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Conserved domains on  [gi|13542693|gb|AAH05553|]
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Clcn4-2 protein [synthetic construct]

Protein Classification

chloride channel protein( domain architecture ID 10132694)

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

CATH:  1.10.3080.10
Gene Ontology:  GO:0006821|GO:0005247|GO:0055085
PubMed:  11182894|9207144|9046241
SCOP:  4003598

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 65-540 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: 670.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  65 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 144
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 225 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 304
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 305 LFYVEYHTPW-------------------------------RRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSEL 353
Cdd:cd03684 193 LFEVEYDRDWhyfelipfillgifgglygaffikanikwarFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 354 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 433
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 434 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 513
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 13542693 514 TSKWVADAFGKEGIYEAHIHLNGYPFL 540
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 ...
 551-701 1.40e-44

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


:

Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 155.37  E-value: 1.40e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 551 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 630
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13542693 631 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 701
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 65-540 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: 670.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  65 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 144
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 225 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 304
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 305 LFYVEYHTPW-------------------------------RRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSEL 353
Cdd:cd03684 193 LFEVEYDRDWhyfelipfillgifgglygaffikanikwarFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 354 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 433
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 434 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 513
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 13542693 514 TSKWVADAFGKEGIYEAHIHLNGYPFL 540
Cdd:cd03684 419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 150-520 6.01e-78

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: 253.24  E-value: 6.01e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   150 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 229
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   230 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 309
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   310 YHTPW------------------------------RRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFN 359
Cdd:pfam00654 153 EPGSLsllelplfillgilcgllgalfnrlllkvqRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFN 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   360 DCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMV 439
Cdd:pfam00654 233 GN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAF 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   440 GIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVA 519
Cdd:pfam00654 279 GLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVS 343


                  .
gi 13542693   520 D 520
Cdd:pfam00654 344 R 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
58-533 2.37e-47

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 173.02  E-value: 2.37e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  58 WVVMLLIGLLAGTLAGVIDLAVDWMTDLkegvclsafwysheqccwtsnettfedrdkcplwqkwseLLLSQSEGASAYI 137
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHL---------------------------------------FLGGLLSAAGSHL 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 138 LNYLmYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:COG0038  49 PPWL-VLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQI 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 218 ACCCGNFFSSLFsKYSKNEgkRREVLSaaaaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInp 297
Cdd:COG0038 126 GAAIGSLLGRLL-RLSPED--RRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL-- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 298 FGNSrlVLFYVEYHTPW-----------------------------RRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQ 348
Cdd:COG0038 201 FGNG--PLFGVPSVPALsllelplylllgilaglvgvlfnrlllkvERLFKRLKLPPWLRPAIGGLLVGLLGLFLPQVLG 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 349 STSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVITIFTFGMKIPSGLFIPS 428
Cdd:COG0038 279 SGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFAPS 324

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 429 MAVGAMAGRMVGIGVEQLAyhhhdwiifrnwcrPGADcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPL 508
Cdd:COG0038 325 LFIGALLGAAFGLLLNLLF--------------PGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389

                       490       500
                ....*....|....*....|....*
gi 13542693 509 MAAAVTSKWVADAFGKEGIYEAHIH 533
Cdd:COG0038 390 MIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 551-701 1.40e-44

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


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 155.37  E-value: 1.40e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 551 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 630
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13542693 631 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 701
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
63-572 2.43e-24

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 106.51  E-value: 2.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   63 LIGLLAGTLAGVIDLAVDWMtdlkegvclsafwysheqccwtsnettfedrdkcplwQKWSELLLSQSEGAsaYILNYLM 142
Cdd:PRK05277   6 VVGTLTGLVGVAFELAVDWV-------------------------------------QNQRLGLLASVADN--GLLLWIV 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  143 YILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCG 222
Cdd:PRK05277  47 AFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIG 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  223 NFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYF----------------------------- 273
Cdd:PRK05277 125 RMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMRPQFryslisikavfigvimativfrlfngeqa 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  274 ----------PLKTLWrsFFAALVAAFTLrsINPFGNsRLVL----FYVEYHtPWRRKttrlgRYpVLEVIAVTAVTAIV 339
Cdd:PRK05277 203 vievgkfsapPLNTLW--LFLLLGIIFGI--FGVLFN-KLLLrtqdLFDRLH-GGNKK-----RW-VLMGGAVGGLCGLL 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  340 AYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVITIFTFGMK 419
Cdd:PRK05277 271 GLLAPAAVGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCFGSG 316

