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Conserved domains on  [gi|1002244810|ref|XP_015626593|]
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chloride channel protein CLC-c [Oryza sativa Japonica Group]

Protein Classification

chloride channel protein( domain architecture ID 10132712)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 81-602 0e+00

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: 566.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810  81 ESLDYEVVENDLFKQDWRSRKKKQIFQYIVLKWTLVLLIGLLTGLVGFFNNLAVENIAGFKLLLTGNLMLKERYLTAFFA 160
Cdd:cd03685     1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIEKGRLFTAFLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 161 YGGCNLVLAAAAAAICAYIAPAAAGSGIPEVKAYLNGVDAYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIA 240
Cdd:cd03685    81 YLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 241 NLLGQGGSRKYRLTCNWLRYFKNDRDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVL 320
Cdd:cd03685   161 AGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVTFTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 321 RSLIEFCRSGKCGLFGQGGLIMFDLSSTVATYSTPDLIAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERGAPFKILLT 400
Cdd:cd03685   241 NFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINHKGKLLKVLEA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 401 ITISIITSMCSYglpwlaactpcpvdaveqcptigrsgnfknfqcppghyndlaslffntnddairnlfsngtesefhMS 480
Cdd:cd03685   321 LLVSLVTSVVAF------------------------------------------------------------------PQ 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 481 TLFIFFTAVYCLGILTYGVAVPSGLFIPVILAGATYGRIVGTLLGSISD---LDPGLFALLGAASFLGGTMRMTVSVCVI 557
Cdd:cd03685   335 TLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGftsIDPGLYALLGAAAFLGGVMRMTVSLTVI 414

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1002244810 558 LLELTNDLAMLPLVMLVLLISKTIADNFNKGVYDQIVVMKGLPYM 602
Cdd:cd03685   415 LLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 605-783 2.13e-31

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: 118.39  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 605 HAEPYMRHlvagdvvsgPLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplTEAPELVGLVTRSHLLVLLngkmfmkdql 684
Cdd:cd04591     1 TAEDVMRP---------PLTVLARDETVGDIVSVLKTTDHNGFPVVDS---TESQTLVGFILRSQLILLL---------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 685 ktsgsfvlQRfgafdfakpgsgkglkiqdldftdeememyvDLHPVTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpk 764
Cdd:cd04591    59 --------EA-------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVT-- 97

                         170
                  ....*....|....*....
gi 1002244810 765 tpDRPPIVGILTRHDFVEE 783
Cdd:cd04591    98 --NNGRLVGIVTRKDLLRA 114
 
Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 81-602 0e+00

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: 566.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810  81 ESLDYEVVENDLFKQDWRSRKKKQIFQYIVLKWTLVLLIGLLTGLVGFFNNLAVENIAGFKLLLTGNLMLKERYLTAFFA 160
Cdd:cd03685     1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIEKGRLFTAFLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 161 YGGCNLVLAAAAAAICAYIAPAAAGSGIPEVKAYLNGVDAYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIA 240
Cdd:cd03685    81 YLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 241 NLLGQGGSRKYRLTCNWLRYFKNDRDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVL 320
Cdd:cd03685   161 AGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVTFTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 321 RSLIEFCRSGKCGLFGQGGLIMFDLSSTVATYSTPDLIAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERGAPFKILLT 400
Cdd:cd03685   241 NFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINHKGKLLKVLEA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 401 ITISIITSMCSYglpwlaactpcpvdaveqcptigrsgnfknfqcppghyndlaslffntnddairnlfsngtesefhMS 480
Cdd:cd03685   321 LLVSLVTSVVAF------------------------------------------------------------------PQ 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 481 TLFIFFTAVYCLGILTYGVAVPSGLFIPVILAGATYGRIVGTLLGSISD---LDPGLFALLGAASFLGGTMRMTVSVCVI 557
Cdd:cd03685   335 TLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGftsIDPGLYALLGAAAFLGGVMRMTVSLTVI 414

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1002244810 558 LLELTNDLAMLPLVMLVLLISKTIADNFNKGVYDQIVVMKGLPYM 602
Cdd:cd03685   415 LLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 185-566 1.28e-42

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: 158.48  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEVKAYLNGVDaySILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGQggsrkyrltcnwLRYFKND 264
Cdd:pfam00654  18 GSGIPEVKAALHGGR--GPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGR------------RLFRLSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 265 RDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFtTAVVAVVLRSLIefcrsgkcglFGQGGLIMFd 344
Cdd:pfam00654  84 RDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLL-ASVVAALVSRLI----------FGNSPLFSV- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 345 lsSTVATYSTPDLIAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERGAPFKilltitisIITSMCSYGLpwLAACTPcp 424
Cdd:pfam00654 152 --GEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLKIPPVLR--------PALGGLLVGL--LGLLFP-- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 425 vdaveqcptigrsgnfknfqcppghyndlasLFFNTNDDAIRNLFSNGTesefHMSTLFIFFTAVYCLGILTYGVAVPSG 504
Cdd:pfam00654 218 -------------------------------EVLGGGYELIQLLFNGNT----SLSLLLLLLLLKFLATALSLGSGAPGG 262

