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Conserved domains on  [gi|3182956|sp|O35454|]
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RecName: Full=H(+)/Cl(-) exchange transporter 6; AltName: Full=Chloride channel protein 6; Short=ClC-6; AltName: Full=Chloride transport protein 6

Protein Classification

chloride channel protein( domain architecture ID 10132712)

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

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_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 49-589 0e+00

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


:

Pssm-ID: 239657 [Multi-domain]  Cd Length: 466  Bit Score: 621.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   49 ESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEecsqKGCLAL 128
Cdd:cd03685   1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIE----KGRLFT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  129 SLLELLGFNLTFVFLASLLVL-IEPVAAGSGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSG 207
Cdd:cd03685  77 AFLVYLGLNLVLVLVAALLVAyIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  208 AVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSA 287
Cdd:cd03685 157 ACIAAGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIV 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  288 TFTLNFFRSGIQFGSWGSFQLPGLLNFgefkcsDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVH 367
Cdd:cd03685 237 TFTLNFFLSGCNSGKCGLFGPGGLIMF------DGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINH 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  368 pKPKLVRVLEsllvslvttvvVFVASMVlgecrqmsstsqtgngsfqlqvtsedvnSTIKAFfcpndtyndmatlffnsq 447
Cdd:cd03685 311 -KGKLLKVLE-----------ALLVSLV----------------------------TSVVAF------------------ 332

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  448 esailqlfhqdgtfsPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGA 527
Cdd:cd03685 333 ---------------PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSIDPGLYALLGA 397

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3182956  528 AAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDLFNKGIYDVHIGLRGVPLL 589
Cdd:cd03685 398 AAFLGGVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 601-854 1.42e-22

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: 93.35  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  601 RASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNekefmkgnqlisnnikfkkssiltrageqrkrgqsmk 680
Cdd:cd04591   1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQ------------------------------------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  681 sypsselrnvcdehvaseepaekedllqqmlerrytpypnlypdqspsedwtmeerfrplTFHGLVLRSQLVTLLVRgvc 760
Cdd:cd04591  44 ------------------------------------------------------------TLVGFILRSQLILLLEA--- 60

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  761 ysesqssasqprlsyaemaedyprypdihdldltllnprmivDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVN 840
Cdd:cd04591  61 ------------------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTN 98

                       250
                ....*....|....
gi 3182956  841 AvGEIVGIITRHNL 854
Cdd:cd04591  99 N-GRLVGIVTRKDL 111
 
Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 49-589 0e+00

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


Pssm-ID: 239657 [Multi-domain]  Cd Length: 466  Bit Score: 621.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   49 ESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEecsqKGCLAL 128
Cdd:cd03685   1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIE----KGRLFT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  129 SLLELLGFNLTFVFLASLLVL-IEPVAAGSGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSG 207
Cdd:cd03685  77 AFLVYLGLNLVLVLVAALLVAyIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  208 AVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSA 287
Cdd:cd03685 157 ACIAAGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIV 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  288 TFTLNFFRSGIQFGSWGSFQLPGLLNFgefkcsDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVH 367
Cdd:cd03685 237 TFTLNFFLSGCNSGKCGLFGPGGLIMF------DGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINH 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  368 pKPKLVRVLEsllvslvttvvVFVASMVlgecrqmsstsqtgngsfqlqvtsedvnSTIKAFfcpndtyndmatlffnsq 447
Cdd:cd03685 311 -KGKLLKVLE-----------ALLVSLV----------------------------TSVVAF------------------ 332

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  448 esailqlfhqdgtfsPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGA 527
Cdd:cd03685 333 ---------------PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSIDPGLYALLGA 397

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3182956  528 AAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDLFNKGIYDVHIGLRGVPLL 589
Cdd:cd03685 398 AAFLGGVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 140-570 2.57e-73

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: 243.99  E-value: 2.57e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    140 FVFLASLLV-LIEPVAAGSGIPEIKCYLNGVKvpGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFq 218
Cdd:pfam00654   1 GGLLAGWLVkRFAPEAAGSGIPEVKAALHGGR--GPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRR- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    219 sisLRKiqfnfpyfRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFrsgi 298
Cdd:pfam00654  78 ---LFR--------LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI---- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    299 qfgswgsFQLPGLLNFGEFkcsdsdkkcHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRmRNVHPKPKLVRVles 378
Cdd:pfam00654 143 -------FGNSPLFSVGEP---------GSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLF-RKLLKIPPVLRP--- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    379 llvslvttvvvFVASMVLGecrqmsstsqtgngsfqlqvtsedvnstIKAFFCPndtyndmatLFFNSQESAILQLFHqd 458
Cdd:pfam00654 203 -----------ALGGLLVG----------------------------LLGLLFP---------EVLGGGYELIQLLFN-- 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    459 GTFSPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVVRMT 538
Cdd:pfam00654 233 GNTSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALLFPIGGLPPGAFALVGMAAFLAAVTRAP 312

                         410       420       430
                  ....*....|....*....|....*....|..
gi 3182956    539 ISLTVILIESTNEITYGLPIMVTLMVAKWTGD 570
Cdd:pfam00654 313 LTAIVIVFELTGSLQLLLPLMLAVLIAYAVSR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
75-578 1.35e-36

