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Conserved domains on  [gi|55770838|ref|NP_001820|]
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H(+)/Cl(-) exchange transporter 3 isoform b [Homo sapiens]

Protein Classification

chloride channel protein( domain architecture ID 10132694)

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

CATH:  1.10.3080.10
Gene Ontology:  GO:0006821|GO:0005247|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 ...
 136-642 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: 750.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 136 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 215
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 216 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 295
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 296 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 375
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 376 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 455
Cdd:cd03684 193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 456 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 535
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 536 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 615
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 55770838 616 TSKWVGDAFGREGIYEAHIRLNGYPFL 642
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 ...
 653-803 4.94e-47

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: 162.69  E-value: 4.94e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 653 LAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegivgssrv 732
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770838 733 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 803
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 ...
 136-642 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: 750.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 136 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 215
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 216 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 295
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 296 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 375
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 376 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 455
Cdd:cd03684 193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 456 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 535
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 536 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 615
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 55770838 616 TSKWVGDAFGREGIYEAHIRLNGYPFL 642
Cdd:cd03684 419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 221-622 4.59e-95

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: 300.62  E-value: 4.59e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   221 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 300
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   301 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 380
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   381 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELF 460
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   461 TDCGPLessslcdyrndmnaskivddipdrpagigvysaiWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 540
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   541 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 620
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 55770838   621 GD 622
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
129-635 3.09e-55

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 196.13  E-value: 3.09e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 129 WLVVTLTGLASGALAGLIDIAADWMTDLkegiclsalwynheqccwgsnettfeerdkcpqwkTWAELIIGQAEGPGSYI 208
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHL-----------------------------------FLGGLLSAAGSHLPPWL 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 209 mnyimyIFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVH 287
Cdd:COG0038  53 ------VLLLPPLGGLLVGlLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQ 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 288 VACCCGNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSIn 367
Cdd:COG0038 125 IGAAIGSLLGRLLR---LSPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 368 pFGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRAnIAWCRRRkSTKFGKYPVLEVIIVAAITAVIAFPNPY 447
Cdd:COG0038 201 -FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQ 275

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 448 TRLNTSELIKELFTdcGPLessslcdyrndmnaskivddipdrpagigvysAIWQLCLALIFKIIMTVFTFGIKVPSGLF 527
Cdd:COG0038 276 VLGSGYGLIEALLN--GEL--------------------------------SLLLLLLLLLLKLLATALTLGSGGPGGIF 321

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 528 IPSMAIGAIAGRIVGIAVEQLayyhhdwfifkewceVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYI 607
Cdd:COG0038 322 APSLFIGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLL 386

                       490       500
                ....*....|....*....|....*...
gi 55770838 608 VPLMAAVMTSKWVGDAFGREGIYEAHIR 635
Cdd:COG0038 387 LPLMIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 653-803 4.94e-47

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: 162.69  E-value: 4.94e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 653 LAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegivgssrv 732
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770838 733 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 803
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
204-632 2.88e-27

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 115.76  E-value: 2.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  204 PGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEG 283
Cdd:PRK05277  37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  284 PLVHVACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 361
Cdd:PRK05277 115 PTVQMGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  362 VLRSINpfGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTKFGKYpVLEVIIVAAIT 438
Cdd:PRK05277 193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLC 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  439 AVIAFPNPYTRLNTSELIKELFTdcgplessslcdyrndmnaskivddipdrpagiGVYSaIWQLCLALIFKIIMTVFTF 518
Cdd:PRK05277 268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNFS-IGMLLFIFVARFITTLLCF 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  519 GIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVF 598
Cdd:PRK05277 314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVL 378

                        410       420       430
                 ....*....|....*....|....*....|....
gi 55770838  599 ELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 632
Cdd:PRK05277 379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
653-809 2.89e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 73.36  E-value: 2.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 653 LAADVMrprrnDPPLAVLTQDnMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKKQegivgssrv 732
Cdd:COG3448   3 TVRDIM-----TRDVVTVSPD-TTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE--------- 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770838 733 cfaqhtpslPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQTAN 809
Cdd:COG3448  66 ---------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 759-802 4.44e-09

