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Conserved domains on  [gi|148236831|ref|NP_001083736|]
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chloride channel, voltage-sensitive 3 S homeolog [Xenopus laevis]

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 ...
 109-615 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: 724.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 109 GLASGALAGFIDIAADWMADLKEGICmtafwfnheqccwdskeatfeerdkcpqwqtwadliigqaegpgsyimNYFMYI 188
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 189 FWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684   33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684  113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 349 LFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFGRYPVLEVIAVAAITAIIAFPNPYTRFNTSQL 428
Cdd:cd03684  193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 429 IKELFTDCGPLESSSLCDYkndmnaskivddiPDRPAGTGVYSAIWQLCLALVFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684  273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684  340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                        490       500
                 ....*....|....*....|....*..
gi 148236831 589 TSKWVGDAFGREGIYEAHIRLNGYPFL 615
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 ...
 626-776 6.10e-48

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: 165.39  E-value: 6.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 626 LARDVMRPrrndpPLAVLTQDdMTVDDVESLINDTSYNGFPVIMSKESQRLVGFALRRDLTLAIENarkkqdgivgssrv 705
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236831 706 cfaqhtpslpaesprtlKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 776
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 ...
 109-615 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: 724.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 109 GLASGALAGFIDIAADWMADLKEGICmtafwfnheqccwdskeatfeerdkcpqwqtwadliigqaegpgsyimNYFMYI 188
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 189 FWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684   33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684  113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 349 LFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFGRYPVLEVIAVAAITAIIAFPNPYTRFNTSQL 428
Cdd:cd03684  193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 429 IKELFTDCGPLESSSLCDYkndmnaskivddiPDRPAGTGVYSAIWQLCLALVFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684  273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684  340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                        490       500
                 ....*....|....*....|....*..
gi 148236831 589 TSKWVGDAFGREGIYEAHIRLNGYPFL 615
Cdd:cd03684  419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 194-595 4.09e-89

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: 284.44  E-value: 4.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  194 FAFLAVCLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 273
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  274 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 353
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  354 YHTPWYLFELIPFILLGVFGGLWGAFFIRANIaWCRRRKSTRFGRYPVLEVIAVAAITAIIAFPNPYTRFNTSQLIKELF 433
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  434 TDCGPLessslcdykndmnaskivddipdrpagtgvysaiWQLCLALVFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 513
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  514 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 593
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 148236831  594 GD 595
Cdd:pfam00654 343 SR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
168-608 6.02e-49

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 178.41  E-value: 6.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 168 DLIIGQAEGPGSYIMNYFMYIFWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVA 247
Cdd:COG0038   34 HLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 248 SGLSLGKEGPLVHVACCCGNIFSYLFPkysTNEAKKREVLSaasaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFF 327
Cdd:COG0038  112 SGGSLGREGPSVQIGAAIGSLLGRLLR---LSPEDRRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 328 AALVAAFVLRSInpFGNSrlVLFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRAnIAWCRRRkSTRFGRYPVLEVIAV 407
Cdd:COG0038  189 ASVVAYLVSRLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIG 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 408 AAITAIIAFPNPYTRFNTSQLIKELFTdcGPLessslcdykndmnaskivddipdrpagtgvysAIWQLCLALVFKIIMT 487
Cdd:COG0038  263 GLLVGLLGLFLPQVLGSGYGLIEALLN--GEL--------------------------------SLLLLLLLLLLKLLAT 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 488 VFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfifkewceVGADCITPGLYAMVGAAACLGGVTRMTVSLV 567
Cdd:COG0038  309 ALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAI 373

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 148236831 568 VIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIR 608
Cdd:COG0038  374 LLVLEMTGSYSLLLPLMIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 626-776 6.10e-48

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: 165.39  E-value: 6.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 626 LARDVMRPrrndpPLAVLTQDdMTVDDVESLINDTSYNGFPVIMSKESQRLVGFALRRDLTLAIENarkkqdgivgssrv 705
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236831 706 cfaqhtpslpaesprtlKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 776
Cdd:cd04591   61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
187-605 1.15e-23