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 142.97  E-value: 1.35e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   75 RYEAVKWMVVFA-IGVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEEcsqkgclalslLELLGFNLTFVFLASLLV----- 148
Cdd:COG0038   1 RRRLLRLLLLAVlVGILAGLAAVLFRLLLELATHLFLGGLLSAAGS-----------HLPPWLVLLLPPLGGLLVgllvr 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  149 LIEPVAAGSGIPEIKCYLNGVKvpGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFqsisLRkiqfn 228
Cdd:COG0038  70 RFAPEARGSGIPQVIEAIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRL----LR----- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  229 fpyfRSDRDKRDFV-------------SagaaagvaaafgaPIGGTLFSLEEGSsfwnQGLTWKVLFCSMSATFTLNFFR 295
Cdd:COG0038 139 ----LSPEDRRILLaagaaaglaaafnA-------------PLAGALFALEVLL----RDFSYRALIPVLIASVVAYLVS 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  296 SGIqFGSWGSFQLPGLlnfgefkcsdsdkkcHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRnvHPKPKLVRV 375
Cdd:COG0038 198 RLL-FGNGPLFGVPSV---------------PALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKR--LKLPPWLRP 259

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  376 lesllvslvttvvvFVASMVLGecrqmsstsqtgngsfqlqvtsedvnstIKAFFCPNdtyndmatLFFNSqESAILQLF 455
Cdd:COG0038 260 --------------AIGGLLVG----------------------------LLGLFLPQ--------VLGSG-YGLIEALL 288

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  456 HqdGTFSPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVV 535
Cdd:COG0038 289 N--GELSLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLGLSPGLFALVGMAAVFAAVT 366

                       490       500       510       520
                ....*....|....*....|....*....|....*....|....
gi 3182956  536 RMTISLTVILIESTNEITYGLPIMVTLMVAKWT-GDLFNKGIYD 578
Cdd:COG0038 367 RAPLTAILLVLEMTGSYSLLLPLMIACVIAYLVsRLLFPRSIYT 410
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 601-854 1.42e-22

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: 93.35  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  601 RASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNekefmkgnqlisnnikfkkssiltrageqrkrgqsmk 680
Cdd:cd04591   1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQ------------------------------------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  681 sypsselrnvcdehvaseepaekedllqqmlerrytpypnlypdqspsedwtmeerfrplTFHGLVLRSQLVTLLVRgvc 760
Cdd:cd04591  44 ------------------------------------------------------------TLVGFILRSQLILLLEA--- 60

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  761 ysesqssasqprlsyaemaedyprypdihdldltllnprmivDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVN 840
Cdd:cd04591  61 ------------------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTN 98

                       250
                ....*....|....
gi 3182956  841 AvGEIVGIITRHNL 854
Cdd:cd04591  99 N-GRLVGIVTRKDL 111
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
87-579 2.37e-18

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 88.80  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    87 IGVCTGLVGLFVDFSVRLFTQLKFGVVQTSveecsqKGCLALSLLELLGFNLTFVFLASLLVL-IEPVAAGSGIPEIKCY 165
Cdd:PRK05277   7 VGTLTGLVGVAFELAVDWVQNQRLGLLASV------ADNGLLLWIVAFLISAVLAMIGYFLVRrFAPEAGGSGIPEIEGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   166 LNGVKvpGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLpqfqsISLRKIqfnfpyfRSDRDKRDFVSAG 245
Cdd:PRK05277  81 LEGLR--PVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMV-----LDIFRL-------RSDEARHTLLAAG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   246 AAAGVAAAFGAPIGGTLFSLEE-GSSFWNQGLTWK-VLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLlnfgefkcsDSd 323
Cdd:PRK05277 147 AAAGLAAAFNAPLAGILFVIEEmRPQFRYSLISIKaVFIGVIMATIVFRLFNGEQAVIEVGKFSAPPL---------NT- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   324 kkchLWtamdlgFFVVMGVIGGLLGATFN-CLNKRLAKYRMRNVHPKPKLVrvlesllvslvttvvvfVASMVLGecrqm 402
Cdd:PRK05277 217 ----LW------LFLLLGIIFGIFGVLFNkLLLRTQDLFDRLHGGNKKRWV-----------------LMGGAVG----- 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   403 sstsqtgnGSFQLQvtsedvnstikAFFCPNDTYNDMATlffnsqesaILQLFhqDGTFSPVTLALFFILYFLLACWTFG 482
Cdd:PRK05277 265 --------GLCGLL-----------GLLAPAAVGGGFNL---------IPIAL--AGNFSIGMLLFIFVARFITTLLCFG 314

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   483 TSVPSGLFVPSL----LCGAAFGRLVANVLKSYiglgHLYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPI 558
Cdd:PRK05277 315 SGAPGGIFAPMLalgtLLGLAFGMVAAALFPQY----HIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPL 390

                        490       500
                 ....*....|....*....|....*
gi 3182956   559 MVT----LMVAKWTGdlfNKGIYDV 579
Cdd:PRK05277 391 IITclgaTLLAQFLG---GKPIYSA 412
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
807-870 1.22e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 62.96  E-value: 1.22e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3182956  807 YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQARLRQHYQTL 870
Cdd:COG3448   7 IMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERL 70
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 812-854 4.19e-11

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: 58.68  E-value: 4.19e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 3182956     812 PFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 804-859 7.58e-11

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: 57.99  E-value: 7.58e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 3182956    804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFL 859
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
798-861 2.02e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 51.37  E-value: 2.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3182956   798 PRMIVDVTP----YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQA 861
Cdd:PRK14869  60 PELIEDVKPqvrdLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYMDI 127
 
Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 49-589 0e+00

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


Pssm-ID: 239657 [Multi-domain]  Cd Length: 466  Bit Score: 621.59  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   49 ESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEecsqKGCLAL 128
Cdd:cd03685   1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIE----KGRLFT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  129 SLLELLGFNLTFVFLASLLVL-IEPVAAGSGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSG 207
Cdd:cd03685  77 AFLVYLGLNLVLVLVAALLVAyIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIG 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  208 AVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSA 287
Cdd:cd03685 157 ACIAAGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIV 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  288 TFTLNFFRSGIQFGSWGSFQLPGLLNFgefkcsDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVH 367
Cdd:cd03685 237 TFTLNFFLSGCNSGKCGLFGPGGLIMF------DGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINH 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  368 pKPKLVRVLEsllvslvttvvVFVASMVlgecrqmsstsqtgngsfqlqvtsedvnSTIKAFfcpndtyndmatlffnsq 447
Cdd:cd03685 311 -KGKLLKVLE-----------ALLVSLV----------------------------TSVVAF------------------ 332

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  448 esailqlfhqdgtfsPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGA 527
Cdd:cd03685 333 ---------------PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSIDPGLYALLGA 397

                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3182956  528 AAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDLFNKGIYDVHIGLRGVPLL 589
Cdd:cd03685 398 AAFLGGVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 88-578 7.18e-95

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: 304.27  E-value: 7.18e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   88 GVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEECSQKGCLALSllellgFNLTFVFLASLLVL-IEPVAAGSGIPEIKCYL 166
Cdd:cd01036   1 GLLMGLVAVVLDYAVESSLDAGQWLLRRIPGSYLLGYLMWVL------WSVVLVLISSGICLyFAPQAAGSGIPEVMAYL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  167 NGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGA 246
Cdd:cd01036  75 NGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLGCHVHLFQLFRNPRDRRDFLVAGA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  247 AAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSdkkc 326
Cdd:cd01036 155 AAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFELLDRSSAMFLSLTVFELHVP---- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  327 hlWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLlvslvttvvvfVASMVLgecrqmssts 406
Cdd:cd01036 231 --LNLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFRKTARYRVLEPV-----------LFTLIY---------- 287

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  407 qtgngsfqlqvtsedvnSTIkaffcpndTYndmatlffnsqesailqlfhqdgtfsPVTLALFFILYFLLACWTFGTSVP 486
Cdd:cd01036 288 -----------------STI--------HY--------------------------APTLLLFLLIYFWMSALAFGIAVP 316

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  487 SGLFVPSLLCGAAFGRLVAnVLKSYIGLGHLYS---------GTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLP 557
Cdd:cd01036 317 GGTFIPSLVIGAAIGRLVG-LLVHRIAVAGIGAesatlwadpGVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLLP 395

                       490       500
                ....*....|....*....|.
gi 3182956  558 IMVTLMVAKWTGDLFNKGIYD 578
Cdd:cd01036 396 LMVAILIAKAVADAFCESLYH 416
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 88-589 1.72e-78

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: 261.39  E-value: 1.72e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   88 GVCTGLVGLFVDFSVRLFTQLKFGVvqtsveeCSqkgclalsLLELLGFNLTFVFLASLLVL-IEPVAAGSGIPEIKCYL 166
Cdd:cd03684   1 GIAIGLIAGLIDIIASWLSDLKEGY-------CN--------YIIYVLLALLFAFIAVLLVKvVAPYAAGSGIPEIKTIL 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  167 NGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFqsislrkiqfnFPYFR-SDRDKRDFVSAG 245
Cdd:cd03684  66 SGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRL-----------FPKYRrNEAKRREILSAA 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  246 AAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRsgiqfgSWGSFQLpgLLNFGEFKcsdsdkk 325
Cdd:cd03684 135 AAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLN------PFGTGRL--VLFEVEYD------- 199

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  326 cHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHpkpKLVRVLEsllvslvttvVVFVASMvlgecrqmsst 405
Cdd:cd03684 200 -RDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLL---KRYPVLE----------VLLVALI----------- 254

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  406 sqTGNGSFQLQVTSEDVNSTIKAFFCPNDTYNDMATLFFNSQEsailqlfHQDGTFSPVTLALF-FILYFLLACWTFGTS 484
Cdd:cd03684 255 --TALISFPNPYTRLDMTELLELLFNECEPGDDNSLCCYRDPP-------AGDGVYKALWSLLLaLIIKLLLTIFTFGIK 325

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  485 VPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYS--------------GTFALIGAAAFLGGVVRMTISLTVILIESTN 550
Cdd:cd03684 326 VPAGIFVPSMAVGALFGRIVGILVEQLAYSYPDSIffacctagpscitpGLYAMVGAAAFLGGVTRMTVSLVVIMFELTG 405

                       490       500       510       520
                ....*....|....*....|....*....|....*....|
gi 3182956  551 EITYGLPIMVTLMVAKWTGDLFNK-GIYDVHIGLRGVPLL 589
Cdd:cd03684 406 ALNYILPLMIAVMVSKWVADAIGKeGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 140-570 2.57e-73