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: 52.90  E-value: 4.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 55770838    759 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILR 802
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIK 46
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 751-805 2.02e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 48.36  E-value: 2.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 55770838   751 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 805
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 757-800 6.71e-05

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 46.12  E-value: 6.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 55770838  757 MSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDI 800
Cdd:PTZ00314 104 MDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 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 ...
 136-642 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: 750.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 136 GLASGALAGLIDIAADWMTDLKEGIClsalwynheqccwgsnettfeerdkcpqwktwaeliigqaegpgsyimNYIMYI 215
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 216 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 295
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 296 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 375
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 376 LFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSEL 455
Cdd:cd03684 193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 456 IKELFTDCGPLESSSLCDYrndmnaskivddiPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGA 535
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 536 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 615
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 55770838 616 TSKWVGDAFGREGIYEAHIRLNGYPFL 642
Cdd:cd03684 419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 136-631 1.48e-151

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: 449.87  E-value: 1.48e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 136 GLASGALAGLIDIAADWMTDLKEGICLSAlwynheqccwgsnettfeerdkcpqwktwaeliigqaegPGSYIMNYIMYI 215
Cdd:cd01036   1 GLLMGLVAVVLDYAVESSLDAGQWLLRRI---------------------------------------PGSYLLGYLMWV 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 216 FWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 295
Cdd:cd01036  42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 296 FSYLFPKYS----------TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRS 365
Cdd:cd01036 122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 366 INPFGNSR----------LVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKF---GKYPVLEVI 432
Cdd:cd01036 202 YNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFrktARYRVLEPV 281

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 433 IVAAITAVIAFpnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagigvysaIWQLCLALIFKII 512
Cdd:cd01036 282 LFTLIYSTIHY--------------------------------------------------------APTLLLFLLIYFW 305

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 513 MTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewCEVGADCITPGLYAMVGAAACLGGVTRMTVS 592
Cdd:cd01036 306 MSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRLTFS 378

                       490       500       510
                ....*....|....*....|....*....|....*....
gi 55770838 593 LVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGrEGIYE 631
Cdd:cd01036 379 ICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 221-622 4.59e-95

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: 300.62  E-value: 4.59e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   221 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 300
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   301 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 380
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   381 YHTPWYLFELFPFILLGVFGGLWGAFFIRANIaWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELF 460
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   461 TDCGPLessslcdyrndmnaskivddipdrpagigvysaiWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 540
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838   541 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 620
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 55770838   621 GD 622
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. ...
 129-642 8.42e-95

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: 304.58  E-value: 8.42e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 129 WLVVTLTGLASGALAGLIDIAADWMTDLKegicLSALWYNHEQCCwgsnettfeerdkcpqwktwaeliigqaegpgsYI 208
Cdd:cd03685  33 WIICLLIGIFTGLVAYFIDLAVENLAGLK----FLVVKNYIEKGR---------------------------------LF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 209 MNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 288
Cdd:cd03685  76 TAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 289 ACCCGNIFS----------YLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALV 358
Cdd:cd03685 156 GACIAAGLSqggstslrldFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMI 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 359 AAFVLRSINPFGNSR---------LVLFYVeYHTP--WYLFELFPFILLGVFGGLWGAFFIRANIAWCR-RRKSTKFGK- 425
Cdd:cd03685 236 VTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRfRKRINHKGKl 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 426 YPVLEVIIVAAITAVIAFPnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagigvysaiWQLCL 505
Cdd:cd03685 315 LKVLEALLVSLVTSVVAFP--------------------------------------------------------QTLLI 338

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 506 ALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQlayyhhdwFIFKEWcevgadcITPGLYAMVGAAACLGG 585
Cdd:cd03685 339 FFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGS--------YFGFTS-------IDPGLYALLGAAAFLGG 403

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 55770838 586 VTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFgREGIYEAHIRLNGYPFL 642
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. ...
 205-642 2.25e-82