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  420 IPSGLFIPSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMFELT 499
Cdd:PRK05277 317 APGGIFAPMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVLEMT 381

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13542693  500 GGLEYIVPLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 572
Cdd:PRK05277 382 DNYQLILPLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
467-702 1.50e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 72.99  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 467 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 546
Cdd:COG2524   4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 547 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 626
Cdd:COG2524  83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13542693 627 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 702
Cdd:COG2524 154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 657-700 1.08e-07

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: 48.66  E-value: 1.08e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 13542693    657 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 700
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 649-703 3.33e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 47.59  E-value: 3.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13542693   649 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 703
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 656-698 8.33e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 8.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 13542693  656 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 698
Cdd:PTZ00314 105 DPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 65-540 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: 670.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  65 GLLAGTLAGVIDLAVDWMTDLKEGVClsafwysheqccwtsnettfedrdkcplwqkwselllsqsegasayilNYLMYI 144
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd03684  33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 225 FSSLFSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLV 304
Cdd:cd03684 113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 305 LFYVEYHTPW-------------------------------RRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSEL 353
Cdd:cd03684 193 LFEVEYDRDWhyfelipfillgifgglygaffikanikwarFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 354 ISELFNDCGALESSQLCDYindpnmtrpvddiPDRPAGVGVYTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGA 433
Cdd:cd03684 273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 434 MAGRMVGIGVEQLAYHHHDWIIFrNWCRPGADCVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAV 513
Cdd:cd03684 340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                       490       500
                ....*....|....*....|....*..
gi 13542693 514 TSKWVADAFGKEGIYEAHIHLNGYPFL 540
Cdd:cd03684 419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 65-529 2.27e-118

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: 361.28  E-value: 2.27e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  65 GLLAGTLAGVIDLAVDWMTDLKEGVCLSAFwysheqccwtsnettfedrdkcplwqkwselllsqsegaSAYILNYLMYI 144
Cdd:cd01036   1 GLLMGLVAVVLDYAVESSLDAGQWLLRRIP---------------------------------------GSYLLGYLMWV 41

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 145 LWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNF 224
Cdd:cd01036  42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 225 FSSLFSKYS----------KNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRS 294
Cdd:cd01036 122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 295 INPFGNSR----------LVLFYVEYHTP--------------------------------WRR--KTTRLGRYPVLEVI 330
Cdd:cd01036 202 YNSFNSGFelldrssamfLSLTVFELHVPlnlyefiptvvigvicgllaalfvrlsiiflrWRRrlLFRKTARYRVLEPV 281

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 331 AVTAVTAIVAYPnpytrqstseliselfndcgalessqlcdyindpnmtrpvddipdrpagvgvytamWQLALALIFKIV 410
Cdd:cd01036 282 LFTLIYSTIHYA--------------------------------------------------------PTLLLFLLIYFW 305

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 411 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHDwiifrnwCRPGADCVTPGLYAMVGAAACLGGVTRMTVS 490
Cdd:cd01036 306 MSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRLTFS 378

                       490       500       510
                ....*....|....*....|....*....|....*....
gi 13542693 491 LVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYE 529
Cdd:cd01036 379 ICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 58-540 1.63e-83

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: 272.22  E-value: 1.63e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  58 WVVMLLIGLLAGTLAGVIDLAVDWMTDLKegvcLSAFWYSHEQCCwtsnettfedrdkcplwqkwselllsqsegasaYI 137
Cdd:cd03685  33 WIICLLIGIFTGLVAYFIDLAVENLAGLK----FLVVKNYIEKGR---------------------------------LF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 138 LNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:cd03685  76 TAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHI 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 218 ACCCGNFFSSLFSK----------YSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALV 287
Cdd:cd03685 156 GACIAAGLSQGGSTslrldfrwfrYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMI 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 288 AAFTLRS------------------INPFGNSRLVLFYV------------------------EYHTPWRRKTTRLG-RY 324
Cdd:cd03685 236 VTFTLNFflsgcnsgkcglfgpgglIMFDGSSTKYLYTYfelipfmligviggllgalfnhlnHKVTRFRKRINHKGkLL 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 325 PVLEVIAVTAVTAIVAYpnpytrqstseliselfndcgalessqlcdyindpnmtrpvddipdrpagvgvytaMWQLALA 404
Cdd:cd03685 316 KVLEALLVSLVTSVVAF--------------------------------------------------------PQTLLIF 339