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: 243.99  E-value: 2.57e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    140 FVFLASLLV-LIEPVAAGSGIPEIKCYLNGVKvpGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFq 218
Cdd:pfam00654   1 GGLLAGWLVkRFAPEAAGSGIPEVKAALHGGR--GPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRR- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    219 sisLRKiqfnfpyfRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFrsgi 298
Cdd:pfam00654  78 ---LFR--------LSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI---- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    299 qfgswgsFQLPGLLNFGEFkcsdsdkkcHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRmRNVHPKPKLVRVles 378
Cdd:pfam00654 143 -------FGNSPLFSVGEP---------GSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLF-RKLLKIPPVLRP--- 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    379 llvslvttvvvFVASMVLGecrqmsstsqtgngsfqlqvtsedvnstIKAFFCPndtyndmatLFFNSQESAILQLFHqd 458
Cdd:pfam00654 203 -----------ALGGLLVG----------------------------LLGLLFP---------EVLGGGYELIQLLFN-- 232

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    459 GTFSPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVVRMT 538
Cdd:pfam00654 233 GNTSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALLFPIGGLPPGAFALVGMAAFLAAVTRAP 312

                         410       420       430
                  ....*....|....*....|....*....|..
gi 3182956    539 ISLTVILIESTNEITYGLPIMVTLMVAKWTGD 570
Cdd:pfam00654 313 LTAIVIVFELTGSLQLLLPLMLAVLIAYAVSR 344
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 81-589 5.57e-48

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: 176.67  E-value: 5.57e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   81 WMVVFAIGVCTGLVGLFVDFSVRLFTQLK---FGVVQTSVeecsqkgclALSLLELLGFNLTFVFLASLLV-LIEPVAAG 156
Cdd:cd03683   2 WLFLALLGILMALISIAMDFAVEKLLNARrwlYSLLTGNS---------LLQYLVWVAYPVALVLFSALFCkYISPQAVG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  157 SGIPEIKCYLNGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAglpqfqsiSLRKIQFNFPYFRSDR 236
Cdd:cd03683  73 SGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAA--------LLSKLTTFFSGIYENE 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  237 DKR-DFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFT---LNFFRSGIQFGSWGSFQlpgll 312
Cdd:cd03683 145 SRRmEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTfrlLAVFFSDQETITALFKT----- 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  313 NFGEFKCSDSDkkchlwtamDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVhpkpklvrvlesllvslvttvvvfVA 392
Cdd:cd03683 220 TFFVDFPFDVQ---------ELPIFALLGIICGLLGALFVFLHRKIVRFRRKNR------------------------LF 266

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  393 SMVLGECRQMsstsqtgngsfqlqvtsedvnstikaffcpndtYNDMATLFFnsqesAILqlfhqdgTFSPVTLALFFIL 472
Cdd:cd03683 267 SKFLKRSPLL---------------------------------YPAIVALLT-----AVL-------TFPFLTLFLFIVV 301

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  473 YFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLK-------SYIGLGHLYSGTFALIGAAAFLGGVVRmTISLTVIL 545
Cdd:cd03683 302 KFVLTALAITLPVPAGIFMPVFVIGAALGRLVGEIMAvlfpegiRGGISNPIGPGGYAVVGAAAFSGAVTH-TVSVAVII 380

                       490       500       510       520
                ....*....|....*....|....*....|....*....|....
gi 3182956  546 IESTNEITYGLPIMVTLMVAKWTGDLFNKGIYDVHIGLRGVPLL 589
Cdd:cd03683 381 FELTGQISHLLPVLIAVLISNAVAQFLQPSIYDSIIKIKKLPYL 424
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 140-579 1.13e-40

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: 154.62  E-value: 1.13e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  140 FVFLASLLV-LIEPVAAGSGIPEIKCYLNGVKVPgiVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQfq 218
Cdd:cd01031  47 LGLLAGWLVkKFAPEAKGSGIPQVEGVLAGLLPP--NWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSK-- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  219 sislrkiqfNFPyfRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEE-GSSFwnQGLTWK-VLFCSMSATFTLNFFrs 296
Cdd:cd01031 123 ---------WFK--TSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEElRHSF--SPLALLtALVASIAADFVSRLF-- 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  297 giqFGSWGSFQLPGLLNFgefkcsdsdkkchlwTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYrMRNVHPKPKLVRVL 376
Cdd:cd01031 188 ---FGLGPVLSIPPLPAL---------------PLKSYWLLLLLGIIAGLLGYLFNRSLLKSQDL-YRKLKKLPRELRVL 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  377 esllvslvttvvvfVASMVLGecrqmsstsqtgngsfqlqvtsedvnstIKAFFCPNdtyndmatlFFNSQESAILQLFH 456
Cdd:cd01031 249 --------------LPGLLIG----------------------------PLGLLLPE---------ALGGGHGLILSLAG 277

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  457 qdGTFSPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVVR 536
Cdd:cd01031 278 --GNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPMLALGALLGLLFGTILVQLGPIPISAPATFAIAGMAAFFAAVVR 355

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 3182956  537 MTISLTVILIESTNEITYGLPIMVTLMVAKWTGDLFN-KGIYDV 579
Cdd:cd01031 356 APITAIILVTEMTGNFNLLLPLMVVCLVAYLVADLLGgKPIYEA 399
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
75-578 1.35e-36