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002244810 505 LFIPVILAGATYGRIVGTLLGS---ISDLDPGLFALLGAASFLGGTMRMTVSVCVILLELTNDLA 566
Cdd:pfam00654 263 IFAPSLAIGAALGRAFGLLLALlfpIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQ 327
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 605-783 2.13e-31

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: 118.39  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 605 HAEPYMRHlvagdvvsgPLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplTEAPELVGLVTRSHLLVLLngkmfmkdql 684
Cdd:cd04591     1 TAEDVMRP---------PLTVLARDETVGDIVSVLKTTDHNGFPVVDS---TESQTLVGFILRSQLILLL---------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 685 ktsgsfvlQRfgafdfakpgsgkglkiqdldftdeememyvDLHPVTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpk 764
Cdd:cd04591    59 --------EA-------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVT-- 97

                         170
                  ....*....|....*....
gi 1002244810 765 tpDRPPIVGILTRHDFVEE 783
Cdd:cd04591    98 --NNGRLVGIVTRKDLLRA 114
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
110-566 6.56e-18

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 86.73  E-value: 6.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 110 VLKWTLV-LLIGLLTGLVGFFNNLAVEniAGFKLLLTGNLMLKERYLTAFFAYGGCnLVLAAAAAAICAYIAPAAAGSGI 188
Cdd:COG0038     4 LLRLLLLaVLVGILAGLAAVLFRLLLE--LATHLFLGGLLSAAGSHLPPWLVLLLP-PLGGLLVGLLVRRFAPEARGSGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 189 PEVKAYLNGVDaySILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGQggsrkyrltcnWLRyfKNDRDRR 268
Cdd:COG0038    81 PQVIEAIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGR-----------LLR--LSPEDRR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 269 DLITCG----------SaagvaaafraPVGGVLFALEE-AASWWRSALLwrAFFTTAVVAVVLRSLiefcrsgkcgLFGQ 337
Cdd:COG0038   146 ILLAAGaaaglaaafnA----------PLAGALFALEVlLRDFSYRALI--PVLIASVVAYLVSRL----------LFGN 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 338 GGLIMFdlsSTVATYSTPDLIAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERgAPFKilltitisiitsmcsyglPWL 417
Cdd:COG0038   204 GPLFGV---PSVPALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRLKLP-PWLR------------------PAI 261

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 418 AACTpcpvdaveqcptIGrsgnfknfqcppghyndLASLFFN----TNDDAIRNLFSNgtesEFHMSTLFIFFTAVYCLG 493
Cdd:COG0038   262 GGLL------------VG-----------------LLGLFLPqvlgSGYGLIEALLNG----ELSLLLLLLLLLLKLLAT 308

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002244810 494 ILTYGVAVPSGLFIPVILAGATYGRIVGTLLGSI---SDLDPGLFALLGAASFLGGTMRMTVSVCVILLELTNDLA 566
Cdd:COG0038   309 ALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLfpgLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYS 384
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
185-563 2.37e-11