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: 270.27  E-value: 2.25e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 205 GSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGP 284
Cdd:cd03683  39 GNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGP 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 285 LVHVACCCGNIFSYLFPKYS---TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAF 361
Cdd:cd03683 119 FVHISSIVAALLSKLTTFFSgiyENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAF 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 362 VLRSINPF---GNSRLVLFYVEYHT--PWYLFELFPFILLGVFGGLWGAFFIRAN--IAWCRRRK---STKFGKYPVLEV 431
Cdd:cd03683 199 TFRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHrkIVRFRRKNrlfSKFLKRSPLLYP 278

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 432 IIVAAITAVIAFPnpytrlntselikelftdcgplessslcdyrndmnaskivddipdrpagigvysaIWQLCLALIFKI 511
Cdd:cd03683 279 AIVALLTAVLTFP-------------------------------------------------------FLTLFLFIVVKF 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 512 IMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGiavEQLAYyhhdWFIFKEWcEVGADCITPGLYAMVGAAACLGGVTRmTV 591
Cdd:cd03683 304 VLTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAV----LFPEGIR-GGISNPIGPGGYAVVGAAAFSGAVTH-TV 374

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 55770838 592 SLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGReGIYEAHIRLNGYPFL 642
Cdd:cd03683 375 SVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQP-SIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 136-617 8.64e-61

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: 210.50  E-value: 8.64e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 136 GLASGALAGLIDIAADWMTDLKEGICLSALwynheqccwgsnettfeerdkcpqwktwaeliigqaeGPGSYImnyIMYI 215
Cdd:cd00400   1 GVLSGLGAVLFRLLIELLQNLLFGGLPGEL-------------------------------------AAGSLS---PLYI 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 216 FWALSFAFLAVSLVKVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGN 294
Cdd:cd00400  41 LLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGS 117

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 295 IFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNsrl 374
Cdd:cd00400 118 WLGRRLR---LSRNDRRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEP--- 191

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 375 vLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKstKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSE 454
Cdd:cd00400 192 -AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYG 268

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 455 LIkelftdcgplessslcdyrndmnaskivddipdrPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIG 534
Cdd:cd00400 269 AI----------------------------------LLALAGELSLLLLLLLLLLKLLATALTLGSGFPGGVFAPSLFIG 314

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 535 AIAGRIVGIAVEQLAYyhhdwfifkewcevgADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAV 614
Cdd:cd00400 315 AALGAAFGLLLPALFP---------------GLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLMLAV 379


                ...
gi 55770838 615 MTS 617
Cdd:cd00400 380 VIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
129-635 3.09e-55

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 196.13  E-value: 3.09e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 129 WLVVTLTGLASGALAGLIDIAADWMTDLkegiclsalwynheqccwgsnettfeerdkcpqwkTWAELIIGQAEGPGSYI 208
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHL-----------------------------------FLGGLLSAAGSHLPPWL 52

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 209 mnyimyIFWALSFAFLAVS-LVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVH 287
Cdd:COG0038  53 ------VLLLPPLGGLLVGlLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQ 124

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 288 VACCCGNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSIn 367
Cdd:COG0038 125 IGAAIGSLLGRLLR---LSPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 368 pFGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRAnIAWCRRRkSTKFGKYPVLEVIIVAAITAVIAFPNPY 447
Cdd:COG0038 201 -FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIGGLLVGLLGLFLPQ 275

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 448 TRLNTSELIKELFTdcGPLessslcdyrndmnaskivddipdrpagigvysAIWQLCLALIFKIIMTVFTFGIKVPSGLF 527
Cdd:COG0038 276 VLGSGYGLIEALLN--GEL--------------------------------SLLLLLLLLLLKLLATALTLGSGGPGGIF 321

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 528 IPSMAIGAIAGRIVGIAVEQLayyhhdwfifkewceVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYI 607
Cdd:COG0038 322 APSLFIGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLL 386

                       490       500
                ....*....|....*....|....*...
gi 55770838 608 VPLMAAVMTSKWVGDAFGREGIYEAHIR 635
Cdd:COG0038 387 LPLMIACVIAYLVSRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 211-632 1.49e-51

