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Conserved domains on  [gi|1126499250|gb|APR64275|]
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hypothetical protein [Populus tomentosa]

Protein Classification

chloride channel protein( domain architecture ID 10087042)

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
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 156-559 2.43e-108

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: 336.07  E-value: 2.43e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 156 ASGLCVAAFNKGVHLIHEWAWAGTPNEGAAWlrlqrlSDTWHRILLIPVAGGVIVGMM---------HGLVEILEQIRqn 226
Cdd:cd00400     3 LSGLGAVLFRLLIELLQNLLFGGLPGELAAG------SLSPLYILLVPVIGGLLVGLLvrllgpargHGIPEVIEAIA-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 227 lssHRKGfdLVAGVFPTVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGFNAP 306
Cdd:cd00400    75 ---LGGG--RLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAAGIAAAFNAP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 307 VAGCFFAIETVLRPLHAEnsppfTTAMILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSVAFT 386
Cdd:cd00400   150 LAGALFAIEVLLGEYSVA-----SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 387 RLVTWFTKAFefikEKFGLHPVACPALGGLGAGIIALKYPGILYWGFTNVEEILhtgksASAPGIWLLTQLAAAKVVATA 466
Cdd:cd00400   225 RLLYKIERLF----RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLLLLLLLLLKLLATA 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 467 LCKGSLLVGGLYAPSLMIGAAVGAVFGgsaaELINSAIPGnaAVAQPQAYALVGMAATLASVCSVPLTSILLLFELTKDY 546
Cdd:cd00400   296 LTLGSGFPGGVFAPSLFIGAALGAAFG----LLLPALFPG--LVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDY 369

                         410
                  ....*....|...
gi 1126499250 547 RIILPLMGAVGLA 559
Cdd:cd00400   370 SLLLPLMLAVVIA 382
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 611-750 1.80e-54

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: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 183.72  E-value: 1.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKTSSdastgdSTIIDVNTCLVSTVCTREI 690
Cdd:cd04592     1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAK------ADNEDPKTILVSSICTRNG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 691 RYRgqvRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGGsqkDWKRRVVAILHYDSIW 750
Cdd:cd04592    75 GYC---RGLWTCTPDMDLLTAKMLMEARGINQLPVVKRGGE---ERRRRVVGLLDRDSID 128
 
Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 156-559 2.43e-108

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: 336.07  E-value: 2.43e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 156 ASGLCVAAFNKGVHLIHEWAWAGTPNEGAAWlrlqrlSDTWHRILLIPVAGGVIVGMM---------HGLVEILEQIRqn 226
Cdd:cd00400     3 LSGLGAVLFRLLIELLQNLLFGGLPGELAAG------SLSPLYILLVPVIGGLLVGLLvrllgpargHGIPEVIEAIA-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 227 lssHRKGfdLVAGVFPTVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGFNAP 306
Cdd:cd00400    75 ---LGGG--RLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAAGIAAAFNAP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 307 VAGCFFAIETVLRPLHAEnsppfTTAMILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSVAFT 386
Cdd:cd00400   150 LAGALFAIEVLLGEYSVA-----SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 387 RLVTWFTKAFefikEKFGLHPVACPALGGLGAGIIALKYPGILYWGFTNVEEILhtgksASAPGIWLLTQLAAAKVVATA 466
Cdd:cd00400   225 RLLYKIERLF----RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLLLLLLLLLKLLATA 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 467 LCKGSLLVGGLYAPSLMIGAAVGAVFGgsaaELINSAIPGnaAVAQPQAYALVGMAATLASVCSVPLTSILLLFELTKDY 546
Cdd:cd00400   296 LTLGSGFPGGVFAPSLFIGAALGAAFG----LLLPALFPG--LVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDY 369

                         410
                  ....*....|...
gi 1126499250 547 RIILPLMGAVGLA 559
Cdd:cd00400   370 SLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
156-562 1.70e-88

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 285.11  E-value: 1.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 156 ASGLCVAAFNKGVHLIHEWAWAGTPNEGAAWLRlqrlsdtWHRILLIPVAGGVIVGMM----------HGLVEILEQIRQ 225
Cdd:COG0038    17 LAGLAAVLFRLLLELATHLFLGGLLSAAGSHLP-------PWLVLLLPPLGGLLVGLLvrrfapeargSGIPQVIEAIHL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 226 NLS--SHRKGFdlvagvfptVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGF 303
Cdd:COG0038    90 KGGriPLRVAP---------VKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLSPEDRRILLAAGAAAGLAAAF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 304 NAPVAGCFFAIETVLRPLHAENSPPfttamILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSV 383
Cdd:COG0038   161 NAPLAGALFALEVLLRDFSYRALIP-----VLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLLLGILAGLVGV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 384 AFTRLVTWFTKAFefikEKFGLHPVACPALGGLGAGIIALKYPGILYWGFTNVEEILHTGksasaPGIWLLTQLAAAKVV 463
Cdd:COG0038   236 LFNRLLLKVERLF----KRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGE-----LSLLLLLLLLLLKLL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 464 ATALCKGSLLVGGLYAPSLMIGAAVGAVFGGsaaeLINSAIPGnaAVAQPQAYALVGMAATLASVCSVPLTSILLLFELT 543
Cdd:COG0038   307 ATALTLGSGGPGGIFAPSLFIGALLGAAFGL----LLNLLFPG--LGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMT 380

                         410
                  ....*....|....*....
gi 1126499250 544 KDYRIILPLMGAVGLAIWV 562
Cdd:COG0038   381 GSYSLLLPLMIACVIAYLV 399
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 206-562 7.43e-76

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: 249.00  E-value: 7.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 206 GGVIVGMM----------HGLVEILEQirqnLSSHRKGFDLVAGVfptVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHG 275
Cdd:pfam00654   1 GGLLAGWLvkrfapeaagSGIPEVKAA----LHGGRGPLPLRVLP---VKFLGTVLTLGSGLSLGREGPSVQIGAAIGSG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 276 FS-LMMANNRERMNTLVAAGAAAGISSGFNAPVAGCFFAIETVLRplhaeNSPPFTTAMILLASVISSTVSNTLLGTQSA 354
Cdd:pfam00654  74 LGrRLFRLSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSR-----SFSLRALIPVLLASVVAALVSRLIFGNSPL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 355 FTVPSYDLKSAAELPLYLILGMLCGVVSVAFTRLVTWFTKAFefiKEKFGLHPVACPALGGLGAGIIALKYPGILYWGFT 434
Cdd:pfam00654 149 FSVGEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLF---RKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 435 NVEEILHtgksaSAPGIWLLTQLAAAKVVATALCKGSLLVGGLYAPSLMIGAAVGAVFGgsaaELINSAIPGNAAvaQPQ 514
Cdd:pfam00654 226 LIQLLFN-----GNTSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFG----LLLALLFPIGGL--PPG 294