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 142.97  E-value: 1.35e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   75 RYEAVKWMVVFA-IGVCTGLVGLFVDFSVRLFTQLKFGVVQTSVEEcsqkgclalslLELLGFNLTFVFLASLLV----- 148
Cdd:COG0038   1 RRRLLRLLLLAVlVGILAGLAAVLFRLLLELATHLFLGGLLSAAGS-----------HLPPWLVLLLPPLGGLLVgllvr 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  149 LIEPVAAGSGIPEIKCYLNGVKvpGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFqsisLRkiqfn 228
Cdd:COG0038  70 RFAPEARGSGIPQVIEAIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRL----LR----- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  229 fpyfRSDRDKRDFV-------------SagaaagvaaafgaPIGGTLFSLEEGSsfwnQGLTWKVLFCSMSATFTLNFFR 295
Cdd:COG0038 139 ----LSPEDRRILLaagaaaglaaafnA-------------PLAGALFALEVLL----RDFSYRALIPVLIASVVAYLVS 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  296 SGIqFGSWGSFQLPGLlnfgefkcsdsdkkcHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRnvHPKPKLVRV 375
Cdd:COG0038 198 RLL-FGNGPLFGVPSV---------------PALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKR--LKLPPWLRP 259

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  376 lesllvslvttvvvFVASMVLGecrqmsstsqtgngsfqlqvtsedvnstIKAFFCPNdtyndmatLFFNSqESAILQLF 455
Cdd:COG0038 260 --------------AIGGLLVG----------------------------LLGLFLPQ--------VLGSG-YGLIEALL 288

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  456 HqdGTFSPVTLALFFILYFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVV 535
Cdd:COG0038 289 N--GELSLLLLLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLGLSPGLFALVGMAAVFAAVT 366

                       490       500       510       520
                ....*....|....*....|....*....|....*....|....
gi 3182956  536 RMTISLTVILIESTNEITYGLPIMVTLMVAKWT-GDLFNKGIYD 578
Cdd:COG0038 367 RAPLTAILLVLEMTGSYSLLLPLMIACVIAYLVsRLLFPRSIYT 410
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 88-565 6.82e-29

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: 119.59  E-value: 6.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   88 GVCTGLVGLFVDFSVRLFTQLKFGVVQtsveecSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPE-IKCYL 166
Cdd:cd00400   1 GVLSGLGAVLFRLLIELLQNLLFGGLP------GELAAGSLSPLYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  167 NGvkvPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLPQFQSISLRKIQ--------------FNfpyf 232
Cdd:cd00400  75 LG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRilvacgaaagiaaaFN---- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  233 rsdrdkrdfvsagaaagvaaafgAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFrsgiqFGSWGSFQLPGLl 312
Cdd:cd00400 148 -----------------------APLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLL-----FGAEPAFGVPLY- 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  313 nfgefkcsdsdkkcHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAkyRMRNVHPKPKLVRVLesllvslvttvvvfVA 392
Cdd:cd00400 199 --------------DPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIE--RLFRRLPIPPWLRPA--------------LG 248

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  393 SMVLGecrqmsstsqtgngsfqlqvtsedvnstIKAFFCPndtyndmATLFFNsqESAILQLFHQDgtFSPVTLALFFIL 472
Cdd:cd00400 249 GLLLG----------------------------LLGLFLP-------QVLGSG--YGAILLALAGE--LSLLLLLLLLLL 289

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  473 YFLLACWTFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGVVRMTISLTVILIestnEI 552
Cdd:cd00400 290 KLLATALTLGSGFPGGVFAPSLFIGAALGAAFGLLLPALFPGLVASPGAYALVGMAALLAAVLRAPLTAILLVL----EL 365

                       490
                ....*....|...
gi 3182956  553 TYGLPIMVTLMVA 565
Cdd:cd00400 366 TGDYSLLLPLMLA 378
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 601-854 1.42e-22

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: 93.35  E-value: 1.42e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  601 RASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNekefmkgnqlisnnikfkkssiltrageqrkrgqsmk 680
Cdd:cd04591   1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQ------------------------------------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  681 sypsselrnvcdehvaseepaekedllqqmlerrytpypnlypdqspsedwtmeerfrplTFHGLVLRSQLVTLLVRgvc 760
Cdd:cd04591  44 ------------------------------------------------------------TLVGFILRSQLILLLEA--- 60

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  761 ysesqssasqprlsyaemaedyprypdihdldltllnprmivDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVN 840
Cdd:cd04591  61 ------------------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTN 98

                       250
                ....*....|....
gi 3182956  841 AvGEIVGIITRHNL 854
Cdd:cd04591  99 N-GRLVGIVTRKDL 111
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
87-579 2.37e-18

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 88.80  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956    87 IGVCTGLVGLFVDFSVRLFTQLKFGVVQTSveecsqKGCLALSLLELLGFNLTFVFLASLLVL-IEPVAAGSGIPEIKCY 165
Cdd:PRK05277   7 VGTLTGLVGVAFELAVDWVQNQRLGLLASV------ADNGLLLWIVAFLISAVLAMIGYFLVRrFAPEAGGSGIPEIEGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   166 LNGVKvpGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVVGAGLpqfqsISLRKIqfnfpyfRSDRDKRDFVSAG 245
Cdd:PRK05277  81 LEGLR--PVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMV-----LDIFRL-------RSDEARHTLLAAG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   246 AAAGVAAAFGAPIGGTLFSLEE-GSSFWNQGLTWK-VLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLlnfgefkcsDSd 323
Cdd:PRK05277 147 AAAGLAAAFNAPLAGILFVIEEmRPQFRYSLISIKaVFIGVIMATIVFRLFNGEQAVIEVGKFSAPPL---------NT- 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   324 kkchLWtamdlgFFVVMGVIGGLLGATFN-CLNKRLAKYRMRNVHPKPKLVrvlesllvslvttvvvfVASMVLGecrqm 402
Cdd:PRK05277 217 ----LW------LFLLLGIIFGIFGVLFNkLLLRTQDLFDRLHGGNKKRWV-----------------LMGGAVG----- 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   403 sstsqtgnGSFQLQvtsedvnstikAFFCPNDTYNDMATlffnsqesaILQLFhqDGTFSPVTLALFFILYFLLACWTFG 482
Cdd:PRK05277 265 --------GLCGLL-----------GLLAPAAVGGGFNL---------IPIAL--AGNFSIGMLLFIFVARFITTLLCFG 314