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 104.59  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 187 YIFWALSF------AFLAVCLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVH 260
Cdd:PRK05277  41 LLLWIVAFlisavlAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQ 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 261 VACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFVLRS 338
Cdd:PRK05277 119 MGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 339 INpfGNSrlVLFYVEYHTPWYLFELIPFILLGVFGGLWGAFF---IRANIAWCRRRKSTRFGRYPVLEVIAVAAITAIIA 415
Cdd:PRK05277 197 FN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRWVLMGGAVGGLCGLLGL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 416 FPNPYTR--FNTsqlikelftdcgplessslcdykndmnaskivddIPDrpAGTGVYSaIWQLCLALVFKIIMTVFTFGI 493
Cdd:PRK05277 273 LAPAAVGggFNL----------------------------------IPI--ALAGNFS-IGMLLFIFVARFITTLLCFGS 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 494 KVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVFEL 573
Cdd:PRK05277 316 GAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVLEM 380

                        410       420       430
                 ....*....|....*....|....*....|..
gi 148236831 574 TGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:PRK05277 381 TDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
542-777 1.82e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 75.69  E-value: 1.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 542 ITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGdAFGREGIYEAHIRLNGYPFLDAKEEF 621
Cdd:COG2524    4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 622 THTTLARDVMRPrrndPPLAVltQDDMTVDDVESLINDTSYNGFPVImskESQRLVGFALRRDLTLAIENARKKQDgivg 701
Cdd:COG2524   83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148236831 702 ssrvcfaqhtpslpaesprtLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHM 777
Cdd:COG2524  150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 732-775 4.92e-08

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 49.82  E-value: 4.92e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 148236831   732 PFTVTDQTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILR 775
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIK 46
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 724-778 3.44e-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: 3.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148236831  724 LRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 778
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 730-773 2.73e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 44.19  E-value: 2.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 148236831 730 MSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDI 773
Cdd:PTZ00314 104 MDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 109-615 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: 724.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 109 GLASGALAGFIDIAADWMADLKEGICmtafwfnheqccwdskeatfeerdkcpqwqtwadliigqaegpgsyimNYFMYI 188
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYV 32

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 189 FWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd03684   33 LLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNI 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 269 FSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLV 348
Cdd:cd03684  113 ISRLFPKYRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLV 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 349 LFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRANIAWCRRRKSTRFGRYPVLEVIAVAAITAIIAFPNPYTRFNTSQL 428
Cdd:cd03684  193 LFEVEYDRDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTEL 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 429 IKELFTDCGPLESSSLCDYkndmnaskivddiPDRPAGTGVYSAIWQLCLALVFKIIMTVFTFGIKVPSGLFIPSMAIGA 508
Cdd:cd03684  273 LELLFNECEPGDDNSLCCY-------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 509 IAGRIVGIAVEQLAYYHHDWFIFkEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVM 588
Cdd:cd03684  340 LFGRIVGILVEQLAYSYPDSIFF-ACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVM 418

                        490       500
                 ....*....|....*....|....*..
gi 148236831 589 TSKWVGDAFGREGIYEAHIRLNGYPFL 615
Cdd:cd03684  419 VSKWVADAIGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 109-604 9.62e-147

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: 436.78  E-value: 9.62e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 109 GLASGALAGFIDIAADWMADLKEGICMTAfwfnheqccwdskeatfeerdkcpqwqtwadliigqaegPGSYIMNYFMYI 188
Cdd:cd01036    1 GLLMGLVAVVLDYAVESSLDAGQWLLRRI---------------------------------------PGSYLLGYLMWV 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 189 FWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNI 268
Cdd:cd01036   42 LWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAG 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 269 FSYLFPKYS----------TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRS 338
Cdd:cd01036  122 LLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQI 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 339 INPFGNSR----------LVLFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRANIAWCRRRKSTRF---GRYPVLEVI 405
Cdd:cd01036  202 YNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFrktARYRVLEPV 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 406 avaaitaiiafpnpytrfntsqlikeLFtdcgplessslcdykndmnaskivddipdrpagTGVYSAI---WQLCLALVF 482
Cdd:cd01036  282 --------------------------LF---------------------------------TLIYSTIhyaPTLLLFLLI 302

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 483 KIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewCEVGADCITPGLYAMVGAAACLGGVTRM 562
Cdd:cd01036  303 YFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIG-------AESATLWADPGVYALIGAAAFLGGTTRL 375

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 148236831 563 TVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGrEGIYE 604
Cdd:cd01036  376 TFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-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. ...
 102-615 2.30e-89