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1126499250 515 AYALVGMAATLASVCSVPLTSILLLFELTKDYRIILPLMGAVGLAIWV 562
Cdd:pfam00654 295 AFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 611-750 1.80e-54

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: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 183.72  E-value: 1.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKTSSdastgdSTIIDVNTCLVSTVCTREI 690
Cdd:cd04592     1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAK------ADNEDPKTILVSSICTRNG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 691 RYRgqvRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGGsqkDWKRRVVAILHYDSIW 750
Cdd:cd04592    75 GYC---RGLWTCTPDMDLLTAKMLMEARGINQLPVVKRGGE---ERRRRVVGLLDRDSID 128
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
156-556 2.35e-53

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 194.58  E-value: 2.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 156 ASGLCVAAFNKGVHLIHEWAwagTPNEGAAWLRLQRLSDTWhRILLiPVAGGVIVGMMHGLVEILEQiRQNLSSHRKGFD 235
Cdd:PRK01862   34 GGAFATTAFREGIELIQHLI---SGHSGSFVEMAKSLPWYV-RVWL-PAAGGFLAGCVLLLANRGAR-KGGKTDYMEAVA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 236 LVAGVFPT----VKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGFNAPVAGCF 311
Cdd:PRK01862  108 LGDGVVPVrqslWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGITSAYNAPIAGAF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 312 FAIETVLRPLHAENSPPfttamILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSvaftrlvTW 391
Cdd:PRK01862  188 FVAEIVLGSIAMESFGP-----LVVASVVANIVMREFAGYQPPYEMPVFPAVTGWEVLLFVALGVLCGAAA-------PQ 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 392 FTKAFEFIKEKFGLHPVACP---ALGGLGAGIIALKYPGILYWGFTNVEEILHTgksasaPGIWL-LTQLAAAKVVATAL 467
Cdd:PRK01862  256 FLRLLDASKNQFKRLPVPLPvrlALGGLLVGVISVWVPEVWGNGYSVVNTILHA------PWTWQaLVAVLVAKLIATAA 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 468 CKGSLLVGGLYAPSLMIGAAVGAVFGGSAaeliNSAIPGnaAVAQPQAYALVGMAATLASVCSVPLTSILLLFELTKDYR 547
Cdd:PRK01862  330 TAGSGAVGGVFTPTLFVGAVVGSLFGLAM----HALWPG--HTSAPFAYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQ 403

                         410
                  ....*....|
gi 1126499250 548 IILPLM-GAV 556
Cdd:PRK01862  404 VVLPLMvSCV 413
CBS COG0517
CBS domain [Signal transduction mechanisms];
605-758 1.15e-21

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 91.08  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 605 LKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSktssdastgDSTIIDVNTCLVST 684
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRAL---------AAEGKDLLDTPVSE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126499250 685 VCTREiryrgqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGgsqkdwkrRVVAILHYDSIWNCLREEIA 758
Cdd:COG0517    72 VMTRP---------PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDG--------RLVGIITIKDLLKALLEPLA 128
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 607-660 7.27e-09

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: 52.22  E-value: 7.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126499250 607 VSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRL 660
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 618-657 1.94e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 36.72  E-value: 1.94e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1126499250  618 VSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI 657
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
 
Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 156-559 2.43e-108

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: 336.07  E-value: 2.43e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 156 ASGLCVAAFNKGVHLIHEWAWAGTPNEGAAWlrlqrlSDTWHRILLIPVAGGVIVGMM---------HGLVEILEQIRqn 226
Cdd:cd00400     3 LSGLGAVLFRLLIELLQNLLFGGLPGELAAG------SLSPLYILLVPVIGGLLVGLLvrllgpargHGIPEVIEAIA-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 227 lssHRKGfdLVAGVFPTVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGFNAP 306
Cdd:cd00400    75 ---LGGG--RLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAAGIAAAFNAP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 307 VAGCFFAIETVLRPLHAEnsppfTTAMILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSVAFT 386
Cdd:cd00400   150 LAGALFAIEVLLGEYSVA-----SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 387 RLVTWFTKAFefikEKFGLHPVACPALGGLGAGIIALKYPGILYWGFTNVEEILhtgksASAPGIWLLTQLAAAKVVATA 466
Cdd:cd00400   225 RLLYKIERLF----RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLLLLLLLLLKLLATA 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 467 LCKGSLLVGGLYAPSLMIGAAVGAVFGgsaaELINSAIPGnaAVAQPQAYALVGMAATLASVCSVPLTSILLLFELTKDY 546
Cdd:cd00400   296 LTLGSGFPGGVFAPSLFIGAALGAAFG----LLLPALFPG--LVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDY 369

                         410
                  ....*....|...
gi 1126499250 547 RIILPLMGAVGLA 559
Cdd:cd00400   370 SLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
156-562 1.70e-88

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 285.11  E-value: 1.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 156 ASGLCVAAFNKGVHLIHEWAWAGTPNEGAAWLRlqrlsdtWHRILLIPVAGGVIVGMM----------HGLVEILEQIRQ 225
Cdd:COG0038    17 LAGLAAVLFRLLLELATHLFLGGLLSAAGSHLP-------PWLVLLLPPLGGLLVGLLvrrfapeargSGIPQVIEAIHL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 226 NLS--SHRKGFdlvagvfptVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGF 303
Cdd:COG0038    90 KGGriPLRVAP---------VKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLSPEDRRILLAAGAAAGLAAAF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 304 NAPVAGCFFAIETVLRPLHAENSPPfttamILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSV 383
Cdd:COG0038   161 NAPLAGALFALEVLLRDFSYRALIP-----VLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLLLGILAGLVGV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 384 AFTRLVTWFTKAFefikEKFGLHPVACPALGGLGAGIIALKYPGILYWGFTNVEEILHTGksasaPGIWLLTQLAAAKVV 463
Cdd:COG0038   236 LFNRLLLKVERLF----KRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGE-----LSLLLLLLLLLLKLL 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 464 ATALCKGSLLVGGLYAPSLMIGAAVGAVFGGsaaeLINSAIPGnaAVAQPQAYALVGMAATLASVCSVPLTSILLLFELT 543
Cdd:COG0038   307 ATALTLGSGGPGGIFAPSLFIGALLGAAFGL----LLNLLFPG--LGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMT 380