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 405 LIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLayhhhdwiifrnwcrPGADCVTPGLYAMVGAAACLGGV 484
Cdd:cd03685 340 FVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSY---------------FGFTSIDPGLYALLGAAAFLGGV 404

                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13542693 485 TRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFgKEGIYEAHIHLNGYPFL 540
Cdd:cd03685 405 MRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 150-520 6.01e-78

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: 253.24  E-value: 6.01e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   150 FAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLF 229
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   230 SKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 309
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   310 YHTPW------------------------------RRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQSTSELISELFN 359
Cdd:pfam00654 153 EPGSLsllelplfillgilcgllgalfnrlllkvqRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFN 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   360 DCgalessqlcdyindpnmtrpvddipdrpagvgvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMV 439
Cdd:pfam00654 233 GN----------------------------------TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAF 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   440 GIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVA 519
Cdd:pfam00654 279 GLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVS 343


                  .
gi 13542693   520 D 520
Cdd:pfam00654 344 R 344
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 135-540 8.79e-69

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: 231.75  E-value: 8.79e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 135 AYILNYLMYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPL 214
Cdd:cd03683  40 NSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPF 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 215 VHVACCCGNFFSSL---FSKYSKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFT 291
Cdd:cd03683 120 VHISSIVAALLSKLttfFSGIYENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFT 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 292 LRSIN---------------------PFGNSRLVLF-------------YVEYHTP---WRRK----TTRLGRYPVLEVI 330
Cdd:cd03683 200 FRLLAvffsdqetitalfkttffvdfPFDVQELPIFallgiicgllgalFVFLHRKivrFRRKnrlfSKFLKRSPLLYPA 279

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 331 AVTAVTAIVAYPnpytrqstseliselfndcgalessqlcdYINdpnmtrpvddipdrpagvgvytamwqLALALIFKIV 410
Cdd:cd03683 280 IVALLTAVLTFP-----------------------------FLT--------------------------LFLFIVVKFV 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 411 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGigvEQLAYHHHDWIifrnwCRPGADCVTPGLYAMVGAAACLGGVTRmTVS 490
Cdd:cd03683 305 LTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAVLFPEGI-----RGGISNPIGPGGYAVVGAAAFSGAVTH-TVS 375

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 13542693 491 LVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGkEGIYEAHIHLNGYPFL 540
Cdd:cd03683 376 VAVIIFELTGQISHLLPVLIAVLISNAVAQFLQ-PSIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 118-515 1.10e-47

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: 173.13  E-value: 1.10e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 118 LWQKWSELLLSQSEGASAYILNYL-MYILWALLFAFLAVSLVRVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLLIKT 195
Cdd:cd00400  13 LLIELLQNLLFGGLPGELAAGSLSpLYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKF 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 196 VTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPL 275
Cdd:cd00400  90 LASALTLGSGGSVGREGPIVQIGAAIGSWLGRRL-RLSRND--RRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSV 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 276 KTL----WRSFFAALVAAFTLRSINPFGNSRLVLF---------------------YVEYHTPWRRKTTRLGRYPVLEVI 330
Cdd:cd00400 167 ASLipvlLASVAAALVSRLLFGAEPAFGVPLYDPLsllelplylllgllaglvgvlFVRLLYKIERLFRRLPIPPWLRPA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 331 AVTAVTAIVAYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvgVYTAMWQLALALIFKIV 410
Cdd:cd00400 247 LGGLLLGLLGLFLPQVLGSGYGAILLALA----------------------------------GELSLLLLLLLLLLKLL 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 411 ITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHHdwiifrnwcrpgadcVTPGLYAMVGAAACLGGVTRMTVS 490
Cdd:cd00400 293 ATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALFPGLV---------------ASPGAYALVGMAALLAAVLRAPLT 357