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 66.84  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEVKAYLNGVdaYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGqggsrkyrltcNWLRyFKND 264
Cdd:PRK05277   71 GSGIPEIEGALEGL--RPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVL-----------DIFR-LRSD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 265 RDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALL-WRAFFTTAVVA-VVLRSLIefcrsgkcglfGQGGLIm 342
Cdd:PRK05277  137 EARHTLLAAGAAAGLAAAFNAPLAGILFVIEEMRPQFRYSLIsIKAVFIGVIMAtIVFRLFN-----------GEQAVI- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 343 fdlssTVATYSTPDLIAI---IILGIIGGIFGGLFNFLLDKVLRVYSIINERgapfkilltitisiitSMCSYGLPWLAA 419
Cdd:PRK05277  205 -----EVGKFSAPPLNTLwlfLLLGIIFGIFGVLFNKLLLRTQDLFDRLHGG----------------NKKRWVLMGGAV 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 420 CTPCPVDAVEQCPTIGrsGNFknfqcppghyndlaslffntnddairNLFSNGTESEFHMSTLFIFFTAVYCLGILTYGV 499
Cdd:PRK05277  264 GGLCGLLGLLAPAAVG--GGF--------------------------NLIPIALAGNFSIGMLLFIFVARFITTLLCFGS 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244810 500 AVPSGLFIPVI----LAGATYGRIVGTLLGSISdLDPGLFALLGAASFLGGTMRMTVSVCVILLELTN 563
Cdd:PRK05277  316 GAPGGIFAPMLalgtLLGLAFGMVAAALFPQYH-IEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTD 382
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
527-782 1.96e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 52.19  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 527 ISDLDPGLFALLGAASFLGGTMRMTVSVCVILLELTNDLAMLPLVMLVLLISKTIADNFNKGVYDQIVVMKGLPYMEAHA 606
Cdd:COG2524     1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 607 EPYMRHLVaGDVVSGPLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplteaPELVGLVTRSHLLVLLNGKMFMKDqlkt 686
Cdd:COG2524    81 GLVLKMKV-KDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD------GKLVGIITERDLLKALAEGRDLLD---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 687 sgsfvlqrfgafdfakpgsgkgLKIQDLdftdeeMemyvdlhpvtNTSPYTVVETMSLAKAAILFRALGLRHLLVVpKTP 766
Cdd:COG2524   150 ----------------------APVSDI------M----------TRDVVTVSEDDSLEEALRLMLEHGIGRLPVV-DDD 190

                         250
                  ....*....|....*.
gi 1002244810 767 DRPpiVGILTRHDFVE 782
Cdd:COG2524   191 GKL--VGIITRTDILR 204
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 730-783 1.48e-04

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: 40.27  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002244810 730 VTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpKTPDRppIVGILTRHDFVEE 783
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVV-DEDGK--LVGIVTLKDLLRA 54
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 622-674 3.06e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 36.34  E-value: 3.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002244810  622 PLITFSGVEKVGNIVHALRFTGHNGFPVVDeppltEAPELVGLVTRSHLLVLL 674
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVD-----EEGRLVGIVTRRDIIKAL 48
 
Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 81-602 0e+00

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: 566.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810  81 ESLDYEVVENDLFKQDWRSRKKKQIFQYIVLKWTLVLLIGLLTGLVGFFNNLAVENIAGFKLLLTGNLMLKERYLTAFFA 160
Cdd:cd03685     1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIEKGRLFTAFLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 161 YGGCNLVLAAAAAAICAYIAPAAAGSGIPEVKAYLNGVDAYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIA 240
Cdd:cd03685    81 YLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 241 NLLGQGGSRKYRLTCNWLRYFKNDRDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVL 320
Cdd:cd03685   161 AGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVTFTL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 321 RSLIEFCRSGKCGLFGQGGLIMFDLSSTVATYSTPDLIAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERGAPFKILLT 400
Cdd:cd03685   241 NFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINHKGKLLKVLEA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 401 ITISIITSMCSYglpwlaactpcpvdaveqcptigrsgnfknfqcppghyndlaslffntnddairnlfsngtesefhMS 480
Cdd:cd03685   321 LLVSLVTSVVAF------------------------------------------------------------------PQ 334

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 481 TLFIFFTAVYCLGILTYGVAVPSGLFIPVILAGATYGRIVGTLLGSISD---LDPGLFALLGAASFLGGTMRMTVSVCVI 557
Cdd:cd03685   335 TLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGftsIDPGLYALLGAAAFLGGVMRMTVSLTVI 414

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 1002244810 558 LLELTNDLAMLPLVMLVLLISKTIADNFNKGVYDQIVVMKGLPYM 602
Cdd:cd03685   415 LLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 120-591 1.33e-73

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: 246.10  E-value: 1.33e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 120 GLLTGLVGFFNNLAVENIAGFKLLLTgnLMLKERYLTAFFAYGGCNLVLAAAAAAICAYIAPAAAGSGIPEVKAYLNGVD 199
Cdd:cd01036     1 GLLMGLVAVVLDYAVESSLDAGQWLL--RRIPGSYLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 200 AYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGQGGSRKYRLTCNWLRYFKNDRDRRDLITCGSAAGV 279
Cdd:cd01036    79 LPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLGCHVHLFQLFRNPRDRRDFLVAGAAAGV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 280 AAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVLRSLIEFCRSGKCGLFGQGGLImfdlSSTVATYSTPdlia 359
Cdd:cd01036   159 ASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFELLDRSSAMFL----SLTVFELHVP---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 360 iiilgiiggifgglfnflldkvLRVYSIInergaPFkilltitisiitsmcsyglpwlaactpcpvdAVeqcptIGRSGN 439
Cdd:cd01036   231 ----------------------LNLYEFI-----PT-------------------------------VV-----IGVICG 247