                         410
                  ....*....|....*....
gi 1126499250 544 KDYRIILPLMGAVGLAIWV 562
Cdd:COG0038   381 GSYSLLLPLMIACVIAYLV 399
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 206-562 7.43e-76

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: 249.00  E-value: 7.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 206 GGVIVGMM----------HGLVEILEQirqnLSSHRKGFDLVAGVfptVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHG 275
Cdd:pfam00654   1 GGLLAGWLvkrfapeaagSGIPEVKAA----LHGGRGPLPLRVLP---VKFLGTVLTLGSGLSLGREGPSVQIGAAIGSG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 276 FS-LMMANNRERMNTLVAAGAAAGISSGFNAPVAGCFFAIETVLRplhaeNSPPFTTAMILLASVISSTVSNTLLGTQSA 354
Cdd:pfam00654  74 LGrRLFRLSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSR-----SFSLRALIPVLLASVVAALVSRLIFGNSPL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 355 FTVPSYDLKSAAELPLYLILGMLCGVVSVAFTRLVTWFTKAFefiKEKFGLHPVACPALGGLGAGIIALKYPGILYWGFT 434
Cdd:pfam00654 149 FSVGEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLF---RKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 435 NVEEILHtgksaSAPGIWLLTQLAAAKVVATALCKGSLLVGGLYAPSLMIGAAVGAVFGgsaaELINSAIPGNAAvaQPQ 514
Cdd:pfam00654 226 LIQLLFN-----GNTSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFG----LLLALLFPIGGL--PPG 294

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1126499250 515 AYALVGMAATLASVCSVPLTSILLLFELTKDYRIILPLMGAVGLAIWV 562
Cdd:pfam00654 295 AFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAV 342
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 611-750 1.80e-54

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: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 183.72  E-value: 1.80e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKTSSdastgdSTIIDVNTCLVSTVCTREI 690
Cdd:cd04592     1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAK------ADNEDPKTILVSSICTRNG 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 691 RYRgqvRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGGsqkDWKRRVVAILHYDSIW 750
Cdd:cd04592    75 GYC---RGLWTCTPDMDLLTAKMLMEARGINQLPVVKRGGE---ERRRRVVGLLDRDSID 128
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 157-562 2.09e-54

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: 193.14  E-value: 2.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 157 SGLCVAAFNKGVHLIHEWawagtpnegaaWLRL-QRLSDTWHRILLIPVAGGVIVGMMHGLVEILE---------QIRQN 226
Cdd:cd01031     5 AGLVAVLFRLGIDKLGNL-----------RLSLyDFAANNPPLLLVLPLISAVLGLLAGWLVKKFApeakgsgipQVEGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 227 LSSHRKGFDLvaGVFPtVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFS-LMMANNRERmNTLVAAGAAAGISSGFNA 305
Cdd:cd01031    74 LAGLLPPNWW--RVLP-VKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSkWFKTSPEER-RQLIAAGAAAGLAAAFNA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 306 PVAGCFFAIETVLRplhaeNSPPFTTAMILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSVAF 385
Cdd:cd01031   150 PLAGVLFVLEELRH-----SFSPLALLTALVASIAADFVSRLFFGLGPVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLF 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 386 TRLVTWFTKAFEFIKekfGLHPVACPALGGLGAGIIALKYPGILYWGFTNVEEILHTGksasaPGIWLLTQLAAAKVVAT 465
Cdd:cd01031   225 NRSLLKSQDLYRKLK---KLPRELRVLLPGLLIGPLGLLLPEALGGGHGLILSLAGGN-----FSISLLLLIFVLRFIFT 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 466 ALCKGSLLVGGLYAPSLMIGAAVGAVFGGSAAELinsaipGNAAVAQPQAYALVGMAATLASVCSVPLTSILLLFELTKD 545
Cdd:cd01031   297 MLSYGSGAPGGIFAPMLALGALLGLLFGTILVQL------GPIPISAPATFAIAGMAAFFAAVVRAPITAIILVTEMTGN 370

                         410
                  ....*....|....*..
gi 1126499250 546 YRIILPLMGAVGLAIWV 562
Cdd:cd01031   371 FNLLLPLMVVCLVAYLV 387
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
156-556 2.35e-53

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 194.58  E-value: 2.35e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 156 ASGLCVAAFNKGVHLIHEWAwagTPNEGAAWLRLQRLSDTWhRILLiPVAGGVIVGMMHGLVEILEQiRQNLSSHRKGFD 235
Cdd:PRK01862   34 GGAFATTAFREGIELIQHLI---SGHSGSFVEMAKSLPWYV-RVWL-PAAGGFLAGCVLLLANRGAR-KGGKTDYMEAVA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 236 LVAGVFPT----VKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGFNAPVAGCF 311
Cdd:PRK01862  108 LGDGVVPVrqslWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGITSAYNAPIAGAF 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 312 FAIETVLRPLHAENSPPfttamILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSvaftrlvTW 391
Cdd:PRK01862  188 FVAEIVLGSIAMESFGP-----LVVASVVANIVMREFAGYQPPYEMPVFPAVTGWEVLLFVALGVLCGAAA-------PQ 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 392 FTKAFEFIKEKFGLHPVACP---ALGGLGAGIIALKYPGILYWGFTNVEEILHTgksasaPGIWL-LTQLAAAKVVATAL 467
Cdd:PRK01862  256 FLRLLDASKNQFKRLPVPLPvrlALGGLLVGVISVWVPEVWGNGYSVVNTILHA------PWTWQaLVAVLVAKLIATAA 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 468 CKGSLLVGGLYAPSLMIGAAVGAVFGGSAaeliNSAIPGnaAVAQPQAYALVGMAATLASVCSVPLTSILLLFELTKDYR 547
Cdd:PRK01862  330 TAGSGAVGGVFTPTLFVGAVVGSLFGLAM----HALWPG--HTSAPFAYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQ 403