                       410       420
                ....*....|....*....|....*
gi 13542693 491 LVVIMFELTGGLEYIVPLMAAAVTS 515
Cdd:cd00400 358 AILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
58-533 2.37e-47

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 173.02  E-value: 2.37e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  58 WVVMLLIGLLAGTLAGVIDLAVDWMTDLkegvclsafwysheqccwtsnettfedrdkcplwqkwseLLLSQSEGASAYI 137
Cdd:COG0038   8 LLLAVLVGILAGLAAVLFRLLLELATHL---------------------------------------FLGGLLSAAGSHL 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 138 LNYLmYILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:COG0038  49 PPWL-VLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQI 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 218 ACCCGNFFSSLFsKYSKNEgkRREVLSaaaaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInp 297
Cdd:COG0038 126 GAAIGSLLGRLL-RLSPED--RRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVSRLL-- 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 298 FGNSrlVLFYVEYHTPW-----------------------------RRKTTRLGRYPVLEVIAVTAVTAIVAYPNPYTRQ 348
Cdd:COG0038 201 FGNG--PLFGVPSVPALsllelplylllgilaglvgvlfnrlllkvERLFKRLKLPPWLRPAIGGLLVGLLGLFLPQVLG 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 349 STSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYTAMWqLALALIFKIVITIFTFGMKIPSGLFIPS 428
Cdd:COG0038 279 SGYGLIEALLN---------------------------------GELSLLL-LLLLLLLKLLATALTLGSGGPGGIFAPS 324

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 429 MAVGAMAGRMVGIGVEQLAyhhhdwiifrnwcrPGADcVTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPL 508
Cdd:COG0038 325 LFIGALLGAAFGLLLNLLF--------------PGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389

                       490       500
                ....*....|....*....|....*
gi 13542693 509 MAAAVTSKWVADAFGKEGIYEAHIH 533
Cdd:COG0038 390 MIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 551-701 1.40e-44

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


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 155.37  E-value: 1.40e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 551 LATDVMRPrrgepPLSVLTQDsMTVEDVETLIKETDYNGFPVLVSRDSERLIGFAQRRELILAIKNarqrqegivsnsim 630
Cdd:cd04591   1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13542693 631 yfteeppelpansphplKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRH 701
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 64-530 1.69e-42

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: 158.86  E-value: 1.69e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  64 IGLLAGTLAGVIDLAVDWMTDLKEgvclsaFWYSHeqccwtsnettfedrdkcplwqkwselllsqsegASAYILNYLMY 143
Cdd:cd01031   1 IGLLAGLVAVLFRLGIDKLGNLRL------SLYDF----------------------------------AANNPPLLLVL 40

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 144 ILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGN 223
Cdd:cd01031  41 PLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQ 118

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 224 FFSSLFsKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPfgnSRL 303
Cdd:cd01031 119 GVSKWF-KTSPEE--RRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFG---LGP 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 304 VLfyveYHTPWrrKTTRLGRYPVLEVIAVTAvtAIVAYpnpytrqstseliseLFNDcGALESSQLCDYIND-------- 375
Cdd:cd01031 193 VL----SIPPL--PALPLKSYWLLLLLGIIA--GLLGY---------------LFNR-SLLKSQDLYRKLKKlprelrvl 248

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 376 -------------PNMTRPVDDIPDRPAGVGvyTAMWQLALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIG 442
Cdd:cd01031 249 lpglligplglllPEALGGGHGLILSLAGGN--FSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLGLLFGTI 326

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 443 VEQLAyhhHDWIIFrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAF 522
Cdd:cd01031 327 LVQLG---PIPISA------------PATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMVVCLVAYLVADLL 391


                ....*...
gi 13542693 523 GKEGIYEA 530
Cdd:cd01031 392 GGKPIYEA 399
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
63-572 2.43e-24

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 106.51  E-value: 2.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693   63 LIGLLAGTLAGVIDLAVDWMtdlkegvclsafwysheqccwtsnettfedrdkcplwQKWSELLLSQSEGAsaYILNYLM 142
Cdd:PRK05277   6 VVGTLTGLVGVAFELAVDWV-------------------------------------QNQRLGLLASVADN--GLLLWIV 46