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: 289.55  E-value: 2.30e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 102 WLVLTLTGLASGALAGFIDIAADWMADLKEgicmtafwfnheqccwdskeatfeerdkcpqwqtwadLIIGQAEGPGSYI 181
Cdd:cd03685   33 WIICLLIGIFTGLVAYFIDLAVENLAGLKF-------------------------------------LVVKNYIEKGRLF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 182 MNYFMYIFWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 261
Cdd:cd03685   76 TAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 262 ACCCGNIFS----------YLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALV 331
Cdd:cd03685  156 GACIAAGLSqggstslrldFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 332 AAFVLRSINPFGNSR---------LVLFYVeYHTP--WYLFELIPFILLGVFGGLWGAFFIRANIawcrrrKSTRFgryp 400
Cdd:cd03685  236 VTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFNHLNH------KVTRF---- 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 401 vleviavaaitaiiafpnpYTRFNTSQLIKELFTDCGPLESSSLCDYkndmnaskivddipdrpagtgvysaIWQLCLAL 480
Cdd:cd03685  305 -------------------RKRINHKGKLLKVLEALLVSLVTSVVAF-------------------------PQTLLIFF 340

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 481 VFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQlayyhhdwFIFKEWcevgadcITPGLYAMVGAAACLGGVT 560
Cdd:cd03685  341 VLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGS--------YFGFTS-------IDPGLYALLGAAAFLGGVM 405

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148236831 561 RMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFgREGIYEAHIRLNGYPFL 615
Cdd:cd03685  406 RMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 194-595 4.09e-89

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: 284.44  E-value: 4.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  194 FAFLAVCLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLF 273
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  274 PKysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSInpFGNSrlVLFYVE 353
Cdd:pfam00654  79 FR--LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  354 YHTPWYLFELIPFILLGVFGGLWGAFFIRANIaWCRRRKSTRFGRYPVLEVIAVAAITAIIAFPNPYTRFNTSQLIKELF 433
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  434 TDCGPLessslcdykndmnaskivddipdrpagtgvysaiWQLCLALVFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRI 513
Cdd:pfam00654 232 NGNTSL----------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  514 VGIAVEQLAYYHHdwfifkewcevgadcITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWV 593
Cdd:pfam00654 278 FGLLLALLFPIGG---------------LPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342


                  ..
gi 148236831  594 GD 595
Cdd:pfam00654 343 SR 344
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 178-615 8.74e-76

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: 252.17  E-value: 8.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 178 GSYIMNYFMYIFWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGP 257
Cdd:cd03683   39 GNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 258 LVHVACCCGNIFSYLFPKYS---TNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAF 334
Cdd:cd03683  119 FVHISSIVAALLSKLTTFFSgiyENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAF 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 335 VLRSINPF---GNSRLVLFYVEYHT--PWYLFELIPFILLGVFGGLWGAFFIRANIAWCRRRKSTR-----FGRYPVLEV 404
Cdd:cd03683  199 TFRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNRlfskfLKRSPLLYP 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 405 IAVAAITAIIAFPnpytrFNTsqlikelftdcgplessslcdykndmnaskivddipdrpagtgvysaiwqLCLALVFKI 484
Cdd:cd03683  279 AIVALLTAVLTFP-----FLT--------------------------------------------------LFLFIVVKF 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 485 IMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGiavEQLAYyhhdWFIFKEWcEVGADCITPGLYAMVGAAACLGGVTRmTV 564
Cdd:cd03683  304 VLTALAITLPVPAGIFMPVFVIGAALGRLVG---EIMAV----LFPEGIR-GGISNPIGPGGYAVVGAAAFSGAVTH-TV 374

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148236831 565 SLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGReGIYEAHIRLNGYPFL 615
Cdd:cd03683  375 SVAVIIFELTGQISHLLPVLIAVLISNAVAQFLQP-SIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 186-590 3.12e-54

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: 192.01  E-value: 3.12e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 186 MYIFWALSFAFLAVCLVKVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACC 264
Cdd:cd00400   38 LYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 265 CGNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGN 344
Cdd:cd00400  115 IGSWLGRRLR---LSRNDRRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEP 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 345 srlvLFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRANIAWCRRRKstRFGRYPVLEVIAVAAITAIIAFPNPYTRFN 424
Cdd:cd00400  192 ----AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPALGGLLLGLLGLFLPQVLGS 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 425 TSQLIKELFtdcgplessslcdykndmnaskivddipdrpagTGVYSaIWQLCLALVFKIIMTVFTFGIKVPSGLFIPSM 504
Cdd:cd00400  266 GYGAILLAL---------------------------------AGELS-LLLLLLLLLLKLLATALTLGSGFPGGVFAPSL 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 505 AIGAIAGRIVGIAVEQLAYyhhdwfifkewcevgADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLM 584
Cdd:cd00400  312 FIGAALGAAFGLLLPALFP---------------GLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLM 376