                         410
                  ....*....|
gi 1126499250 548 IILPLM-GAV 556
Cdd:PRK01862  404 VVLPLMvSCV 413
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
158-559 2.92e-43

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 162.75  E-value: 2.92e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 158 GLCVAAFNKGVHLIHEWAwagtpnegAAWLrlQRLSDTWHRILLIPVAGGVIVGM-----MH---------GLVEI---L 220
Cdd:PRK05277   12 GLVGVAFELAVDWVQNQR--------LGLL--ASVADNGLLLWIVAFLISAVLAMigyflVRrfapeaggsGIPEIegaL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 221 EQIRQnLSSHRkgfdlvagVFPtVKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGF-SLMMANNRERMNTLVAAGAAAGI 299
Cdd:PRK05277   82 EGLRP-VRWWR--------VLP-VKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVlDIFRLRSDEARHTLLAAGAAAGL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 300 SSGFNAPVAGCFFAIETvLRPLHAENSPPFTtaMILLASVISSTVSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCG 379
Cdd:PRK05277  152 AAAFNAPLAGILFVIEE-MRPQFRYSLISIK--AVFIGVIMATIVFRLFNGEQAVIEVGKFSAPPLNTLWLFLLLGIIFG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 380 VVSVAFTRLVTWFTKAFEFIKEKFGLHPVACPALGGLGAGIIALKYPGILYWGFTNVEEILHTGKSASapgiwLLTQLAA 459
Cdd:PRK05277  229 IFGVLFNKLLLRTQDLFDRLHGGNKKRWVLMGGAVGGLCGLLGLLAPAAVGGGFNLIPIALAGNFSIG-----MLLFIFV 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 460 AKVVATALCKGSLLVGGLYAPSLMIGAAVGAVFGGSAAELINSAIPgnaavaQPQAYALVGMAATLASVCSVPLTSILLL 539
Cdd:PRK05277  304 ARFITTLLCFGSGAPGGIFAPMLALGTLLGLAFGMVAAALFPQYHI------EPGTFAIAGMGALFAATVRAPLTGIVLV 377

                         410       420
                  ....*....|....*....|....
gi 1126499250 540 FELTKDYRIILPLM----GAVGLA 559
Cdd:PRK05277  378 LEMTDNYQLILPLIitclGATLLA 401
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 196-567 3.74e-33

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: 132.03  E-value: 3.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 196 WHRiLLIPVAGGVIVGMMHGLVeileqirqnlssHRKGFDLVAGV--------FPTVKAIQAAV----TLGTGCSLGPEG 263
Cdd:cd01033    40 IRR-ALSLTVGGLIAGLGWYLL------------RRKGKKLVSIKqavrgkkrMPFWETIIHAVlqivTVGLGAPLGREV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 264 PSVDIGKSCAHGFSLMMANNRERMNTLVAAGAAAGISSGFNAPVAGCFFAIETVLRPLHAENsppftTAMILLASVISST 343
Cdd:cd01033   107 APREVGALLAQRFSDWLGLTVADRRLLVACAAGAGLAAVYNVPLAGALFALEILLRTISLRS-----VVAALATSAIAAA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 344 VSNTLLGTQSAFTVPSYDLkSAAELPLYLILGMLCGVVSVAFTRLVTWFTKafefiKEKFGLH-PVACPaLGGLGAGIIA 422
Cdd:cd01033   182 VASLLKGDHPIYDIPPMQL-STPLLIWALLAGPVLGVVAAGFRRLSQAARA-----KRPKGKRiLWQMP-LAFLVIGLLS 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 423 LKYPGILYWGFTNVEEILHTGksasaPGIWLLTQLAAAKVVATALCKGSLLVGGLYAPSLMIGAAVGAVFGGsaaeLINS 502
Cdd:cd01033   255 IFFPQILGNGRALAQLAFSTT-----LTLSLLLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGI----VWNA 325

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126499250 503 AIPGnaavAQPQAYALVGMAATLASVCSVPLTSILLLFELTK-DYRIILPLMGAVGLAIWVPSVAD 567
Cdd:cd01033   326 LLPP----LSIAAFALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGAVAVSRFIL 387
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 256-562 2.18e-31

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: 126.96  E-value: 2.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 256 GCSLGPEGPSVDIGKSCAHGFSLMM-ANNRERMNTLVAAGAAAGISSGFNAPVAGCFFAIETVLRplhaenSPPFTTAMI 334
Cdd:cd01034    94 GASVGREGPSVQIGAAVMLAIGRRLpKWGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSR------DFELRFSGL 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 335 LLASVISST-VSNTLLGTQSAFTVPSYDLKSAAELPLYLILGMLCGVVSVAFTRLVTWFTKAFEFIKEKF-GLHPVACPA 412
Cdd:cd01034   168 VLLAVIAAGlVSLAVLGNYPYFGVAAVALPLGEAWLLVLVCGVVGGLAGGLFARLLVALSSGLPGWVRRFrRRRPVLFAA 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 413 LGGLGAGIIALKYPGILYW-GFTNVEEILHTGKSASApgiwlltQLAAAKVVATALCKGSLLVGGLYAPSLMIGAAVGAV 491
Cdd:cd01034   248 LCGLALALIGLVSGGLTFGtGYLQARAALEGGGGLPL-------WFGLLKFLATLLSYWSGIPGGLFAPSLAVGAGLGSL 320

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126499250 492 FGGSAAElinsaipgnaavAQPQAYALVGMAATLASVCSVPLTSILLLFELTKDYRIILPLMGAVGLAIWV 562
Cdd:cd01034   321 LAALLGS------------VSQGALVLLGMAAFLAGVTQAPLTAFVIVMEMTGDQQMLLPLLAAALLASGV 379
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 244-562 3.54e-24