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 440 FknfqcppghyndLASLFFNTNDDAIR----NLFSNGTESEF--------------HMSTLFIFFTAVYCLGILTYGVAV 501
Cdd:cd01036   248 L------------LAALFVRLSIIFLRwrrrLLFRKTARYRVlepvlftliystihYAPTLLLFLLIYFWMSALAFGIAV 315

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 502 PSGLFIPVILAGATYGRIVGTLL-----------GSISDLDPGLFALLGAASFLGGTMRMTVSVCVILLELTNDLAMLPL 570
Cdd:cd01036   316 PGGTFIPSLVIGAAIGRLVGLLVhriavagigaeSATLWADPGVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLLP 395

                         490       500
                  ....*....|....*....|.
gi 1002244810 571 VMLVLLISKTIADNFNKGVYD 591
Cdd:cd01036   396 LMVAILIAKAVADAFCESLYH 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 185-566 1.28e-42

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: 158.48  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEVKAYLNGVDaySILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGQggsrkyrltcnwLRYFKND 264
Cdd:pfam00654  18 GSGIPEVKAALHGGR--GPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGR------------RLFRLSP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 265 RDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFtTAVVAVVLRSLIefcrsgkcglFGQGGLIMFd 344
Cdd:pfam00654  84 RDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLL-ASVVAALVSRLI----------FGNSPLFSV- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 345 lsSTVATYSTPDLIAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERGAPFKilltitisIITSMCSYGLpwLAACTPcp 424
Cdd:pfam00654 152 --GEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLKIPPVLR--------PALGGLLVGL--LGLLFP-- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 425 vdaveqcptigrsgnfknfqcppghyndlasLFFNTNDDAIRNLFSNGTesefHMSTLFIFFTAVYCLGILTYGVAVPSG 504
Cdd:pfam00654 218 -------------------------------EVLGGGYELIQLLFNGNT----SLSLLLLLLLLKFLATALSLGSGAPGG 262

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002244810 505 LFIPVILAGATYGRIVGTLLGS---ISDLDPGLFALLGAASFLGGTMRMTVSVCVILLELTNDLA 566
Cdd:pfam00654 263 IFAPSLAIGAALGRAFGLLLALlfpIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQ 327
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 185-602 5.09e-42

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: 159.31  E-value: 5.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEVKAYLNGVDAYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLgqggsrkYRLTcnwLRYFKND 264
Cdd:cd03684    55 GSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNII-------SRLF---PKYRRNE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 265 RDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVLRSLiefcrsgkcGLFGQGGLIMFD 344
Cdd:cd03684   125 AKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSL---------NPFGTGRLVLFE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 345 LSstvatYSTPDLIAIIILgiiggifgglfnFLLDKVL-----RVYSIINERGAPFKILLTITI---------SIITSMC 410
Cdd:cd03684   196 VE-----YDRDWHYFELIP------------FILLGIFgglygAFFIKANIKWARFRKKSLLKRypvlevllvALITALI 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 411 SYGLPWLA---------ACTPC-PVDAVEQCptigrsgNFKNFQCPPGHYNDLASLFFNTnddairnlfsngtesefhms 480
Cdd:cd03684   259 SFPNPYTRldmtellelLFNECePGDDNSLC-------CYRDPPAGDGVYKALWSLLLAL-------------------- 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 481 TLFIFFTavyclgILTYGVAVPSGLFIPVILAGATYGRIVGTLLGSI-----------------SDLDPGLFALLGAASF 543
Cdd:cd03684   312 IIKLLLT------IFTFGIKVPAGIFVPSMAVGALFGRIVGILVEQLaysypdsiffacctagpSCITPGLYAMVGAAAF 385

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 544 LGGTMRMTVSVCVILLELTNDLAMLPLVMLVLLISKTIADNFNK-GVYDQIVVMKGLPYM 602
Cdd:cd03684   386 LGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWVADAIGKeGIYDAHIHLNGYPFL 445
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 113-602 3.97e-39