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   483 TSVPSGLFVPSL----LCGAAFGRLVANVLKSYiglgHLYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPI 558
Cdd:PRK05277 315 SGAPGGIFAPMLalgtLLGLAFGMVAAALFPQY----HIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPL 390

                        490       500
                 ....*....|....*....|....*
gi 3182956   559 MVT----LMVAKWTGdlfNKGIYDV 579
Cdd:PRK05277 391 IITclgaTLLAQFLG---GKPIYSA 412
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 152-578 8.08e-15

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: 77.27  E-value: 8.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  152 PVAAGSGIPEIKCYL---NGVKVPGIVRLRTLLCKVFGVLFSVSGGLFVGKEGPMIHSGAVV----GAGLPQFQSISLRK 224
Cdd:cd01034  49 PGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREGPSVQIGAAVmlaiGRRLPKWGGLSERG 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  225 I-----------QFNfpyfrsdrdkrdfvsagaaagvaaafgAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLnf 293
Cdd:cd01034 129 LilaggaaglaaAFN---------------------------TPLAGIVFAIEELSRDFELRFSGLVLLAVIAAGLVS-- 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  294 frsgiqFGSWGSFqlpglLNFGEFKCsdsdkkcHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLV 373
Cdd:cd01034 180 ------LAVLGNY-----PYFGVAAV-------ALPLGEAWLLVLVCGVVGGLAGGLFARLLVALSSGLPGWVRRFRRRR 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  374 RVLesllvsLVTTVVVFVASMVLGecrqmsstsqTGNGSFqlqvtsedvnstikaffcpndtyndmatlffNSQESAILQ 453
Cdd:cd01034 242 PVL------FAALCGLALALIGLV----------SGGLTF-------------------------------GTGYLQARA 274

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  454 LFHQDGTFSPvtlalFFILYFLLACW-TFGTSVPSGLFVPSLLCGAAFGRLVANVLksyiglGHLYSGTFALIGAAAFLG 532
Cdd:cd01034 275 ALEGGGGLPL-----WFGLLKFLATLlSYWSGIPGGLFAPSLAVGAGLGSLLAALL------GSVSQGALVLLGMAAFLA 343

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 3182956  533 GVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDLF-NKGIYD 578
Cdd:cd01034 344 GVTQAPLTAFVIVMEMTGDQQMLLPLLAAALLASGVSRLVcPEPLYH 390
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
807-870 1.22e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 62.96  E-value: 1.22e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3182956  807 YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQARLRQHYQTL 870
Cdd:COG3448   7 IMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERL 70
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 812-854 4.19e-11

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: 58.68  E-value: 4.19e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 3182956     812 PFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 804-859 7.58e-11

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: 57.99  E-value: 7.58e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 3182956    804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFL 859
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
808-865 1.38e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 59.88  E-value: 1.38e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQARLRQ 865
Cdd:COG3448  79 MTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 804-854 1.40e-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: 59.18  E-value: 1.40e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:cd02205  61 VAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
CBS COG0517
CBS domain [Signal transduction mechanisms];
804-860 1.48e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 59.49  E-value: 1.48e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQ 860
Cdd:COG0517  69 VSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
789-858 2.02e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 61.44  E-value: 2.02e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3182956  789 HDLDLTLLNPRMIVD--VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEF 858
Cdd:COG2524 135 RDLLKALAEGRDLLDapVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 807-860 1.14e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 56.76  E-value: 1.14e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 3182956  807 YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITRHNLTNEFLQ 860
Cdd:COG2905  70 VMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSE 122
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 804-858 5.58e-09

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: 54.84  E-value: 5.58e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEF 858
Cdd:cd09836  61 VEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 808-855 2.41e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) 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: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 52.83  E-value: 2.41e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLT 855
Cdd:cd04607  64 MNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLL 111
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 807-850 2.72e-08

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: 53.19  E-value: 2.72e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 3182956  807 YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIIT 850
Cdd:cd04584   5 IMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDD-GKLVGIVT 47
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
804-866 3.26e-08

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 54.89  E-value: 3.26e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITRHNLTNEFLQARLRQH 866
Cdd:COG2524  88 VKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLD 149
CBS COG0517
CBS domain [Signal transduction mechanisms];
807-854 1.33e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 51.02  E-value: 1.33e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 3182956  807 YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:COG0517   6 IMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDL 53
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 809-856 1.75e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 50.79  E-value: 1.75e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 3182956  809 NPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTN 856
Cdd:cd04632   1 TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVD 48
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 801-865 2.93e-07

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: 50.23  E-value: 2.93e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3182956  801 IVDVtpyMNPSPFTV--SPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITrhnltneflQARLRQ 865
Cdd:cd04620  81 IAEV---MTQPVITLkeSEFQDIFTVLSLLRQHQIRHLPIVDDQGQLVGLIT---------PESLRQ 135
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 808-854 3.18e-07

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: 50.25  E-value: 3.18e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:cd04600  81 MTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDL 127
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 808-866 5.10e-07

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: 49.48  E-value: 5.10e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLtneFLQARLRQH 866
Cdd:cd04600   1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADL---LKHADLDPP 56
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 808-854 7.24e-07