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: 106.54  E-value: 3.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 244 VKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMM---ANNRERMNTLVAAGAAAGISSGFNAPVAGCFFAIETVlrp 320
Cdd:cd03684    81 IKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFpkyRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEV--- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 321 lhaenSPPFTTAMiLLASVISSTVSNTLL------GTQSA--FTVpSYDLK-SAAELPLYLILGMLCGVVSVAFTRLVTW 391
Cdd:cd03684   158 -----SYYFPLKT-LWRSFFCALVAAFTLkslnpfGTGRLvlFEV-EYDRDwHYFELIPFILLGIFGGLYGAFFIKANIK 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 392 FTKafEFIKEKFGLHPVACPALGGLGAGIIALKYPGI-------LYWGFT-----NVEEILHTGKSASAPGIW-LLTQLA 458
Cdd:cd03684   231 WAR--FRKKSLLKRYPVLEVLLVALITALISFPNPYTrldmtelLELLFNecepgDDNSLCCYRDPPAGDGVYkALWSLL 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 459 AAKVVATALCK---GSLLVGGLYAPSLMIGAAVGAVFG--------GSAAELINSAIPGNAAVAQPQAYALVGMAATLAS 527
Cdd:cd03684   309 LALIIKLLLTIftfGIKVPAGIFVPSMAVGALFGRIVGilveqlaySYPDSIFFACCTAGPSCITPGLYAMVGAAAFLGG 388

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1126499250 528 VCSVPLTSILLLFELTKDYRIILPLMGAVGLAIWV 562
Cdd:cd03684   389 VTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWV 423
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 245-567 7.20e-23

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: 101.94  E-value: 7.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 245 KAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFSLMMA------NNRERMNTLVAAGAAAGISSGFNAPVAGCFFAIETVL 318
Cdd:cd03683    99 KVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTTffsgiyENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTS 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 319 RPLHAENS-PPFTTAMI------LLASVISSTVSNTLLGTQSAFTVPSYDLKsaaELPLYLILGMLCGVVSVAFTRLVTW 391
Cdd:cd03683   179 TYFAVRNYwRGFFAATCgaftfrLLAVFFSDQETITALFKTTFFVDFPFDVQ---ELPIFALLGIICGLLGALFVFLHRK 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 392 ---FTKAFEFIKEKFGLHPVACPALGGLGAGIIAlkYPgilywgFTNveeilhtgksasapgiwlLTQLAAAKVVATALC 468
Cdd:cd03683   256 ivrFRRKNRLFSKFLKRSPLLYPAIVALLTAVLT--FP------FLT------------------LFLFIVVKFVLTALA 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 469 KGSLLVGGLYAPSLMIGAAVGAVFGgsaaELINSAIPGNAAVAQ-----PQAYALVGMAATLASVcSVPLTSILLLFELT 543
Cdd:cd03683   310 ITLPVPAGIFMPVFVIGAALGRLVG----EIMAVLFPEGIRGGIsnpigPGGYAVVGAAAFSGAV-THTVSVAVIIFELT 384

                         330       340
                  ....*....|....*....|....*....
gi 1126499250 544 KDYRIILPLMGAVGLAIWV-----PSVAD 567
Cdd:cd03683   385 GQISHLLPVLIAVLISNAVaqflqPSIYD 413
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 244-562 2.00e-22

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: 100.50  E-value: 2.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 244 VKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFS-------------LMMANNRERMNTLVAAGAAAGISSGFNAPVAGC 310
Cdd:cd01036    90 AKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLqgrsrtlgchvhlFQLFRNPRDRRDFLVAGAAAGVASAFGAPIGGL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 311 FFAIETVlrplhAENSPPFTTAMILLASVISSTVSNTLLGTQSAFTVP-------SYDLKSAAELPLYL-------ILGM 376
Cdd:cd01036   170 LFVLEEV-----STFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFELLdrssamfLSLTVFELHVPLNLyefiptvVIGV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 377 LCGVVSVAFTRLvTWFtkAFEFIKE----KFGLHPVACPALgglgagiIALKYPGILYWGFtnveeilhtgksasapgiw 452
Cdd:cd01036   245 ICGLLAALFVRL-SII--FLRWRRRllfrKTARYRVLEPVL-------FTLIYSTIHYAPT------------------- 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 453 LLTQLaAAKVVATALCKGSLLVGGLYAPSLMIGAAVGAVFGGSAAELINSAIPGNAAV--AQPQAYALVGMAATLASVCS 530
Cdd:cd01036   296 LLLFL-LIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIGAESATlwADPGVYALIGAAAFLGGTTR 374

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1126499250 531 VPLTSILLLFELTKDYRIILPLMGAVGLAIWV 562
Cdd:cd01036   375 LTFSICVIMMELTGDLHHLLPLMVAILIAKAV 406
CBS COG0517
CBS domain [Signal transduction mechanisms];
605-758 1.15e-21

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 91.08  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 605 LKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSktssdastgDSTIIDVNTCLVST 684
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRAL---------AAEGKDLLDTPVSE 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126499250 685 VCTREiryrgqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGgsqkdwkrRVVAILHYDSIWNCLREEIA 758
Cdd:COG0517    72 VMTRP---------PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDG--------RLVGIITIKDLLKALLEPLA 128
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
515-730 2.15e-18

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 84.16  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 515 AYALVGMAATLASVCSVPLTSILLLFELTKDYRIILPLMGAVGLAIWVPSVADHGKENERPGAHSLARGYSSLsndtdge 594
Cdd:COG2524     8 ALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 595 ainedLLAENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIRRLskTSSDASTGDSTi 674
Cdd:COG2524    81 -----GLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLV-GIITERDLLKA--LAEGRDLLDAP- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1126499250 675 idvntclVSTVCTREiryrgqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSG 730
Cdd:COG2524   152 -------VSDIMTRD---------VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDG 191
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 607-749 8.21e-18

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 79.87  E-value: 8.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 607 VSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR--LSKTssdastgdstiIDVNTCLVST 684
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRrvLAEG-----------LDPLDTPVSE 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126499250 685 VCTREiryrgqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVKrsggsqkdwKRRVVAILHYDSI 749
Cdd:COG2905    70 VMTRP---------PITVSPDDSLAEALELMEEHRIRHLPVVD---------DGKLVGIVSITDL 116
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 196-559 4.22e-17