                 ....*.
gi 148236831 585 AAVMTS 590
Cdd:cd00400  377 LAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
168-608 6.02e-49

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 178.41  E-value: 6.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 168 DLIIGQAEGPGSYIMNYFMYIFWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVA 247
Cdd:COG0038   34 HLFLGGLLSAAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 248 SGLSLGKEGPLVHVACCCGNIFSYLFPkysTNEAKKREVLSaasaagvsvaFGAPIGGVLFSLEEVSYYFPLKTLWRSFF 327
Cdd:COG0038  112 SGGSLGREGPSVQIGAAIGSLLGRLLR---LSPEDRRILLAagaaaglaaaFNAPLAGALFALEVLLRDFSYRALIPVLI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 328 AALVAAFVLRSInpFGNSrlVLFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRAnIAWCRRRkSTRFGRYPVLEVIAV 407
Cdd:COG0038  189 ASVVAYLVSRLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRL-LLKVERL-FKRLKLPPWLRPAIG 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 408 AAITAIIAFPNPYTRFNTSQLIKELFTdcGPLessslcdykndmnaskivddipdrpagtgvysAIWQLCLALVFKIIMT 487
Cdd:COG0038  263 GLLVGLLGLFLPQVLGSGYGLIEALLN--GEL--------------------------------SLLLLLLLLLLKLLAT 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 488 VFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfifkewceVGADCITPGLYAMVGAAACLGGVTRMTVSLV 567
Cdd:COG0038  309 ALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLL---------------FPGLGLSPGLFALVGMAAVFAAVTRAPLTAI 373

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 148236831 568 VIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIR 608
Cdd:COG0038  374 LLVLEMTGSYSLLLPLMIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 626-776 6.10e-48

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: 165.39  E-value: 6.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 626 LARDVMRPrrndpPLAVLTQDdMTVDDVESLINDTSYNGFPVIMSKESQRLVGFALRRDLTLAIENarkkqdgivgssrv 705
Cdd:cd04591    1 TAEDVMRP-----PLTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236831 706 cfaqhtpslpaesprtlKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRH 776
Cdd:cd04591   61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 184-605 1.20e-47

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: 174.27  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 184 YFMYIFWALSFAFLAVCLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVAC 263
Cdd:cd01031   37 LLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 264 CCGNIFSYLFPkysTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFG 343
Cdd:cd01031  115 AIGQGVSKWFK---TSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 344 nsrlVLFYVEYHTPWYLFELIPFILLGVFGGLWGAFFIRANIA---WCRRRKSTRFGRYPVLEVIAVAAITAIIafpnPY 420
Cdd:cd01031  192 ----PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKsqdLYRKLKKLPRELRVLLPGLLIGPLGLLL----PE 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 421 TRFNTSQLIKELFTdcGPLessslcdykndmnaskivddipdrpagtgvysAIWQLCLALVFKIIMTVFTFGIKVPSGLF 500
Cdd:cd01031  264 ALGGGHGLILSLAG--GNF--------------------------------SISLLLLIFVLRFIFTMLSYGSGAPGGIF 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 501 IPSMAIGAIAGRIVGIAVEQLAYYHHDwfifkewcevgadciTPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYI 580
Cdd:cd01031  310 APMLALGALLGLLFGTILVQLGPIPIS---------------APATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLL 374

                        410       420
                 ....*....|....*....|....*
gi 148236831 581 VPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:cd01031  375 LPLMVVCLVAYLVADLLGGKPIYEA 399
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 187-603 1.20e-26