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: 150.47  E-value: 3.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 113 WTLVLLIGLLTGLVGFFNNLAVENIAGFKLLLTGnlMLKERYLTAFFAYGGCNLVLAAAAAAICAYIAPAAAGSGIPEVK 192
Cdd:cd03683     2 WLFLALLGILMALISIAMDFAVEKLLNARRWLYS--LLTGNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 193 AYLNGVDAYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGqggsrkyRLTCNWLRYFKNDRDRRDLIT 272
Cdd:cd03683    80 TILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLS-------KLTTFFSGIYENESRRMEMLA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 273 CGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVLRSLIEFCRSGKcglfgqgglimfdlsSTVATY 352
Cdd:cd03683   153 AACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTFRLLAVFFSDQE---------------TITALF 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 353 STpdliaiiilgiiggifgglfNFLLDKVLRVYSIInergapfkilltiTISIITSMCSYGLPWLAACTpcpvdaveqcp 432
Cdd:cd03683   218 KT--------------------TFFVDFPFDVQELP-------------IFALLGIICGLLGALFVFLH----------- 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 433 tiGRSGNFKNfqcppghYNDLASLFFNTNDDAIRNLFSNGTES-EFHMSTLFIFFTAVYCLGILTYGVAVPSGLFIPVIL 511
Cdd:cd03683   254 --RKIVRFRR-------KNRLFSKFLKRSPLLYPAIVALLTAVlTFPFLTLFLFIVVKFVLTALAITLPVPAGIFMPVFV 324

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 512 AGATYGRIVGTLL----------GSISDLDPGLFALLGAASFLGGTMRmTVSVCVILLELTNDLAMLPLVMLVLLISKTI 581
Cdd:cd03683   325 IGAALGRLVGEIMavlfpegirgGISNPIGPGGYAVVGAAAFSGAVTH-TVSVAVIIFELTGQISHLLPVLIAVLISNAV 403

                         490       500
                  ....*....|....*....|.
gi 1002244810 582 ADNFNKGVYDQIVVMKGLPYM 602
Cdd:cd03683   404 AQFLQPSIYDSIIKIKKLPYL 424
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 605-783 2.13e-31

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: 118.39  E-value: 2.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 605 HAEPYMRHlvagdvvsgPLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplTEAPELVGLVTRSHLLVLLngkmfmkdql 684
Cdd:cd04591     1 TAEDVMRP---------PLTVLARDETVGDIVSVLKTTDHNGFPVVDS---TESQTLVGFILRSQLILLL---------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 685 ktsgsfvlQRfgafdfakpgsgkglkiqdldftdeememyvDLHPVTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpk 764
Cdd:cd04591    59 --------EA-------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVT-- 97

                         170
                  ....*....|....*....
gi 1002244810 765 tpDRPPIVGILTRHDFVEE 783
Cdd:cd04591    98 --NNGRLVGIVTRKDLLRA 114
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 119-565 3.86e-21

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: 96.46  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 119 IGLLTGLVGFFNNLAVENIAGFKLLLtgnLMLKERYLTAFFAYGGCNLVLAAAAAAICAYIAPAAAGSGIPEVKAYLNGV 198
Cdd:cd01031     1 IGLLAGLVAVLFRLGIDKLGNLRLSL---YDFAANNPPLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 199 DAYSILapSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIanllGQGGSRKYRLTcnwlryfknDRDRRDLITCGSAAG 278
Cdd:cd01031    78 LPPNWW--RVLPVKFVGGVLALGSGLSLGREGPSVQIGAAI----GQGVSKWFKTS---------PEERRQLIAAGAAAG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 279 VAAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVLRSliefcrsgkcgLFGQGglimFDLSST-VATYSTPDL 357
Cdd:cd01031   143 LAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRL-----------FFGLG----PVLSIPpLPALPLKSY 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 358 IAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERGAPFKilltitISIITSMCSYGLPWLaactpcpvdaveqcPTIGRS 437
Cdd:cd01031   208 WLLLLLGIIAGLLGYLFNRSLLKSQDLYRKLKKLPRELR------VLLPGLLIGPLGLLL--------------PEALGG 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 438 GNfknfqcppghyndlaslffntnddairNLFSNGTESEFHMSTLFIFFTAVYCLGILTYGVAVPSGLFIPVILAGATYG 517
Cdd:cd01031   268 GH---------------------------GLILSLAGGNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLG 320

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002244810 518 RIVGTLLGSISDLD---PGLFALLGAASFLGGTMRMTVSVCVILLELTNDL 565
Cdd:cd01031   321 LLFGTILVQLGPIPisaPATFAIAGMAAFFAAVVRAPITAIILVTEMTGNF 371
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 185-565 3.88e-18