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 84.44  E-value: 4.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 196 WHRiLLIPVAGGVIVGMMHGLVEILEQIRQNLSS------HRKG-FDLVAGVfptVKAIQAAVTLGTGCSLGPEGPSVDI 268
Cdd:PRK01610   51 WRR-LLTPALGGLAAGLLLWGWQKFTQQRPHAPTdymealQTDGqFDYAASL---VKSLASLLVVTSGSAIGREGAMILL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 269 GKSCAHGFSLMMANnRERMNTLVAAGAAAGISSGFNAPVAGCFFAIETVLRPLHAENSPPfttamILLASVISSTVSNTL 348
Cdd:PRK01610  127 AALAASCFAQRFTP-RQEWKLWIACGAAAGMASAYHAPLAGSLFIAEILFGTLMLASLGP-----VVISAVVALLTTNLL 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 349 LGTQSA-FTVPSYDLKSAAELPLYLILGMLCGVVSVAFTRLVTWFTKAFEFIKekfgLHPVACPALGGLGAGIIALKYPG 427
Cdd:PRK01610  201 NGSDALlYNVQLSVTVQARDYALIISTGLLAGLCGPLLLTLMNASHRGFVSLK----LAPPWQLALGGLIVGLLSLFTPA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 428 ILYWGFTNVEEILhtgksASAPGIWLLTQLAAAKVVATALCKGSLLVGGLYAPSLMIGAAVGAVFGgsaaELINSAIPGN 507
Cdd:PRK01610  277 VWGNGYSVVQSFL-----TAPPLLMLIAGIFLCKLLAVLASSGSGAPGGVFTPTLFVGLAIGMLYG----RSLGLWLPDG 347

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1126499250 508 AAVAqpQAYALVGMAATLASVCSVPLTSILLLFELTKDYRIILPLMGAVGLA 559
Cdd:PRK01610  348 EEIT--LLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLLIACVIA 397
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
604-744 1.56e-16

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 76.83  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 604 NLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKtssdASTGDSTIIDVNTCLVS 683
Cdd:COG3448     1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALL----PDRLDELEERLLDLPVE 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126499250 684 TVCTREIryrgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVVkrsggsqkDWKRRVVAIL 744
Cdd:COG3448    77 DVMTRPV---------VTVTPDTPLEEAAELMLEHGIHRLPVV--------DDDGRLVGIV 120
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 612-730 1.84e-16

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: 75.74  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 612 SKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKTSSDAStgDSTIIDVNTclvstvctreir 691
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLAL--DTPVAEVMT------------ 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1126499250 692 yrgqvRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSG 730
Cdd:cd02205    67 -----PDVITVSPDTDLEEALELMLEHGIRRLPVVDDDG 100
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 244-562 7.96e-14

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: 74.61  E-value: 7.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 244 VKAIQAAVTLGTGCSLGPEGPSVDIGKSCAHGFS--------------LMMANNRERMNtLVAAGAAAGISSGFNAPVAG 309
Cdd:cd03685   131 VKIVGVILSVSGGLALGKEGPMIHIGACIAAGLSqggstslrldfrwfRYFRNDRDKRD-FVTCGAAAGVAAAFGAPVGG 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 310 CFFAIETVlrplhAENSPPFTTAMILLASVISSTVSNTLL-------------GTQSAFTVPS-YDLKSAAELPLYLILG 375
Cdd:cd03685   210 VLFSLEEV-----ASFWNQALTWRTFFSSMIVTFTLNFFLsgcnsgkcglfgpGGLIMFDGSStKYLYTYFELIPFMLIG 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 376 MLCGVVSVAFTRLVTWFTKAFEFIKEKFGLHPVacpaLGGLGAGII--ALKYPGILyWGFTNVEEILhtgksasapGIWl 453
Cdd:cd03685   285 VIGGLLGALFNHLNHKVTRFRKRINHKGKLLKV----LEALLVSLVtsVVAFPQTL-LIFFVLYYFL---------ACW- 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 454 ltqlaaakvvaTAlckGSLLVGGLYAPSLMIGAAVGAVFG---GSAAELINsaipgnaavAQPQAYALVGMAATLASVC- 529
Cdd:cd03685   350 -----------TF---GIAVPSGLFIPMILIGAAYGRLVGillGSYFGFTS---------IDPGLYALLGAAAFLGGVMr 406

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1126499250 530 -SVPLTSILLlfELTKDYRIILPLMGAVGLAIWV 562
Cdd:cd03685   407 mTVSLTVILL--ELTNNLTYLPPIMLVLMIAKWV 438
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 605-745 1.85e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 64.71  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 605 LKVSKAMSKNYA--KVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR-LSKTssdastgdstiIDVNTCL 681
Cdd:cd04604     3 LRVSDLMHTGDElpLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRaLEKG-----------LDILNLP 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126499250 682 VSTVCTREIRyrgqvrgllTCYPDTDLAIAKDLMEAKGIKQLPVVkrsggsqkDWKRRVVAILH 745
Cdd:cd04604    72 AKDVMTRNPK---------TISPDALAAEALELMEEHKITVLPVV--------DEDGKPVGILH 118
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 611-744 3.11e-11

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: 60.90  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDI--RRLSKTSsdastgdstiiDVNTCLVSTVCTR 688
Cdd:cd04622     1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLV-GMVTDRDIvvRAVAEGK-----------DPNTTTVREVMTG 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1126499250 689 EIryrgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGgsqkdwkrRVVAIL 744
Cdd:cd04622    69 DV---------VTCSPDDDVEEAARLMAEHQVRRLPVVDDDG--------RLVGIV 107
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 618-758 5.35e-11

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: 60.29  E-value: 5.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 618 VSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI-RRLskTSSDastgdstiIDVNTCLVSTVCTREIryrgqv 696
Cdd:cd17781     7 VPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLaRRV--VASG--------LDPRSTLVSSVMTPNP------ 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126499250 697 rgllTCYPDTDLAI-AKDLMEAKGIKQLPVVKRSGgsqkdwkrRVVAILHydsIWNCLREEIA 758
Cdd:cd17781    71 ----LCVTMDTSATdALDLMVEGKFRHLPVVDDDG--------DVVGVLD---ITKCLYDAIE 118
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 251-542 7.98e-11