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: 113.09  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 187 YIFWALSFA--FLAVCLVKVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHV 261
Cdd:cd01034   27 WLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 262 ACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWRSFFAALVAAFVLR 337
Cdd:cd01034  107 GAAVMLAIGRRLPKWGGLSE--RGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLAVIAAGLVSLAVLG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 338 SINPFGNSRLVLfyveyhTPWYLFELIPFIllGVFGGLWGAFFIRANIAWCRRRKSTRFG---RYPVLEVIAVAAITAII 414
Cdd:cd01034  185 NYPYFGVAAVAL------PLGEAWLLVLVC--GVVGGLAGGLFARLLVALSSGLPGWVRRfrrRRPVLFAALCGLALALI 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 415 AFPNPYTRFNTSQLIKElftdcgplessslcdykndmnaskivddipDRPAGTGVYSAiwqlcLALVFKIIMTVFTFGIK 494
Cdd:cd01034  257 GLVSGGLTFGTGYLQAR------------------------------AALEGGGGLPL-----WFGLLKFLATLLSYWSG 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 495 VPSGLFIPSMAIGAiagrIVGIAVEQLAYYHHdwfifkewcevgadcitPGLYAMVGAAACLGGVTRMTVSLVVIVFELT 574
Cdd:cd01034  302 IPGGLFAPSLAVGA----GLGSLLAALLGSVS-----------------QGALVLLGMAAFLAGVTQAPLTAFVIVMEMT 360

                        410       420
                 ....*....|....*....|....*....
gi 148236831 575 GGLEYIVPLMAAVMTSKWVGDAFGREGIY 603
Cdd:cd01034  361 GDQQMLLPLLAAALLASGVSRLVCPEPLY 389
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
187-605 1.15e-23

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 104.59  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 187 YIFWALSF------AFLAVCLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVH 260
Cdd:PRK05277  41 LLLWIVAFlisavlAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQ 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 261 VACCCGNIFSYLFPKYSTNEAkkREVLSAASAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFVLRS 338
Cdd:PRK05277 119 MGGNIGRMVLDIFRLRSDEAR--HTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 339 INpfGNSrlVLFYVEYHTPWYLFELIPFILLGVFGGLWGAFF---IRANIAWCRRRKSTRFGRYPVLEVIAVAAITAIIA 415
Cdd:PRK05277 197 FN--GEQ--AVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFnklLLRTQDLFDRLHGGNKKRWVLMGGAVGGLCGLLGL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 416 FPNPYTR--FNTsqlikelftdcgplessslcdykndmnaskivddIPDrpAGTGVYSaIWQLCLALVFKIIMTVFTFGI 493
Cdd:PRK05277 273 LAPAAVGggFNL----------------------------------IPI--ALAGNFS-IGMLLFIFVARFITTLLCFGS 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 494 KVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfiFKEWcevgadCITPGLYAMVGAAACLGGVTRMTVSLVVIVFEL 573
Cdd:PRK05277 316 GAPGGIFAPMLALGTLLGLAFGMVAAAL---------FPQY------HIEPGTFAIAGMGALFAATVRAPLTGIVLVLEM 380

                        410       420       430
                 ....*....|....*....|....*....|..
gi 148236831 574 TGGLEYIVPLMAAVMTSKWVGDAFGREGIYEA 605
Cdd:PRK05277 381 TDNYQLILPLIITCLGATLLAQFLGGKPIYSA 412
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
236-633 3.18e-18

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 89.03  E-value: 3.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 236 MIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYL--FPKystneAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEV 313
Cdd:PRK01862 119 LWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFahFDP-----PRLRLLVACGAAAGITSAYNAPIAGAFFVAEIV 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 314 SYYFPLKTLWRSFFAALVAAFVLRSinpFGNSRlVLFYVEYH---TPWylfELIPFILLGVFGGLWGAFFIRAniawcRR 390
Cdd:PRK01862 194 LGSIAMESFGPLVVASVVANIVMRE---FAGYQ-PPYEMPVFpavTGW---EVLLFVALGVLCGAAAPQFLRL-----LD 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 391 RKSTRFGRYPVleviavaaitaiiafpNPYTRFNTSQLIKELFtdcgplessslcdykndmnaSKIVDDIpdrpAGTGvY 470
Cdd:PRK01862 262 ASKNQFKRLPV----------------PLPVRLALGGLLVGVI--------------------SVWVPEV----WGNG-Y 300

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 471 SAI---------WQ-LCLALVFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLayyhhdwfifkeWCEVGAD 540
Cdd:PRK01862 301 SVVntilhapwtWQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHAL------------WPGHTSA 368

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 541 citPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNgypflDAKEE 620
Cdd:PRK01862 369 ---PFAYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLRRH-----QDEAE 440