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 49.35  E-value: 7.24e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITRHNL 854
Cdd:cd04586  89 MTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADL 134
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 808-850 1.43e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; 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: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 47.92  E-value: 1.43e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIIT 850
Cdd:cd17775  67 MSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVT 109
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
449-568 1.69e-06

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 51.67  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   449 SAILQLFHQdgtfSPVTLALFFILYFLLACW--TFGTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIG 526
Cdd:PRK01862 301 SVVNTILHA----PWTWQALVAVLVAKLIATaaTAGSGAVGGVFTPTLFVGAVVGSLFGLAMHALWPGHTSAPFAYAMVG 376

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 3182956   527 AAAFLGG-----------VVRMTISLTVIliestneitygLPIMVTLMVAKWT 568
Cdd:PRK01862 377 MGAFLAGatqaplmailmIFEMTLSYQVV-----------LPLMVSCVVAYFT 418
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
798-861 2.02e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 51.37  E-value: 2.02e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3182956   798 PRMIVDVTP----YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQA 861
Cdd:PRK14869  60 PELIEDVKPqvrdLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYMDI 127
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 797-854 2.35e-06

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: 47.85  E-value: 2.35e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3182956  797 NPRMIVDVtpyMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:cd17789  84 NGKVVGDV---MTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNV 138
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 804-861 4.33e-06

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 46.28  E-value: 4.33e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITRHNLtnefLQA 861
Cdd:cd04629  64 VADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDV----LRA 116
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 804-864 4.65e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 46.75  E-value: 4.65e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQARLR 864
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLD 61
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
795-861 5.90e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 46.44  E-value: 5.90e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3182956  795 LLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQA 861
Cdd:COG4109  69 ILGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQKI 135
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 450-559 8.32e-06

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: 49.21  E-value: 8.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  450 AILQLFHQDGTFSPVTLALFF--ILYFLLACWTFGTSvpsGLFVPSLLCGAAFGRLVANVLKSYigLGHLYSGTFALIGA 527
Cdd:cd01033 266 ALAQLAFSTTLTLSLLLILLVlkIVATLLALRAGAYG---GLLTPSLALGALLGALLGIVWNAL--LPPLSIAAFALIGA 340

                        90       100       110
                ....*....|....*....|....*....|....
gi 3182956  528 AAFLGGVVRMTISLTVILIEST--NEITYgLPIM 559
Cdd:cd01033 341 AAFLAATQKAPLTALILVLEFTrqNPLFL-IPLM 373
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 812-856 9.26e-06

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: 45.31  E-value: 9.26e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 3182956  812 PFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTN 856
Cdd:cd02205   4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILR 48
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 804-854 1.42e-05

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 45.22  E-value: 1.42e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:cd04608   4 VRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNL 54
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 789-854 1.42e-05

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. 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: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 45.41  E-value: 1.42e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3182956  789 HDLDL-TLLNPRMIVDvtpYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNL 854
Cdd:cd17777  70 HQGDLySALNREVVET---IMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDL 133
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 808-850 2.61e-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: 44.73  E-value: 2.61e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIIT 850
Cdd:cd04586   1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVS 43
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 785-856 2.61e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. 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: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 44.05  E-value: 2.61e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3182956  785 YPDIHDLDLTLLNPRMIVDVtpyMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTN 856
Cdd:cd04583  40 IVDIEDINRNYRKAKKVGEI---MERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTRASLVD 108
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 803-850 3.33e-05

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: 43.85  E-value: 3.33e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 3182956  803 DVTPYMNPSPFTVSPNTHVSQVFN-LFRtMGLRHLPVVNAVGEIVGIIT 850
Cdd:cd04610  54 KVSEIMSRDTVVADPDMDITDAARvIFR-SGISKLPVVDDEGNLVGIIT 101
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 808-850 3.35e-05

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. 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: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 43.95  E-value: 3.35e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIIT 850
Cdd:cd04622  66 MTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVS 108
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 790-849 4.25e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 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: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 43.73  E-value: 4.25e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3182956  790 DLDLTL------LNPRmIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGII 849
Cdd:cd17781  43 DKDLARrvvasgLDPR-STLVSSVMTPNPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVL 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 609-656 1.16e-04

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: 40.19  E-value: 1.16e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 3182956     609 NLTYVYPHTRIQSLVSILRTTVHHAFPVVTENrGNEKEFMKGNQLISN 656
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKA 47
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 811-851 1.41e-04

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: 42.02  E-value: 1.41e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 3182956  811 SPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITR 851
Cdd:cd04601   3 DPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTS 43
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 804-850 1.63e-04

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: 42.21  E-value: 1.63e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVfnlFRTM---GLRHLPVVNAvGEIVGIIT 850
Cdd:cd04631   2 VEDYMTKNVITATPGTPIEDV---AKIMvrnGFRRLPVVSD-GKLVGIVT 47
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 802-856 1.84e-04

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


Pssm-ID: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 41.78  E-value: 1.84e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3182956  802 VDVTPYMNPSPFTVSPNTHVSQVFNLFrtMGLRH--LPVVNAvGEIVGIITRHNLTN 856
Cdd:cd17772  58 LPVSEYMTTEFATVTPDAPLSEIQEII--VEQRQrlVPVVED-GRLVGVITRTDLLN 111
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
591-641 1.99e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 42.21  E-value: 1.99e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 3182956  591 WETDVEMDKLRASDIM-EPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENR 641
Cdd:COG4109   7 TSYDTFKEILLVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG 58
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 804-849 2.44e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; 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: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 41.25  E-value: 2.44e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 3182956  804 VTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGII 849
Cdd:cd04623  62 VSEIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVED-GKLVGIV 106
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 808-850 3.05e-04

