDIPDRPAGVGVYTAMWqlalal 443
Cdd:cd03682 236 YLRPFVGGLLIILLVY----------------------LLGSR--RYLG-----LGTPLIEDSFFGGTVYPYDW------ 280

                       250       260       270
                ....*....|....*....|....*....|....*
gi 76563948 444 IFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVG 478
Cdd:cd03682 281 LLKLIFTVITLGAGFKGGEVTPLFFIGATLGNALA 315
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 695-751 1.32e-04

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 41.85  E-value: 1.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 76563948 695 PFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMAQMANQDPESI 751
Cdd:cd02205   4 VVTVDPDTTVREALELMAENGIGALPVVdDDGKLVGIVTERDILRALVEGGLALDTPV 61
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 601-739 2.02e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 41.75  E-value: 2.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 601 PPLSVLTQDsmTVEDVETLIKETDYNGFPVVVsrDSERLIGFAQRRELILAIKNARQRQEGIVSnSIMYftEEPPELPAN 680
Cdd:cd04608  11 APVTVLPDD--TLGEAIEIMREYGVDQLPVVD--EDGRVVGMVTEGNLLSSLLAGRAQPSDPVS-KAMY--KQFKQVDLD 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 76563948 681 SPHPlKLRRILNlspftvTDHTPMetVVDifrklglrqclvtRSGRLLGIITKKDVLRH 739
Cdd:cd04608  84 TPLG-ALSRILE------RDHFAL--VVD-------------GQGKVLGIVTRIDLLNY 120
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 694-736 8.90e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 8.90e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 76563948  694 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 736
Cdd:PTZ00314 105 DPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 694-736 9.10e-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: 9.10e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 76563948 694 SP-FTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDV 736
Cdd:cd04595   2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 45
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 687-751 1.20e-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: 1.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 76563948 687 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTR-SGRLLGIITKKDVLRHMAQmANQDPESI 751
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDdDGRLVGIITDRDLRRRVLA-EGLDPLDT 65
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
669-738 1.37e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 42.13  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76563948  669 YFTEEPPELPANSpHPlKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLR 738
Cdd:PRK14869  54 YFGVEAPELIEDV-KP-QVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTlPVVDEEGKLLGLVSLSDLAR 122
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 605-653 3.86e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 35.95  E-value: 3.86e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 76563948    605 VLTQDSMTVEDVETLIKETDYNGFPVVVSRDseRLIGFAQRRELILAIK 653
Cdd:smart00116   3 VTVSPDTTLEEALELLRENGIRRLPVVDEEG--RLVGIVTRRDIIKALA 49
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
611-747 4.46e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 40.05  E-value: 4.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 611 MTVEDV------ETLIKETDYNGFpvVVSRDsERLIGFAQRRELILAiknarqrqegivsnsimyfteePPElpansphp 684
Cdd:COG2239 146 WTVGEAlrylrrQAEDPETIYYIY--VVDDD-GRLVGVVSLRDLLLA----------------------DPD-------- 192

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76563948 685 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRqCL--VTRSGRLLGIITKKDVLRHMAQMANQD 747
Cdd:COG2239 193 TKVSDIMDTDVISVPADDDQEEVARLFERYDLL-ALpvVDEEGRLVGIITVDDVVDVIEEEATED 256
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 590-654 4.70e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.04  E-value: 4.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76563948   590 ATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVVVsrDSERLIGFAQRRELILAIKN 654
Cdd:pfam00571   1 VKDIMTK----DVVTV--SPDTTLEEALELMREHGISRLPVVD--EDGKLVGIVTLKDLLRALLG 57
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 199-343 6.35e-03

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 39.76  E-value: 6.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948  199 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKysKNEGKRRevLSAAAAAGVSVAFGAPIGGVLFSLEEVSY 278
Cdd:PRK01610 101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTP--RQEWKLW--IACGAAAGMASAYHAPLAGSLFIAEILFG 176

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76563948  279 YFPLKTLWRSFFAALVAAFTLRSINPfgnSRLVLFYVEYHTPWYMAELFPFILLGVFGGLWGTVF 343
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 ...
 687-751 6.75e-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: 6.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76563948 687 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQC----------------LVTRSGRLLGIITKKDVLRHMAQMANQDPES 750
Cdd:cd04620   1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                .
gi 76563948 751 I 751
Cdd:cd04620  81 I 81
 
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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