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  143 YILWALLFAFLAVSLVRVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCG 222
Cdd:PRK05277  47 AFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIG 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  223 NFFSSLFSKYSKNEgkRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYF----------------------------- 273
Cdd:PRK05277 125 RMVLDIFRLRSDEA--RHTLLAAGAAAGLAAAFNAPLAGILFVIEEMRPQFryslisikavfigvimativfrlfngeqa 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  274 ----------PLKTLWrsFFAALVAAFTLrsINPFGNsRLVL----FYVEYHtPWRRKttrlgRYpVLEVIAVTAVTAIV 339
Cdd:PRK05277 203 vievgkfsapPLNTLW--LFLLLGIIFGI--FGVLFN-KLLLrtqdLFDRLH-GGNKK-----RW-VLMGGAVGGLCGLL 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  340 AYPNPYTRQSTSELISELFNdcgalessqlcdyindpnmtrpvddipdrpagvGVYtAMWQLALALIFKIVITIFTFGMK 419
Cdd:PRK05277 271 GLLAPAAVGGGFNLIPIALA---------------------------------GNF-SIGMLLFIFVARFITTLLCFGSG 316

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  420 IPSGLFIPSMAVGAMAGRMVGIGVEQLayhHHDWIIfrnwcrpgadcvTPGLYAMVGAAACLGGVTRMTVSLVVIMFELT 499
Cdd:PRK05277 317 APGGIFAPMLALGTLLGLAFGMVAAAL---FPQYHI------------EPGTFAIAGMGALFAATVRAPLTGIVLVLEMT 381

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13542693  500 GGLEYIVPLMAAAVTSKWVADAFGKEGIYEAhihlngypfldvkdeFTHRTLATDvMRPRRGEPPLSVLTQDS 572
Cdd:PRK05277 382 DNYQLILPLIITCLGATLLAQFLGGKPIYSA---------------LLERTLAKQ-EAEQAARSKAAPASENT 438
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 143-528 1.02e-21

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: 98.07  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 143 YILWALLFA--FLAVSLVRVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLLIKTVTLVLVVSSGLSLGKEGPLVHV 217
Cdd:cd01034  27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 218 ACCCGNFFSSLFSKysKNEGKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFTLR 293
Cdd:cd01034 107 GAAVMLAIGRRLPK--WGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 294 SINPFGN----------------------------SRLVLFYVEYHTPWRRKttRLGRYPVLEVIAVTAVTAIVAYpnpy 345
Cdd:cd01034 185 NYPYFGVaavalplgeawllvlvcgvvgglagglfARLLVALSSGLPGWVRR--FRRRRPVLFAALCGLALALIGL---- 258

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 346 trqSTSELIselFNDcGALESSQlcdyindpnmtrpvddipdrpAGVGVYTAMWQLALAlifKIVITIFTFGMKIPSGLF 425
Cdd:cd01034 259 ---VSGGLT---FGT-GYLQARA---------------------ALEGGGGLPLWFGLL---KFLATLLSYWSGIPGGLF 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 426 IPSMAVGAmagrmvGIG--VEQLAYHHHdwiifrnwcrpgadcvtPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLE 503
Cdd:cd01034 308 APSLAVGA------GLGslLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVMEMTGDQQ 364

                       410       420
                ....*....|....*....|....*
gi 13542693 504 YIVPLMAAAVTSKWVADAFGKEGIY 528
Cdd:cd01034 365 MLLPLLAAALLASGVSRLVCPEPLY 389
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
467-702 1.50e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 72.99  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 467 VTPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVAdAFGKEGIYEAHIHLNGYPFLDVKDEF 546
Cdd:COG2524   4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 547 THRTLATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIKNARQRQEGIVS 626
Cdd:COG2524  83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLDAPVS 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13542693 627 nSIMyfTEEPPelpansphplklrrilnlspfTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHM 702
Cdd:COG2524 154 -DIM--TRDVV---------------------TVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
192-529 2.25e-14