                        410
                 ....*....|....*
gi 148236831 621 FTH--TTLARDVMRP 633
Cdd:PRK01862 441 RERlrTTQMRELIQP 455
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
542-777 1.82e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 75.69  E-value: 1.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 542 ITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGdAFGREGIYEAHIRLNGYPFLDAKEEF 621
Cdd:COG2524    4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 622 THTTLARDVMRPrrndPPLAVltQDDMTVDDVESLINDTSYNGFPVImskESQRLVGFALRRDLTLAIENARKKQDgivg 701
Cdd:COG2524   83 VLKMKVKDIMTK----DVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148236831 702 ssrvcfaqhtpslpaesprtLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHM 777
Cdd:COG2524  150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
626-784 2.43e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 73.36  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 626 LARDVMRPrrndPPLAVltQDDMTVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLTLAIENARKKQdgivgssrv 705
Cdd:COG3448    3 TVRDIMTR----DVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE--------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 706 cfaqhtpslPAESPRTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQMANH 783
Cdd:COG3448   66 ---------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLEE 135


                 .
gi 148236831 784 D 784
Cdd:COG3448  136 E 136
CBS COG0517
CBS domain [Signal transduction mechanisms];
626-779 2.34e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 70.28  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 626 LARDVMRPrrnDPPLAvltQDDMTVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLTLAIenarkkqdgivgssrv 705
Cdd:COG0517    2 KVKDIMTT---DVVTV---SPDATVREALELMSEKRIGGLPVV--DEDGKLVGIVTDRDLRRAL---------------- 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148236831 706 cfaqhtpSLPAESPRTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLV-THNGRLLGIITKKDILRHMAQ 779
Cdd:COG0517   58 -------AAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
620-780 5.87e-14

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 69.56  E-value: 5.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 620 EFTHTTLARDVMRprRNDPplAVLTqDDMTVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLtlaienarkkqdgi 699
Cdd:COG4109   11 TFKEILLVEDIMT--LEDV--ATLS-EDDTVEDALELLEKTGHSRFPVV--DENGRLVGIVTSKDI-------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 700 vgssrvcfaqhtpslpAESPRTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 778
Cdd:COG4109   70 ----------------LGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLKALQ 133


                 ..
gi 148236831 779 QM 780
Cdd:COG4109  134 KI 135
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 627-780 3.59e-11

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 61.00  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 627 ARDVMRprrnDPPLAVltQDDMTVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLTLAIenarkkqdgivgssrvc 706
Cdd:COG2905    1 VKDIMS----RDVVTV--SPDATVREAARLMTEKGVGSLVVV--DDDGRLVGIITDRDLRRRV----------------- 55

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148236831 707 FAQHtpslpaESPRTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQM 780
Cdd:COG2905   56 LAEG------LDPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 233-590 4.34e-10

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: 62.31  E-value: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 233 WTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFpkySTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLE- 311
Cdd:cd01033   83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFSDWL---GLTVADRRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 312 ---EVSyyfplktlWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLfeLIPF-ILLGVFGGLWGAFFIRANiAW 387
Cdd:cd01033  160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDIPPMQLSTP--LLIWaLLAGPVLGVVAAGFRRLS-QA 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 388 CRRRKSTRFGRYPVLEVIAVAAITAIIAFPnpytrfntsqlikELFTDCGPLESSSLcdykndmnaskivddipdrpAGT 467
Cdd:cd01033  229 ARAKRPKGKRILWQMPLAFLVIGLLSIFFP-------------QILGNGRALAQLAF--------------------STT 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 468 GVYSAIWQLclaLVFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIaveqlaYYHHDWFIfkewcevgadcITPGLY 547
Cdd:cd01033  276 LTLSLLLIL---LVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGI------VWNALLPP-----------LSIAAF 335

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 148236831 548 AMVGAAACLGGVTRMTVSLVVIVFELTG-GLEYIVPLMAAVMTS 590
Cdd:cd01033  336 ALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 646-775 4.35e-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: 4.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 646 DDMTVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLTLAIENARKkqdgivgssrvcfaqhtpslpaesPRTLKLR 725
Cdd:cd02205    9 PDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRALVEGGL------------------------ALDTPVA 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 148236831 726 SILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILR 775
Cdd:cd02205   63 EVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 647-775 2.18e-08