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: 185.44  E-value: 1.49e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 211 YIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVAC 290
Cdd:cd01031  37 LLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 291 CCGNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFG 370
Cdd:cd01031 115 AIGQGVSKWFK---TSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 371 nsrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIA---WCRRRKSTKfgkyPVLEVIIVAAITAVIAFPNPY 447
Cdd:cd01031 192 ----PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKsqdLYRKLKKLP----RELRVLLPGLLIGPLGLLLPE 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 448 TRLNTSELIKELFTdcGPLessslcdyrndmnaskivddipdrpagigvysAIWQLCLALIFKIIMTVFTFGIKVPSGLF 527
Cdd:cd01031 264 ALGGGHGLILSLAG--GNF--------------------------------SISLLLLIFVLRFIFTMLSYGSGAPGGIF 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 528 IPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewcevgadciTPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYI 607
Cdd:cd01031 310 APMLALGALLGLLFGTILVQLGPIPIS---------------APATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLL 374

                       410       420
                ....*....|....*....|....*
gi 55770838 608 VPLMAAVMTSKWVGDAFGREGIYEA 632
Cdd:cd01031 375 LPLMVVCLVAYLVADLLGGKPIYEA 399
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 653-803 4.94e-47

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: 162.69  E-value: 4.94e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 653 LAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESarkkqegivgssrv 732
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55770838 733 cfaqhtpslpaesprplKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 803
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 214-630 2.93e-28

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


Pssm-ID: 238506 [Multi-domain]  Cd Length: 390  Bit Score: 117.71  E-value: 2.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 214 YIFWALSFA--FLAVSLVKVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 288
Cdd:cd01034  27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 289 ACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFVLR 364
Cdd:cd01034 107 GAAVMLAIGRRLPKWGGLSE--RGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 365 SINPFGNSRLVLfyveyhTPWYLfeLFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFG---KYPVLEVIIVAAITAVI 441
Cdd:cd01034 185 NYPYFGVAAVAL------PLGEA--WLLVLVCGVVGGLAGGLFARLLVALSSGLPGWVRRfrrRRPVLFAALCGLALALI 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 442 AFPNPYTRLNTSELIkelftdcgplessslcdyrndmnaskivddipDRPAGIGVYSAIWQLCLAlifKIIMTVFTFGIK 521
Cdd:cd01034 257 GLVSGGLTFGTGYLQ--------------------------------ARAALEGGGGLPLWFGLL---KFLATLLSYWSG 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 522 VPSGLFIPSMAIGAiagrIVGIAVEQLAYYHHdwfifkewcevgadcitPGLYAMVGAAACLGGVTRMTVSLVVIVFELT 601
Cdd:cd01034 302 IPGGLFAPSLAVGA----GLGSLLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVMEMT 360

                       410       420
                ....*....|....*....|....*....
gi 55770838 602 GGLEYIVPLMAAVMTSKWVGDAFGREGIY 630
Cdd:cd01034 361 GDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
204-632 2.88e-27

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 115.76  E-value: 2.88e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  204 PGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEG 283
Cdd:PRK05277  37 ADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  284 PLVHVACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAF 361
Cdd:PRK05277 115 PTVQMGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATI 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  362 VLRSINpfGNSrlVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFF---IRANIAWCRRRKSTKFGKYpVLEVIIVAAIT 438
Cdd:PRK05277 193 VFRLFN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRW-VLMGGAVGGLC 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  439 AVIAFPNPYTRLNTSELIKELFTdcgplessslcdyrndmnaskivddipdrpagiGVYSaIWQLCLALIFKIIMTVFTF 518
Cdd:PRK05277 268 GLLGLLAPAAVGGGFNLIPIALA---------------------------------GNFS-IGMLLFIFVARFITTLLCF 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  519 GIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVF 598
Cdd:PRK05277 314 GSGAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVL 378

                        410       420       430
                 ....*....|....*....|....*....|....
gi 55770838  599 ELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 632
Cdd:PRK05277 379 EMTDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
263-713 2.34e-19