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 76.71  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  192 LIKTVTLVLVVSSGLSLGKEGPLVHVACCCGnffsSLFSKYSKNEGKR-REVLSAAAAAGVSVAFGAPIGGVLFSLEEVS 270
Cdd:PRK01862 119 LWRSASSLLTIGSGGSIGREGPMVQLAALAA----SLVGRFAHFDPPRlRLLVACGAAAGITSAYNAPIAGAFFVAEIVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  271 YYFPLKTLWRSFFAALVAAFTLR-----------SINPFGNSRLVLFYVEYHT------PW-----RRKTTRLGRYPVLE 328
Cdd:PRK01862 195 GSIAMESFGPLVVASVVANIVMRefagyqppyemPVFPAVTGWEVLLFVALGVlcgaaaPQflrllDASKNQFKRLPVPL 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  329 VI------AVTAVTAiVAYP----NPYTrqstseLISELFNdcgalessqlcdyindpnmTRPVddipdrpagvgvytam 398
Cdd:PRK01862 275 PVrlalggLLVGVIS-VWVPevwgNGYS------VVNTILH-------------------APWT---------------- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693  399 WQ-LALALIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHHhdwiifrnwcrpgadCVTPGLYAMVGA 477
Cdd:PRK01862 313 WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHALWPGH---------------TSAPFAYAMVGM 377

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13542693  478 AACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAVTSKWVADAFGKEGIYE 529
Cdd:PRK01862 378 GAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYE 429
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
554-707 4.77e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 66.81  E-value: 4.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 554 DVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGFAQRRELILAIKNARQRQegivsnsimyft 633
Cdd:COG3448   6 DIMTR----DVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE------------ 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13542693 634 eeppelPANSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMAQMAN 707
Cdd:COG3448  66 ------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVdDDGRLVGIVTRTDLLRALARLLE 134
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
544-705 1.78e-12

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 64.93  E-value: 1.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 544 DEFTHRTLATDVMRprrgEPPLSVLTQDsMTVEDVETLIKETDYNGFPVLvsRDSERLIGfaqrrelILAIKNARQRQEG 623
Cdd:COG4109  10 DTFKEILLVEDIMT----LEDVATLSED-DTVEDALELLEKTGHSRFPVV--DENGRLVG-------IVTSKDILGKDDD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 624 ivsnsimyfteeppelpansphpLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHM 702
Cdd:COG4109  76 -----------------------TPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKAL 132


                ...
gi 13542693 703 AQM 705
Cdd:COG4109 133 QKI 135
CBS COG0517
CBS domain [Signal transduction mechanisms];
551-704 1.09e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 59.88  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 551 LATDVMRPrrgePPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGfaqrrelilaiknarqrqegIVSNS-I 629
Cdd:COG0517   2 KVKDIMTT----DVVTV--SPDATVREALELMSEKRIGGLPVV--DEDGKLVG--------------------IVTDRdL 53

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13542693 630 MYFTEEPPELPANSPhplkLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLV-TRSGRLLGIITKKDVLRHMAQ 704
Cdd:COG0517  54 RRALAAEGKDLLDTP----VSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 562-700 3.58e-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: 57.64  E-value: 3.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 562 EPPLSVltQDSMTVEDVETLIKETDYNGFPVLvsRDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppeLPA 641
Cdd:cd02205   2 RDVVTV--DPDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRAL------------------------VEG 53

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 642 NSPHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLR 700
Cdd:cd02205  54 GLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 572-700 3.27e-09

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 55.02  E-value: 3.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 572 SMTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAIknarqrqegivsnsimyfteeppelpansPHPlKLRR 651
Cdd:cd04610  11 DDTVKDVIKLIKETGHDGFPVV---DDGKVVGYVTAKDLLGKD-----------------------------DDE-KVSE 57

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 13542693 652 IlnLSPFTVTDHTPMeTVVDIFRKLgLRQCL-----VTRSGRLLGIITKKDVLR 700
Cdd:cd04610  58 I--MSRDTVVADPDM-DITDAARVI-FRSGIsklpvVDDEGNLVGIITNMDVIR 107
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 554-705 5.64e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 54.84  E-value: 5.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 554 DVMRprrgEPPLSVltQDSMTVEDVETLIKETDYNGfpVLVSRDSERLIGFAQRRELILAIKNARqrqegivsnsimyft 633
Cdd:COG2905   3 DIMS----RDVVTV--SPDATVREAARLMTEKGVGS--LVVVDDDGRLVGIITDRDLRRRVLAEG--------------- 59