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


Pssm-ID: 239654 [Multi-domain]  Cd Length: 378  Bit Score: 64.52  E-value: 7.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 251 VTLGT------GCSLGPEGPSVDIGKSCAHGFS-LMMANNRERMNTLVAAgaaagISSGFNA----PVAGCFFAIE-TVL 318
Cdd:cd03682    81 VLFGTvlthlfGGSAGREGTAVQMGGSLADAFGrVFKLPEEDRRILLIAG-----IAAGFAAvfgtPLAGAIFALEvLVL 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 319 RPLHAEnsppfttAMI--LLASVISSTVSnTLLGTQSAFTVPSYDLKSAAELPLYLILGMLC-GVVSVAFTRLVTWFTKA 395
Cdd:cd03682   156 GRLRYS-------ALIpcLVAAIVADWVS-HALGLEHTHYHIVFIPTLDPLLFVKVILAGIIfGLAGRLFAELLHFLKKL 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 396 FefikEKFGLHPVACPALGGLgaGIIALKYpgilywgftnveeILHTGKSaSAPGIWLLTQLAA----------AKVVAT 465
Cdd:cd03682   228 L----KKRIKNPYLRPFVGGL--LIILLVY-------------LLGSRRY-LGLGTPLIEDSFFggtvypydwlLKLIFT 287

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126499250 466 ALCKGSLLVGGLYAPSLMIGAAVGAVFGGsaaeLINSAIPGNAAvaqpqayalVGMAATLASVCSVPLTSILLLFEL 542
Cdd:cd03682   288 VITLGAGFKGGEVTPLFFIGATLGNALAP----ILGLPVSLLAA---------LGFVAVFAGATNTPLACIIMGIEL 351
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 616-730 2.18e-10

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: 58.61  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 616 AKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR--LSKTSSDAStgdstiidvntclVSTV-CTREIry 692
Cdd:cd04607     5 VLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRglLKGLSLDAP-------------VEEVmNKNPI-- 69

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1126499250 693 rgqvrgllTCYPDTDLAIAKDLMEAKGIKQLPVVKRSG 730
Cdd:cd04607    70 --------TASPSTSREELLALMRAKKILQLPIVDEQG 99
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
603-730 4.35e-10

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 58.39  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 603 ENLKVSKAM-SKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKTSsdastgdstiidvntcL 681
Cdd:COG4109    14 EILLVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDT----------------P 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1126499250 682 VSTVCTREiryrgqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSG 730
Cdd:COG4109    78 IEDVMTKN---------PITVTPDTSLASAAHKMIWEGIELLPVVDDDG 117
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 607-749 1.41e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. 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: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 56.09  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 607 VSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIrrlsktsSDASTGDSTIIDvntclvsTVC 686
Cdd:cd04605     2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDI-------SKAVALKKDSLE-------EIM 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126499250 687 TREIryrgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVVkrsggsqkDWKRRVVAILHYDSI 749
Cdd:cd04605    68 TRNV---------ITARPDEPIELAARKMEKHNISALPVV--------DDDRRVIGIITSDDI 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 607-660 7.27e-09

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: 52.22  E-value: 7.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1126499250 607 VSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRL 660
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 611-726 7.46e-09

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: 54.74  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGD-IRRLSK------------TSSDASTGDSTIIDV 677
Cdd:cd04586     1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDlLRREEPgteprrvwwldaLLESPERLAEEYVKA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1126499250 678 NTCLVSTVCTREIryrgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVV 726
Cdd:cd04586    81 HGRTVGDVMTRPV---------VTVSPDTPLEEAARLMERHRIKRLPVV 120
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 611-731 7.51e-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: 54.07  E-value: 7.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLskTSSDASTgDSTIIDVNTclvstvctrei 690
Cdd:cd09836     1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRA--VAEGIDL-DTPVEEIMT----------- 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1126499250 691 ryrgqvRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGG 731
Cdd:cd09836    67 ------KNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGK 101
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 588-657 1.13e-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: 53.96  E-value: 1.13e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 588 SNDTDGEAINEDLLAENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDI 657
Cdd:cd04584    57 SKATSLSIYELNYLLSKIPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLV-GIITETDI 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 598-659 1.33e-08

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: 53.40  E-value: 1.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126499250 598 EDLLAENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR 659
Cdd:cd02205    52 EGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
594-659 1.69e-08

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 55.27  E-value: 1.69e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126499250 594 EAINEDLLAENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR 659
Cdd:COG2524   139 KALAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 613-726 1.10e-07

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: 50.59  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 613 KNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKTSSdastgdstiidvntcLVSTVCTREIry 692
Cdd:cd04583     2 TNPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNYRKAK---------------KVGEIMERDV-- 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1126499250 693 rgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVV 726
Cdd:cd04583    65 -------FTVKEDSLLRDTVDRILKRGLKYVPVV 91
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
602-667 1.29e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 51.40  E-value: 1.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126499250 602 AENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI-RRLSKTSSDA 667
Cdd:COG3448    70 LLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLlRALARLLEEE 136
CBS COG0517
CBS domain [Signal transduction mechanisms];
604-659 1.79e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 50.63  E-value: 1.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1126499250 604 NLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR 659
Cdd:COG0517    66 DTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLK 121
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 606-730 4.33e-07

CBS pair domains found in archeal proteins, repeat 2; 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: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 49.64  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 606 KVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIrrLSKTSSDASTGDSTIIDVNTCLVSTV 685
Cdd:cd17778     1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLV-GIVTAMDI--VKYFGSHEAKKRLTTGDIDEAYSTPV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1126499250 686 ctREIRYRGqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSG 730
Cdd:cd17778    78 --EEIMSKE----VVTIEPDADIAEAARLMIKKNVGSLLVVDDEG 116
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 606-726 1.05e-06