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: 52.71  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 647 DMTVDDVESLINDTSYNGFPVimsKESQRLVGFALRRDLTLAIENArkkqdgivgssrvcfaqhtpslpaesprtlKLRS 726
Cdd:cd04610   11 DDTVKDVIKLIKETGHDGFPV---VDDGKVVGYVTAKDLLGKDDDE------------------------------KVSE 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148236831 727 IldMSPFTVTDQTPMEIvVDIFRKLgLRQCL-----VTHNGRLLGIITKKDILR 775
Cdd:cd04610   58 I--MSRDTVVADPDMDI-TDAARVI-FRSGIsklpvVDDEGNLVGIITNMDVIR 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 732-775 4.92e-08

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 49.82  E-value: 4.92e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 148236831   732 PFTVTDQTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILR 775
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIK 46
CBS COG0517
CBS domain [Signal transduction mechanisms];
722-778 6.85e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 51.79  E-value: 6.85e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148236831 722 LKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRHMA 778
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVdEDGKLVGIVTDRDLRRALA 58
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 647-775 2.70e-07

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 49.42  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 647 DMTVDDVESLINDTSYNGFPVImskESQRLVGFALRRDltlaIENARKKQDGivgssrvcfaqHTPslpaesprtlkLRS 726
Cdd:cd04595   10 DTTIEEARKIMLRYGHTGLPVV---EDGKLVGIISRRD----VDKAKHHGLG-----------HAP-----------VKG 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 148236831 727 ILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04595   61 YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLR 109
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 724-778 3.44e-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: 3.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148236831  724 LRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDILRHMA 778
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 629-775 1.03e-06

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


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 47.95  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 629 DVMRPRrndpplAVLTQDDMTVDDVESLINDTSYNGFPVImskESQRLVGFalrrdLTLaiENARKKQDGIVGSSRVcfa 708
Cdd:cd04801    1 DIMTPE------VVTVTPEMTVSELLDRMFEEKHLGYPVV---ENGRLVGI-----VTL--EDIRKVPEVEREATRV--- 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 709 qhtpslpaesprtlklRSILDMSPFTVTDQTPmeiVVDIFRKL---GLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04801   62 ----------------RDVMTKDVITVSPDAD---AMEALKLMsqnNIGRLPVVEDGELVGIISRTDLMR 112
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 647-775 1.10e-05

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 45.50  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 647 DMTVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLTLAIENARKKQDGIVGSSRVcfaqHTPSLPAESPRTLKLRS 726
Cdd:cd04586   11 DTSVREAARLLLEHRISGLPVV--DDDGKLVGIVSEGDLLRREEPGTEPRRVWWLDALL----ESPERLAEEYVKAHGRT 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 148236831 727 ILD-MS--PFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04586   85 VGDvMTrpVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 627-774 2.10e-05

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 44.41  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 627 ARDVMRPRRNdpplaVLTQD-DMTVDDVESLINDTSYNGFPVImSKESQRLVGFALRRDLtLAienarkkqdgivgssrv 705
Cdd:cd04590    2 VREVMTPRTD-----VVALDaDATLEELLELILESGYSRFPVY-EGDLDNIIGVLHVKDL-LA----------------- 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 706 cfaqhtpsLPAESPRTLKLRSILdMSPFTVTDQTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDIL 774
Cdd:cd04590   58 --------ALLEGREKLDLRALL-RPPLFVPETTPLDDLLEEFRKERSHMAIVVdEYGGTAGIVTLEDIL 118
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 730-781 3.44e-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: 3.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148236831 730 MS--PFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQMA 781
Cdd:cd04584    6 MTknVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 647-775 3.50e-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: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 647 DMTVDDVESLINDTSYNGFPVImskESQRLVGFALRRDLTLAienarkkqdgivgssrvcfaqhTPSlPAESPRTLKLRS 726
Cdd:cd04584   16 DTSLAEARELMKEHKIRHLPVV---DDGKLVGIVTDRDLLRA----------------------SPS-KATSLSIYELNY 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148236831 727 ILD-------MS--PFTVTDQTPMEIVVDIFR--KLGlrqCL-VTHNGRLLGIITKKDILR 775
Cdd:cd04584   70 LLSkipvkdiMTkdVITVSPDDTVEEAALLMLenKIG---CLpVVDGGKLVGIITETDILR 127
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
720-779 3.69e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 45.64  E-value: 3.69e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 720 RTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQ 779
Cdd:COG2524   84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 718-777 4.47e-05