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: 87.23  E-value: 3.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEV-KAYLNGvdaYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGQggsrkyrltcnWLRYfkN 263
Cdd:cd00400    63 GHGIPEViEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGR-----------RLRL--S 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 264 DRDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSA----LLWRAFFTTAVVAVVLRSLIEFCRSGK-------- 331
Cdd:cd00400   127 RNDRRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVAslipVLLASVAAALVSRLLFGAEPAFGVPLYdplsllel 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 332 ---------CGLFGqgglIMFdlsstvatystpdliaiiilgiiggifgglfNFLLDKVLRVYSIINeRGAPFKillTIT 402
Cdd:cd00400   207 plylllgllAGLVG----VLF-------------------------------VRLLYKIERLFRRLP-IPPWLR---PAL 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 403 ISIITSMCSYGLPWLaactpcpvdaveqcptigrsgnfknfqcpPGHYNDLASLFFNtnddairnlfsngteSEFHMSTL 482
Cdd:cd00400   248 GGLLLGLLGLFLPQV-----------------------------LGSGYGAILLALA---------------GELSLLLL 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 483 FIFFTAVYCLGILTYGVAVPSGLFIPVILAGATYGRIVGTLLGSI---SDLDPGLFALLGAASFLGGTMRMTVSVCVILL 559
Cdd:cd00400   284 LLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALfpgLVASPGAYALVGMAALLAAVLRAPLTAILLVL 363


                  ....*.
gi 1002244810 560 ELTNDL 565
Cdd:cd00400   364 ELTGDY 369
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
110-566 6.56e-18

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 86.73  E-value: 6.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 110 VLKWTLV-LLIGLLTGLVGFFNNLAVEniAGFKLLLTGNLMLKERYLTAFFAYGGCnLVLAAAAAAICAYIAPAAAGSGI 188
Cdd:COG0038     4 LLRLLLLaVLVGILAGLAAVLFRLLLE--LATHLFLGGLLSAAGSHLPPWLVLLLP-PLGGLLVGLLVRRFAPEARGSGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 189 PEVKAYLNGVDaySILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGQggsrkyrltcnWLRyfKNDRDRR 268
Cdd:COG0038    81 PQVIEAIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGR-----------LLR--LSPEDRR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 269 DLITCG----------SaagvaaafraPVGGVLFALEE-AASWWRSALLwrAFFTTAVVAVVLRSLiefcrsgkcgLFGQ 337
Cdd:COG0038   146 ILLAAGaaaglaaafnA----------PLAGALFALEVlLRDFSYRALI--PVLIASVVAYLVSRL----------LFGN 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 338 GGLIMFdlsSTVATYSTPDLIAIIILGIIGGIFGGLFNFLLDKVLRVYSIINERgAPFKilltitisiitsmcsyglPWL 417
Cdd:COG0038   204 GPLFGV---PSVPALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRLKLP-PWLR------------------PAI 261

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 418 AACTpcpvdaveqcptIGrsgnfknfqcppghyndLASLFFN----TNDDAIRNLFSNgtesEFHMSTLFIFFTAVYCLG 493
Cdd:COG0038   262 GGLL------------VG-----------------LLGLFLPqvlgSGYGLIEALLNG----ELSLLLLLLLLLLKLLAT 308

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002244810 494 ILTYGVAVPSGLFIPVILAGATYGRIVGTLLGSI---SDLDPGLFALLGAASFLGGTMRMTVSVCVILLELTNDLA 566
Cdd:COG0038   309 ALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLfpgLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYS 384
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
185-563 2.37e-11

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 66.84  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEVKAYLNGVdaYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGqggsrkyrltcNWLRyFKND 264
Cdd:PRK05277   71 GSGIPEIEGALEGL--RPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVL-----------DIFR-LRSD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 265 RDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALL-WRAFFTTAVVA-VVLRSLIefcrsgkcglfGQGGLIm 342
Cdd:PRK05277  137 EARHTLLAAGAAAGLAAAFNAPLAGILFVIEEMRPQFRYSLIsIKAVFIGVIMAtIVFRLFN-----------GEQAVI- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 343 fdlssTVATYSTPDLIAI---IILGIIGGIFGGLFNFLLDKVLRVYSIINERgapfkilltitisiitSMCSYGLPWLAA 419
Cdd:PRK05277  205 -----EVGKFSAPPLNTLwlfLLLGIIFGIFGVLFNKLLLRTQDLFDRLHGG----------------NKKRWVLMGGAV 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 420 CTPCPVDAVEQCPTIGrsGNFknfqcppghyndlaslffntnddairNLFSNGTESEFHMSTLFIFFTAVYCLGILTYGV 499
Cdd:PRK05277  264 GGLCGLLGLLAPAAVG--GGF--------------------------NLIPIALAGNFSIGMLLFIFVARFITTLLCFGS 315

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002244810 500 AVPSGLFIPVI----LAGATYGRIVGTLLGSISdLDPGLFALLGAASFLGGTMRMTVSVCVILLELTN 563
Cdd:PRK05277  316 GAPGGIFAPMLalgtLLGLAFGMVAAALFPQYH-IEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTD 382
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 185-323 1.49e-07