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


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 41.17  E-value: 3.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIIT 850
Cdd:cd04606  71 MDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIIT 113
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
800-856 3.57e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.44  E-value: 3.57e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3182956  800 MIVDVTPYM-NPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTN 856
Cdd:COG4109  14 EILLVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG 71
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 786-851 4.35e-04

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 40.87  E-value: 4.35e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3182956  786 PDIHDLDLtLLNPRMIVDVtpyMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITR 851
Cdd:cd04584  62 LSIYELNY-LLSKIPVKDI---MTKDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITE 122
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 807-851 4.47e-04

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 40.56  E-value: 4.47e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 3182956  807 YMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITR 851
Cdd:cd04595  61 YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEE-GKLVGIVTR 104
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 808-850 4.60e-04

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 40.40  E-value: 4.60e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIIT 850
Cdd:cd04599   1 MTRNPITISPLDSVARAAALMERQRIGGLPVVEN-GKLVGIIT 42
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 602-640 5.88e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 38.73  E-value: 5.88e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 3182956    602 ASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTEN 640
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDED 39
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 808-855 7.31e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. 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: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 40.10  E-value: 7.31e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITRHNLT 855
Cdd:cd04587  66 MTPPPVTIDADALVFEALLLMLERNIHHLPVVDD-GRVVGVVTATDLM 112
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 808-850 8.75e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; 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: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 39.63  E-value: 8.75e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIIT 850
Cdd:cd04638  61 MSRDPITISPDDTLSEAAELMLEHNIRRVPVVDD-DKLVGIVT 102
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
795-850 1.12e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 42.36  E-value: 1.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3182956  795 LLNPR--MIVDVtpyMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIIT 850
Cdd:COG2239 187 LLADPdtKVSDI---MDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIIT 241
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 799-855 1.38e-03

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: 39.09  E-value: 1.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3182956  799 RMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAvGEIVGIITRHNLT 855
Cdd:cd04801  56 REATRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 789-851 2.38e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; 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: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 38.28  E-value: 2.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3182956  789 HDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITR 851
Cdd:cd04588  43 TDIAKALAEGKENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITR 105
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 807-852 2.48e-03

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 38.22  E-value: 2.48e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 3182956  807 YMNPSPFTVSPNT---HVSQVfnlfrtM---GLRHLPVVNAVGEIVGIITRH 852
Cdd:cd04596  58 VMTKNPITVKPKTsvaSAAHM------MiweGIELLPVVDENRKLLGVISRQ 103
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 800-854 5.18e-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: 40.45  E-value: 5.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 3182956    800 MIVDvtpymnpsPFTVSPNTHVSQVFNLFRTMGLRHLPVVNaVGEIVGIITRHNL 854
Cdd:pfam00478  86 MITD--------PVTLSPDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDL 131
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 778-850 5.21e-03

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: 37.86  E-value: 5.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956  778 MAEDYPRYP-------------DIHDLDLTLLNPRMIVDVTPYMNPsPFTVSPNTHVSQVFNLFRT----MGLrhlpVVN 840
Cdd:cd04590  29 LESGYSRFPvyegdldniigvlHVKDLLAALLEGREKLDLRALLRP-PLFVPETTPLDDLLEEFRKershMAI----VVD 103

                        90
                ....*....|
gi 3182956  841 AVGEIVGIIT 850
Cdd:cd04590 104 EYGGTAGIVT 113
CBS_pair_GGDEF_EAL cd04598
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 814-860 5.44e-03

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


Pssm-ID: 341373 [Multi-domain]  Cd Length: 121  Bit Score: 37.80  E-value: 5.44e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 3182956  814 TVSPNTHVSQVFNLFRTM-GLRHLPVVNAvGEIVGIITRHNLTNEFLQ 860
Cdd:cd04598   7 PVSPDTTNDEVYELFEENpDLHALPVVDN-GRPVGLINRHQFLDRLAT 53
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 482-570 6.46e-03

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 39.76  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3182956   482 GTSVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHLYSGTFALIGAAAFLGGvvrmtisltviliestneiTYGLPIMVT 561
Cdd:PRK01610 314 GSGAPGGVFTPTLFVGLAIGMLYGRSLGLWLPDGEEITLLLGLTGMATLLAA-------------------TTHAPIMST 374


                 ....*....
gi 3182956   562 LMVAKWTGD 570
Cdd:PRK01610 375 LMICEMTGE 383
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 808-860 7.91e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 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: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 37.23  E-value: 7.91e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTNEFLQ 860
Cdd:cd17782  66 MTPNPETAPPSTTILDALHKMHEGKFLNLPVVDDEGEIVGLVDVLQLTYATLQ 118
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 808-856 9.38e-03

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: 36.78  E-value: 9.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 3182956  808 MNPSPFTVSPNTHVSQVFNL-FRTmglRHL--PVVNAvGEIVGIITRHNLTN 856
Cdd:cd04801   3 MTPEVVTVTPEMTVSELLDRmFEE---KHLgyPVVEN-GRLVGIVTLEDIRK 50
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 808-850 9.97e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 36.65  E-value: 9.97e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 3182956  808 MNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIIT 850
Cdd:cd04629   1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLS 43
 
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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