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


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 43.48  E-value: 4.47e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148236831 718 SPRTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLrqcL----VTHNGRLLGIITKKDILRHM 777
Cdd:cd04606   61 ADPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 649-775 2.51e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 42.07  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 649 TVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLtLAIenarkkqDGIVGSSRvcfaQHTPSLPAESP-----RTLK 723
Cdd:cd17789   13 TVDEALELLVENRITGLPVI--DEDWRLVGVVSDYDL-LAL-------DSISGRSQ----TDNNFPPADSTwktfnEVQK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148236831 724 L------RSILDM---SPFTVTDQTPMEIVVDI-----FRKLGLrqclVTHNGRLLGIITKKDILR 775
Cdd:cd17789   79 LlsktngKVVGDVmtpSPLVVREKTNLEDAARIlletkFRRLPV----VDSDGKLVGIITRGNVVR 140
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 730-773 2.73e-04

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 44.19  E-value: 2.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 148236831 730 MSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDI 773
Cdd:PTZ00314 104 MDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 732-788 5.84e-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: 40.31  E-value: 5.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148236831 732 PFTVTDQTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDILRHMAQMANHDPESI 788
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDdDGKLVGIVTERDILRALVEGGLALDTPV 61
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 724-782 9.19e-04

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


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 40.21  E-value: 9.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148236831 724 LRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQC----------------LVTHNGRLLGIITKKDILRHMAQMAN 782
Cdd:cd04620    1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGID 75
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 719-775 1.29e-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: 39.04  E-value: 1.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 148236831 719 PRTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILR 775
Cdd:cd09836   56 DLDTPVEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVdGGGKLVGVISIRDLAR 113
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
718-784 1.62e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 41.59  E-value: 1.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148236831 718 SPRTLKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDILRHMAQMANHD 784
Cdd:COG2239  189 ADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLL-ALpvVDEEGRLVGIITVDDVVDVIEEEATED 256
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 722-775 1.84e-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: 39.13  E-value: 1.84e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 148236831 722 LKLRSILDMSPFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04631   75 VPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILR 128
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 627-691 2.53e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.81  E-value: 2.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148236831  627 ARDVMRPrrndPPLAVltQDDMTVDDVESLINDTSYNGFPVImsKESQRLVGFALRRDLTLAIEN 691
Cdd:pfam00571   1 VKDIMTK----DVVTV--SPDTTLEEALELMREHGISRLPVV--DEDGKLVGIVTLKDLLRALLG 57
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 647-776 2.85e-03

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 40.83  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831  647 DMTVDDVESLINDTSYNGFPVImskESQRLVGFALRRDLtlaienarkkqdgivgssRVcfaqhtpslpaESPRTLKLRS 726
Cdd:pfam00478  96 DATVADALALMERYGISGVPVV---DDGKLVGIVTNRDL------------------RF-----------ETDLSQPVSE 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 148236831  727 IL-DMSPFTVTDQTPMEIVVDIFRKLGL-RQCLVTHNGRLLGIITKKDILRH 776
Cdd:pfam00478 144 VMtKENLVTAPEGTTLEEAKEILHKHKIeKLPVVDDNGRLVGLITIKDIEKA 195
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 730-775 3.61e-03

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 38.36  E-value: 3.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 148236831 730 MS--PFTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04631    6 MTknVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMR 53
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 647-775 5.32e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 37.39  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148236831 647 DMTVDDVESLINDTSYNGFPVIMSKEsqRLVGFALRRDLTLaienarkkqdgivgssrvcfaqhtpslpaESPRTLKLRS 726
Cdd:cd04601   10 DATVADVLELKAEYGISGVPVTEDGG--KLVGIVTSRDIRF-----------------------------ETDLSTPVSE 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 148236831 727 IldMSPF----TVTDQTPMEIVVDIFR--KLGlRQCLVTHNGRLLGIITKKDILR 775
Cdd:cd04601   59 V--MTPDerlvTAPEGITLEEAKEILHkhKIE-KLPIVDDNGELVGLITRKDIEK 110
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 730-776 5.50e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. 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: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 37.93  E-value: 5.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 148236831 730 MS--PFTVTDQTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDILRH 776
Cdd:cd04600    1 MSrdVVTVTPDTSLEEAWRLLRRHRIKALPVVdRARRLVGIVTLADLLKH 50
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 731-773 7.62e-03

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 36.71  E-value: 7.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 148236831 731 SP-FTVTDQTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDI 773
Cdd:cd04595    2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV 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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