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13542693 634 EEPPELPAnsphplklRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQM 705
Cdd:COG2905  60 LDPLDTPV--------SEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 189-515 4.23e-08

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: 56.15  E-value: 4.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 189 WTLLIKTVTLVLVVSSGLSLGKEGPLVHVACCCGNFFSSLFSKYSKNegkRREVLSAAAAAGVSVAFGAPIGGVLFSLEE 268
Cdd:cd01033  83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVAD---RRLLVACAAGAGLAAVYNVPLAGALFALEI 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 269 VSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSrlvlfyveYHTPWRRKTTRLgryPVLEVIAVTAVTAIVAYpnpyTRQ 348
Cdd:cd01033 160 LLRTISLRSVVAALATSAIAAAVASLLKGDHPI--------YDIPPMQLSTPL---LIWALLAGPVLGVVAAG----FRR 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 349 STSELISElfndcgalessqlcdyindpnmtRPVDD--IPDRP---AGVGVYTAMW-----------QLALA-------- 404
Cdd:cd01033 225 LSQAARAK-----------------------RPKGKriLWQMPlafLVIGLLSIFFpqilgngralaQLAFSttltlsll 281

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 405 ---LIFKIVITIFTFGMKIPSGLFIPSMAVGAMAGRMVGIGVEQLAYHhhdwiifrnwcrpgadcVTPGLYAMVGAAACL 481
Cdd:cd01033 282 lilLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGIVWNALLPP-----------------LSIAAFALIGAAAFL 344

                       330       340       350
                ....*....|....*....|....*....|....*
gi 13542693 482 GGVTRMTVSLVVIMFELTG-GLEYIVPLMAAAVTS 515
Cdd:cd01033 345 AATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 657-700 1.08e-07

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: 48.66  E-value: 1.08e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 13542693    657 PFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLR 700
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
647-703 3.03e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 49.86  E-value: 3.03e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13542693 647 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVLRHMA 703
Cdd:COG0517   1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEdGKLVGIVTDRDLRRALA 58
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 649-703 3.33e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 47.59  E-value: 3.33e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13542693   649 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLRHMA 703
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
647-703 1.55e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 47.94  E-value: 1.55e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13542693 647 LKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMA 703
Cdd:COG3448   2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALL 59
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 563-700 2.29e-06

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 47.42  E-value: 2.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 563 PPLSVltQDSMTVEDVETLIKETDYNGFPVLvsrDSE-RLIGFAQRRELILAIKNARQRQEGIVSNSIMYFTEEPPELPA 641
Cdd:cd04586   4 DVVTV--TPDTSVREAARLLLEHRISGLPVV---DDDgKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLAEEYV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13542693 642 NSpHPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 700
Cdd:cd04586  79 KA-HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 657-706 1.15e-05

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 45.49  E-value: 1.15e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 13542693 657 PFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQMA 706
Cdd:cd04584  10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
645-704 2.75e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 45.64  E-value: 2.75e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 645 HPLKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLRHMAQ 704
Cdd:COG2524  84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 573-700 2.96e-05

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 43.95  E-value: 2.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 573 MTVEDVETLIKETDYNGFPVLvsrDSERLIGFAQRRELILAiknarqrqegivSNSImyFTEEPPELPANSPHPLKLRRI 652
Cdd:cd04584  17 TSLAEARELMKEHKIRHLPVV---DDGKLVGIVTDRDLLRA------------SPSK--ATSLSIYELNYLLSKIPVKDI 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 13542693 653 LNLSPFTVTDHTPMETVVDIFR--KLGlrqCL-VTRSGRLLGIITKKDVLR 700
Cdd:cd04584  80 MTKDVITVSPDDTVEEAALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 570-700 6.29e-05

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 42.46  E-value: 6.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 570 QDSMTVEDVETLIKETDYNGFPVLvsrDSE-RLIGfaqrrelILAIKNArqrqegivsnsimyfTEEPPELPansphplk 648
Cdd:cd04596   8 RETDTVRDYKQLSEETGHSRFPVV---DEEnRVVG-------IVTAKDV---------------IGKEDDTP-------- 54