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: 54.54  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEVKAYL---NGVDAYSILAPSTLFVKIFGSILGVSAGFVLGKEGPMVHTGACIANLLGQggsrkyrltcnWLRyF 261
Cdd:cd01034    53 GSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQIGAAVMLAIGR-----------RLP-K 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002244810 262 KNDRDRRDLITCGSAAGVAAAFRAPVGGVLFALEE--AASWWRSALLWraffTTAVVAVVLRSL 323
Cdd:cd01034   121 WGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEElsRDFELRFSGLV----LLAVIAAGLVSL 180
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
527-782 1.96e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 52.19  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 527 ISDLDPGLFALLGAASFLGGTMRMTVSVCVILLELTNDLAMLPLVMLVLLISKTIADNFNKGVYDQIVVMKGLPYMEAHA 606
Cdd:COG2524     1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 607 EPYMRHLVaGDVVSGPLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplteaPELVGLVTRSHLLVLLNGKMFMKDqlkt 686
Cdd:COG2524    81 GLVLKMKV-KDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD------GKLVGIITERDLLKALAEGRDLLD---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 687 sgsfvlqrfgafdfakpgsgkgLKIQDLdftdeeMemyvdlhpvtNTSPYTVVETMSLAKAAILFRALGLRHLLVVpKTP 766
Cdd:COG2524   150 ----------------------APVSDI------M----------TRDVVTVSEDDSLEEALRLMLEHGIGRLPVV-DDD 190

                         250
                  ....*....|....*.
gi 1002244810 767 DRPpiVGILTRHDFVE 782
Cdd:COG2524   191 GKL--VGIITRTDILR 204
CBS COG0517
CBS domain [Signal transduction mechanisms];
615-788 2.06e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 50.63  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 615 AGDVVSGPLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplteAPELVGLVTRSHLLVLLNgkmfmkdqlktsgsfvlqr 694
Cdd:COG0517     3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDE-----DGKLVGIVTDRDLRRALA------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 695 fgafdfAKPGSGKGLKIQDLdftdeemeMyvdlhpvtNTSPYTVVETMSLAKAAILFRALGLRHLLVVPKTpDRppIVGI 774
Cdd:COG0517    59 ------AEGKDLLDTPVSEV--------M--------TRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDD-GR--LVGI 113

                         170
                  ....*....|....
gi 1002244810 775 LTRHDFVEEHIHGL 788
Cdd:COG0517   114 ITIKDLLKALLEPL 127
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
612-781 2.00e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 47.94  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 612 HLVAGDVVSGPLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplteAPELVGLVTRSHLLvllngkmfmkdqlktsgsfv 691
Cdd:COG3448     1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDE-----DGRLVGIVTERDLL-------------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 692 lqrfgafDFAKPGSGKGLKIQDLDFTDEEmemyvdlhpVTNTSPYTVVETMSLAKAAILFRALGLRHLLVVPKTpDRppI 771
Cdd:COG3448    56 -------RALLPDRLDELEERLLDLPVED---------VMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GR--L 116

                         170
                  ....*....|
gi 1002244810 772 VGILTRHDFV 781
Cdd:COG3448   117 VGIVTRTDLL 126
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
624-779 1.54e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 45.29  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 624 ITFSGVEKVGNIVHALRFTGHNGFPVVDeppltEAPELVGLVTRSHLLvllngkmfmkdqlktsgsfvlqrfgafdfakp 703
Cdd:COG4109    28 ATLSEDDTVEDALELLEKTGHSRFPVVD-----ENGRLVGIVTSKDIL-------------------------------- 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002244810 704 GSGKGLKIQDldftdeememyvdlhpVTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpKTPDRppIVGILTRHD 779
Cdd:COG4109    71 GKDDDTPIED----------------VMTKNPITVTPDTSLASAAHKMIWEGIELLPVV-DDDGR--LLGIISRQD 127
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 714-781 4.39e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. 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: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 43.37  E-value: 4.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244810 714 LDFTDEEmemyVDLHPVTN--TSP-YTVVETMSLAKAAILFRALGLRHLLVVpkTPDRPPiVGILTRHDFV 781
Cdd:cd09833    51 LDFSDPD----AFRRPISEvmSSPvLTIPQDTTLGEAAVRFRQEGVRHLLVV--DDDGRP-VGIVSQTDVV 114
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 622-781 5.69e-05

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 43.00  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 622 PLITFSGVEKVGNIVHALRFTGHNGFPVVDEpplteAPELVGLVTRSHLL-VLLNGKMFMKDQLKTsgsfvlqrfgafdf 700
Cdd:cd02205     3 DVVTVDPDTTVREALELMAENGIGALPVVDD-----DGKLVGIVTERDILrALVEGGLALDTPVAE-------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 701 akpgsgkglkiqdldftdeememyvdlhpVTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpKTPDRppIVGILTRHDF 780
Cdd:cd02205    64 -----------------------------VMTPDVITVSPDTDLEEALELMLEHGIRRLPVV-DDDGK--LVGIVTRRDI 111