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 92.50  E-value: 2.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  263 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYL--FPKystneAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEV 340
Cdd:PRK01862 119 LWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFahFDP-----PRLRLLVACGAAAGITSAYNAPIAGAFFVAEIV 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  341 SYYFPLKTLWRSFFAALVAAFVLRSinpFGNSRlVLFYVEYH---TPWylfELFPFILLGVFGGLWGAFFIRAniawcRR 417
Cdd:PRK01862 194 LGSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRL-----LD 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  418 RKSTKFGKYPVLEVIIVA---AITAVIAFPNPYTRLNTSELIKELftdcgpLESSSLcdyrndmnaskivddipdrpagi 494
Cdd:PRK01862 262 ASKNQFKRLPVPLPVRLAlggLLVGVISVWVPEVWGNGYSVVNTI------LHAPWT----------------------- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  495 gvysaiWQ-LCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfifkeWCEVGADcitPGL 573
Cdd:PRK01862 313 ------WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHAL------------WPGHTSA---PFA 371

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  574 YAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNgypflDAKEEFTH--T 651
Cdd:PRK01862 372 YAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLRRH-----QDEAERERlrT 446

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55770838  652 TLAADVMRPRrndpplAVLTQDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLT 713
Cdd:PRK01862 447 TQMRELIQPA------QTVVPPTASVADMTRVFLEYPVKYLYVV--DDDGRFRGAVALKDIT 500
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
653-809 2.89e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 73.36  E-value: 2.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 653 LAADVMrprrnDPPLAVLTQDnMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKKQegivgssrv 732
Cdd:COG3448   3 TVRDIM-----TRDVVTVSPD-TTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE--------- 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770838 733 cfaqhtpslPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQTAN 809
Cdd:COG3448  66 ---------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
569-804 1.43e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 73.38  E-value: 1.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 569 ITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGdAFGREGIYEAHIRLNGYPFLDAKEEF 648
Cdd:COG2524   4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 649 THTTLAADVMRPrrndpPLAVLTQDnMTVDDIENMINETSYNGFPVImskESQRLVGFALRRDLTIAIESARKKQEgivg 728
Cdd:COG2524  83 VLKMKVKDIMTK-----DVITVSPD-TTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55770838 729 ssrvcfaqhtpslpaesprpLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHM 804
Cdd:COG2524 150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 260-617 7.05e-13

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: 71.17  E-value: 7.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 260 WTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkySTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE- 338
Cdd:cd01033  83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWL---GLTVADRRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 339 ---EVSyyfplktlWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLfeLFPF-ILLGVFGGLWGAFFIRANiAW 414
Cdd:cd01033 160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTP--LLIWaLLAGPVLGVVAAGFRRLS-QA 228

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 415 CRRRKSTkfGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDcgplessslcdyrndmnaskivddipdrpaGI 494
Cdd:cd01033 229 ARAKRPK--GKRILWQMPLAFLVIGLLSIFFPQILGNGRALAQLAFST------------------------------TL 276

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 495 GVYSAIWQLCLalifKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIaveqlaYYHHDWFIfkewcevgadcITPGLY 574
Cdd:cd01033 277 TLSLLLILLVL----KIVATLLALRAGAYGGLLTPSLALGALLGALLGI------VWNALLPP-----------LSIAAF 335

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 55770838 575 AMVGAAACLGGVTRMTVSLVVIVFELTG-GLEYIVPLMAAVMTS 617
Cdd:cd01033 336 ALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
647-806 8.00e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 66.09  E-value: 8.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 647 EFTHTTLAADVMRprRNDPplAVLTqDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLtiaiesarkkqegi 726
Cdd:COG4109  11 TFKEILLVEDIMT--LEDV--ATLS-EDDTVEDALELLEKTGHSRFPVV--DENGRLVGIVTSKDI-------------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 727 vgssrvcfaqhtpslpAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 805
Cdd:COG4109  70 ----------------LGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKALQ 133


                .
gi 55770838 806 Q 806
Cdd:COG4109 134 K 134
CBS COG0517
CBS domain [Signal transduction mechanisms];
653-806 1.04e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 65.66  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 653 LAADVMRPrrnDPPLAvltQDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESarkkqegivgssrv 732
Cdd:COG0517   2 KVKDIMTT---DVVTV---SPDATVREALELMSEKRIGGLPVV--DEDGKLVGIVTDRDLRRALAA-------------- 59

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55770838 733 cfaqhtpslPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLV-THNGRLLGIITKKDILRHMAQ 806
Cdd:COG0517  60 ---------EGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 673-802 3.54e-10