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13542693 649 LRRILNLSPFTVTDHTpmeTVVDIFRKL---GLRQCLVTRSGR-LLGIITKKDVLR 700
Cdd:cd04596  55 IEKVMTKNPITVKPKT---SVASAAHMMiweGIELLPVVDENRkLLGVISRQDVLK 107
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 552-699 1.28e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 42.10  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 552 ATDVMRPRRgepplSVLTQD-SMTVEDVETLIKETDYNGFPVlVSRDSERLIGFAQRRELILAIKNARQrqegivsnsim 630
Cdd:cd04590   2 VREVMTPRT-----DVVALDaDATLEELLELILESGYSRFPV-YEGDLDNIIGVLHVKDLLAALLEGRE----------- 64

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 631 yfteeppelpansphPLKLRRILNlSPFTVTDHTPMETVVDIFRKLGLRQCLVTRS-GRLLGIITKKDVL 699
Cdd:cd04590  65 ---------------KLDLRALLR-PPLFVPETTPLDDLLEEFRKERSHMAIVVDEyGGTAGIVTLEDIL 118
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 657-713 1.50e-04

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 41.85  E-value: 1.50e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13542693 657 PFTVTDHTPMETVVDIFRKLGLRQCLVT-RSGRLLGIITKKDVLRHMAQMANQDPESI 713
Cdd:cd02205   4 VVTVDPDTTVREALELMAENGIGALPVVdDDGKLVGIVTERDILRALVEGGLALDTPV 61
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 572-702 1.88e-04

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


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 41.55  E-value: 1.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 572 SMTVEDV------ETLIKETDYNGFpvlVSRDSERLIGFAQRRELILAiknarqrqegivsnsimyfteePPELpansph 645
Cdd:cd04606  17 DWTVEEAleylrrLAPDPETIYYIY---VVDEDRRLLGVVSLRDLLLA----------------------DPDT------ 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13542693 646 plKLRRILNLSPFTVTDHTPMETVVDIFRKLGLrqcL----VTRSGRLLGIITKKDVLRHM 702
Cdd:cd04606  66 --KVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 563-701 5.42e-04

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 40.21  E-value: 5.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 563 PPLSVLTQDsmTVEDVETLIKETDYNGFPVLVsrDSERLIGFAQRRELILAIKNARQRQEGIVSnSIMYftEEPPELPAN 642
Cdd:cd04608  11 APVTVLPDD--TLGEAIEIMREYGVDQLPVVD--EDGRVVGMVTEGNLLSSLLAGRAQPSDPVS-KAMY--KQFKQVDLD 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13542693 643 SPHPlKLRRILNlspftvTDHTPMetVVDifrklglrqclvtRSGRLLGIITKKDVLRH 701
Cdd:cd04608  84 TPLG-ALSRILE------RDHFAL--VVD-------------GQGKVLGIVTRIDLLNY 120
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 656-698 8.33e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 42.65  E-value: 8.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 13542693  656 SPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGR----LLGIITKKDV 698
Cdd:PTZ00314 105 DPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 656-698 9.66e-04

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 39.40  E-value: 9.66e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 13542693 656 SP-FTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDV 698
Cdd:cd04595   2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 45
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
631-700 1.37e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.74  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13542693  631 YFTEEPPELPANSpHPlKLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQ-CLVTRSGRLLGIITKKDVLR 700
Cdd:PRK14869  54 YFGVEAPELIEDV-KP-QVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTlPVVDEEGKLLGLVSLSDLAR 122
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 649-713 1.38e-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: 1.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13542693 649 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTR-SGRLLGIITKKDVLRHMAQmANQDPESI 713
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDdDGRLVGIITDRDLRRRVLA-EGLDPLDT 65
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 649-713 7.35e-03

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


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 37.52  E-value: 7.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13542693 649 LRRILNLSPFTVTDHTPMETVVDIFRKLGLRQC----------------LVTRSGRLLGIITKKDVLRHMAQMANQDPES 712
Cdd:cd04620   1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                .
gi 13542693 713 I 713
Cdd:cd04620  81 I 81
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 648-700 9.64e-03

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 36.82  E-value: 9.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 13542693 648 KLRRILNLSPFTVTDHTPMETVVDIFRKLGLRQCLVTRSGRLLGIITKKDVLR 700
Cdd:cd04631   1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMR 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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