                  .
gi 1002244810 781 V 781
Cdd:cd02205   112 L 112
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 730-781 1.14e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 42.51  E-value: 1.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002244810 730 VTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpktpDRPPIVGILTRHDFV 781
Cdd:COG2905    70 VMTRPPITVSPDDSLAEALELMEEHRIRHLPVV----DDGKLVGIVSITDLL 117
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 730-783 1.48e-04

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: 40.27  E-value: 1.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002244810 730 VTNTSPYTVVETMSLAKAAILFRALGLRHLLVVpKTPDRppIVGILTRHDFVEE 783
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVV-DEDGK--LVGIVTLKDLLRA 54
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 185-562 5.75e-04

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: 43.05  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 185 GSGIPEVKAYLNGVDAYSILapsTLFVKIFGSILGVSAGFVLGKEGPMVHTGAcianLLGQGGSRKYRLTcnwlryfknD 264
Cdd:cd01033    64 GKKLVSIKQAVRGKKRMPFW---ETIIHAVLQIVTVGLGAPLGREVAPREVGA----LLAQRFSDWLGLT---------V 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 265 RDRRDLITCGSAAGVAAAFRAPVGGVLFALEEAASWWRSALLWRAFFTTAVVAVVlrsliefcrsgkcGLFGQGGLIMFD 344
Cdd:cd01033   128 ADRRLLVACAAGAGLAAVYNVPLAGALFALEILLRTISLRSVVAALATSAIAAAV-------------ASLLKGDHPIYD 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 345 LssTVATYSTPdliaiiilgiiggifgglfnflldkvLRVYSIInergapfkilLTITISIITSMCSYGLPWLAACTPCP 424
Cdd:cd01033   195 I--PPMQLSTP--------------------------LLIWALL----------AGPVLGVVAAGFRRLSQAARAKRPKG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002244810 425 VDAVEQCPTIGRSGNFKNFQCP--PGHYNDLASLFFNTNddairnlfsngteseFHMSTLFIFFTAVYCLGILTYGVAVP 502
Cdd:cd01033   237 KRILWQMPLAFLVIGLLSIFFPqiLGNGRALAQLAFSTT---------------LTLSLLLILLVLKIVATLLALRAGAY 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002244810 503 SGLFIPVILAGATYGRIVGTLLGSISDLDP-GLFALLGAASFLGGTMRMTVSVCVILLELT 562
Cdd:cd01033   302 GGLLTPSLALGALLGALLGIVWNALLPPLSiAAFALIGAAAFLAATQKAPLTALILVLEFT 362
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 615-676 6.47e-04

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: 38.35  E-value: 6.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002244810 615 AGDVVSGPLITFSGVEKVGNIVHALRFTGHNGFPVVDeppltEAPELVGLVTRSHLLVLLNG 676
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVD-----EDGKLVGIVTLKDLLRALLG 57
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
732-793 1.58e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.46  E-value: 1.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002244810 732 NTSPYTVVETMSLAKAAILFRALGLRHLLVVPKTpDRppIVGILTRHDFVEEHIHGLFPNLN 793
Cdd:COG3448     9 TRDVVTVSPDTTLREALELMREHGIRGLPVVDED-GR--LVGIVTERDLLRALLPDRLDELE 67
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 730-783 1.95e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; 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: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 38.66  E-value: 1.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002244810 730 VTNTSPYTVVETMSLAKAAILFRALGLRHLLVVPKTPDrppIVGILTRHDFVEE 783
Cdd:cd09836    64 IMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGK---LVGVISIRDLARE 114
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 622-674 3.06e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 36.34  E-value: 3.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1002244810  622 PLITFSGVEKVGNIVHALRFTGHNGFPVVDeppltEAPELVGLVTRSHLLVLL 674
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVD-----EEGRLVGIVTRRDIIKAL 48
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 732-779 4.19e-03

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: 38.17  E-value: 4.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1002244810 732 NTSPYTVVETMSLAKAAILFRALGLRHLLVVpktpDRPPIVGILTRHD 779
Cdd:cd04584     7 TKNVVTVTPDTSLAEARELMKEHKIRHLPVV----DDGKLVGIVTDRD 50
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 735-781 7.74e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 35.18  E-value: 7.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1002244810  735 PYTVVETMSLAKAAILFRALGLRHLLVVpKTPDRppIVGILTRHDFV 781
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVV-DEEGR--LVGIVTRRDII 45
 
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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