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 58.02  E-value: 3.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 673 DNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKkqegivgssrvcfaqhtpslpaesPRPLKLR 752
Cdd:cd02205   9 PDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRALVEGGL------------------------ALDTPVA 62

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 55770838 753 SILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILR 802
Cdd:cd02205  63 EVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 654-806 3.72e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 55.22  E-value: 3.72e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 654 AADVMRprrnDPPLAVltQDNMTVDDIENMINETSYNGFPVImsKESQRLVGFALRRDLTIAIESARKkqegivgssrvc 733
Cdd:COG2905   1 VKDIMS----RDVVTV--SPDATVREAARLMTEKGVGSLVVV--DDDGRLVGIITDRDLRRRVLAEGL------------ 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55770838 734 faqhtpslpaeSPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQ 806
Cdd:COG2905  61 -----------DPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSE 122
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 759-802 4.44e-09

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: 52.90  E-value: 4.44e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 55770838    759 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILR 802
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
749-805 5.64e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 52.18  E-value: 5.64e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 55770838 749 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHMA 805
Cdd:COG0517   1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVdEDGKLVGIVTDRDLRRALA 58
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 751-805 2.02e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 48.36  E-value: 2.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 55770838   751 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 805
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 656-802 2.91e-07

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


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 49.49  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 656 DVMRPRrndpplAVLTQDNMTVDDIENMINETSYNGFPVImskESQRLVGFalrrdltIAIESARKKQEGIVGSSRVcfa 735
Cdd:cd04801   1 DIMTPE------VVTVTPEMTVSELLDRMFEEKHLGYPVV---ENGRLVGI-------VTLEDIRKVPEVEREATRV--- 61

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 736 qhtpslpaesprplklRSILDMSPFTVTDHTPmeiVVDIFRKL---GLRQCLVTHNGRLLGIITKKDILR 802
Cdd:cd04801  62 ----------------RDVMTKDVITVSPDAD---AMEALKLMsqnNIGRLPVVEDGELVGIISRTDLMR 112
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 674-802 3.82e-07

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: 49.03  E-value: 3.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 674 NMTVDDIENMINETSYNGFPVImskESQRLVGFALRRDltiaIESARKKQEGivgssrvcfaqHTPslpaesprplkLRS 753
Cdd:cd04595  10 DTTIEEARKIMLRYGHTGLPVV---EDGKLVGIISRRD----VDKAKHHGLG-----------HAP-----------VKG 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 55770838 754 ILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 802
Cdd:cd04595  61 YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLR 109
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
749-811 1.92e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 47.94  E-value: 1.92e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55770838 749 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHMAQTANQD 811
Cdd:COG3448   2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLPDRLDE 65
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 757-808 9.71e-06

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 45.88  E-value: 9.71e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 55770838 757 MS--PFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQTA 808
Cdd:cd04584   6 MTknVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 745-804 4.05e-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: 43.86  E-value: 4.05e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55770838 745 SPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLrqcL----VTHNGRLLGIITKKDILRHM 804
Cdd:cd04606  61 ADPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 757-802 4.10e-05

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: 43.96  E-value: 4.10e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 55770838 757 MS--PFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 802
Cdd:cd04586  89 MTrpVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
747-806 4.88e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 45.26  E-value: 4.88e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 747 RPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQ 806
Cdd:COG2524  84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 757-800 6.71e-05

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 46.12  E-value: 6.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 55770838  757 MSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDI 800
Cdd:PTZ00314 104 MDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 693-802 1.07e-04

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: 42.79  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 693 PVImskESQRLVGFALRRDLTIAIESarkkqegIVGSSRVcfaQHTPSLPAEsprpLKLRSIldMS--PFTVTDHTPMEI 770
Cdd:cd04584  35 PVV---DDGKLVGIVTDRDLLRASPS-------KATSLSI---YELNYLLSK----IPVKDI--MTkdVITVSPDDTVEE 95

                        90       100       110
                ....*....|....*....|....*....|....*
gi 55770838 771 VVDIFR--KLGlrqCL-VTHNGRLLGIITKKDILR 802
Cdd:cd04584  96 AALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 759-815 2.10e-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: 41.46  E-value: 2.10e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 55770838 759 PFTVTDHTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILRHMAQTANQDPASI 815
Cdd:cd02205   4 VVTVDPDTTVREALELMAENGIGALPVVDdDGKLVGIVTERDILRALVEGGLALDTPV 61
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 751-815 3.33e-04

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: 41.37  E-value: 3.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 751 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQC----------------LVTHNGRLLGIITKKDILRHMAQTANQDPAS 814
Cdd:cd04620   1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                .
gi 55770838 815 I 815
Cdd:cd04620  81 I 81
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 276-443 1.25e-03

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


Pssm-ID: 239654 [Multi-domain]  Cd Length: 378  Bit Score: 41.80  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 276 GLSLGKEGPLVHVAcccGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlkt 348
Cdd:cd03682  92 GGSAGREGTAVQMG---GSLADAFGRVFKLPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP--- 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 349 lwrSFFAALVAAFVLRSINPFGNSRLVLFYVEYhTPWYLFELfpfILLGVFGGLWGAFFIRAnIAWCrRRKSTKFGKYPV 428
Cdd:cd03682 166 ---CLVAAIVADWVSHALGLEHTHYHIVFIPTL-DPLLFVKV---ILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNPY 236

                       170
                ....*....|....*
gi 55770838 429 LEVIIVAAITAVIAF 443
Cdd:cd03682 237 LRPFVGGLLIILLVY 251
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 263-633 1.25e-03

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 42.07  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  263 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSY 342
Cdd:PRK01610 101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRF----TPRQEWKLWIACGAAAGMASAYHAPLAGSLFIAEILFG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  343 YFPLKTLWRSFFAALVAAFVLRSINPfgnSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTK 422
Cdd:PRK01610 177 TLMLASLGPVVISAVVALLTTNLLNG---SDALLYNVQLSVTVQARDYALIISTGLLAGLCGPLLLTLMNASHRGFVSLK 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  423 FGkyPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDcgplessslcdyrndmnaskivddipdrPAGIGVYSAIwq 502
Cdd:PRK01610 254 LA--PPWQLALGGLIVGLLSLFTPAVWGNGYSVVQSFLTA----------------------------PPLLMLIAGI-- 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838  503 lclaLIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIaveqlayyhhdwfIFKEWCEVGADciTPGLYAMVGAAAC 582
Cdd:PRK01610 302 ----FLCKLLAVLASSGSGAPGGVFTPTLFVGLAIGMLYGR-------------SLGLWLPDGEE--ITLLLGLTGMATL 362

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55770838  583 LGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAH 633
Cdd:PRK01610 363 LAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIASVISRTLRRDSIYRQH 413
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 758-800 1.60e-03

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: 39.02  E-value: 1.60e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 55770838 758 SP-FTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDI 800
Cdd:cd04595   2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 45
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 751-815 1.77e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.04  E-value: 1.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55770838 751 LRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHMAQtANQDPASI 815
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVdDDGRLVGIITDRDLRRRVLA-EGLDPLDT 65
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
745-811 1.81e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 41.59  E-value: 1.81e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55770838 745 SPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQTANQD 811
Cdd:COG2239 189 ADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLL-ALpvVDEEGRLVGIITVDDVVDVIEEEATED 256
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 749-802 3.15e-03

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 38.36  E-value: 3.15e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 55770838 749 LKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 802
Cdd:cd04631  75 VPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILR 128
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 674-802 6.70e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 37.01  E-value: 6.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55770838 674 NMTVDDIENMINETSYNGFPVIMSKEsqRLVGFALRRDLTIaiesarkkqegivgssrvcfaqhtpslpaESPRPLKLRS 753
Cdd:cd04601  10 DATVADVLELKAEYGISGVPVTEDGG--KLVGIVTSRDIRF-----------------------------ETDLSTPVSE 58

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55770838 754 IldMSPF----TVTDHTPMEIVVDIFR--KLGlRQCLVTHNGRLLGIITKKDILR 802
Cdd:cd04601  59 V--MTPDerlvTAPEGITLEEAKEILHkhKIE-KLPIVDDNGELVGLITRKDIEK 110
 
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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