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 48.57  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 606 KVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIRRLSktSSDASTGDSTIIDVntcLVSTV 685
Cdd:cd04584     1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLV-GIVTDRDLLRAS--PSKATSLSIYELNY---LLSKI 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1126499250 686 CTREIryrgQVRGLLTCYPDTDLAIAKDLMEAKGIKQLPVV 726
Cdd:cd04584    75 PVKDI----MTKDVITVSPDDTVEEAALLMLENKIGCLPVV 111
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 621-744 1.23e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in 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 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: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 47.96  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 621 SLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLSKtssdastgdstiidvNTCLVSTVCTREIryrgQVRGLL 700
Cdd:cd04613    11 GMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLF---------------EEELWDLVVVKDL----ATTDVI 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1126499250 701 TCYPDTDLAIAKDLMEAKGIKQLPVVKRsggsqkDWKRRVVAIL 744
Cdd:cd04613    72 TVTPDDDLYTALLKFTSTNLDQLPVVDD------DDPGKVLGML 109
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 611-727 2.76e-06

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


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 46.79  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIRRLSKTSSDASTgdstiidvntclVSTVCTREi 690
Cdd:cd04801     3 MTPEVVTVTPEMTVSELLDRMFEEKHLGYPVVENGRLV-GIVTLEDIRKVPEVEREATR------------VRDVMTKD- 68

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1126499250 691 ryrgqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVK 727
Cdd:cd04801    69 --------VITVSPDADAMEALKLMSQNNIGRLPVVE 97
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 606-729 3.29e-06

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: 46.84  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 606 KVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIRRL---SKTSSDASTGDstIIDVNTCLV 682
Cdd:cd04631     1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLV-GIVTSTDIMRYlgsGEAFEKLKTGN--IHEVLNVPI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1126499250 683 STVCTREIRyrgqvrgllTCYPDTDLAIAKDLMEAKGIKQLPVVKRS 729
Cdd:cd04631    78 SSIMKRDII---------TTTPDTDLGEAAELMLEKNIGALPVVDDG 115
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 618-726 4.88e-06

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: 45.87  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 618 VSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI-RRLSKTSSDAStgdstiidvnTCLVSTVCTREiryrgqv 696
Cdd:cd04623     7 VSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYvRKLALRGASSL----------DTPVSEIMTRD------- 69

                          90       100       110
                  ....*....|....*....|....*....|
gi 1126499250 697 rgLLTCYPDTDLAIAKDLMEAKGIKQLPVV 726
Cdd:cd04623    70 --VVTCTPDDTVEECMALMTERRIRHLPVV 97
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 618-726 6.05e-06

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: 45.87  E-value: 6.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 618 VSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRrlskTSSDASTgdstiidvntcLVSTVCTREIRyrgqvr 697
Cdd:cd04601     7 LSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIR----FETDLST-----------PVSEVMTPDER------ 65

                          90       100
                  ....*....|....*....|....*....
gi 1126499250 698 gLLTCYPDTDLAIAKDLMEAKGIKQLPVV 726
Cdd:cd04601    66 -LVTAPEGITLEEAKEILHKHKIEKLPIV 93
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
598-657 6.40e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 46.44  E-value: 6.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126499250 598 EDLLA--ENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI 657
Cdd:COG4109    67 KDILGkdDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 595-660 1.25e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 45.21  E-value: 1.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126499250 595 AINEDLLAENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIRRL 660
Cdd:COG2905    55 VLAEGLDPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLV-GIVSITDLLRA 119
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 591-659 2.09e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 44.68  E-value: 2.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126499250 591 TDGE---AINEDLLAENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR 659
Cdd:cd04604    53 TDGDlrrALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHDLLR 124
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 607-731 2.38e-05

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


Pssm-ID: 341384 [Multi-domain]  Cd Length: 131  Bit Score: 44.63  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 607 VSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDI-RRLSKTSSDASTGDstiidvntcLVStv 685
Cdd:cd04611     7 VGSAMNRSPLVLPGDASLAEAARRMRSHRADAAVIECPDGGL-GILTERDLvRFIARHPGNTPVGE---------LAS-- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1126499250 686 ctreiryrgqvRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGG 731
Cdd:cd04611    75 -----------RPLLTVGAEDSLIHARDLLIDHRIRHLAVVDEDGQ 109
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 ...
 611-729 2.73e-05

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: 43.95  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIR-RLSKTSSDASTgdstiidvntcLVSTVCTRE 689
Cdd:cd04587     2 MSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLV-GIVTDRDLRnRVVAEGLDPDT-----------PVSEIMTPP 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1126499250 690 iryrgqvrgLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRS 729
Cdd:cd04587    70 ---------PVTIDADALVFEALLLMLERNIHHLPVVDDG 100
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 611-750 4.45e-05

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: 43.30  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI-RRLSKTSSDAStgDSTIIDVNTclvstvctre 689
Cdd:cd17775     1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIvVEVVAKGLDPK--DVTVGDIMS---------- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126499250 690 iryrgqvRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGgsqkdwkrRVVAILHYDSIW 750
Cdd:cd17775    69 -------ADLITAREDDGLFEALERMREKGVRRLPVVDDDG--------ELVGIVTLDDIL 114
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 593-657 4.87e-05

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: 43.29  E-value: 4.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126499250 593 GEAINEDLlaENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI 657
Cdd:cd04588    46 AKALAEGK--ENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDI 108
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 611-727 6.39e-05

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: 42.81  E-value: 6.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGD-IRRLSKTSSDASTGDstiidvntcLVSTVCTRE 689
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDcLKALLEASYHCEPGG---------TVADYMSTE 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1126499250 690 IryrgqvrglLTCYPDTD-LAIAKDLMEAKgIKQLPVVK 727
Cdd:cd04629    72 V---------LTVSPDTSiVDLAQLFLKNK-PRRYPVVE 100
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 611-729 8.82e-05

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: 42.33  E-value: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIRRLSktssdastgdstiidVNTcLVSTVCTREI 690
Cdd:cd04599     1 MTRNPITISPLDSVARAAALMERQRIGGLPVVENGKLV-GIITSRDVRRAH---------------PNR-LVADAMSRNV 63

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1126499250 691 ryrgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVVKRS 729
Cdd:cd04599    64 ---------VTISPEASLWEAKELMEEHGIERLVVVEEG 93
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 606-662 9.15e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; 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: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 42.79  E-value: 9.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126499250 606 KVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQ-----NCLLVVDDEDLLeGILTYGDIRRLSK 662
Cdd:cd17784    60 TVEEVMVKDVATVHPDETLLEAIKKMDSNAPdeeiiNQLPVVDDGKLV-GIISDGDIIRAIK 120
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 598-659 1.18e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in 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: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 42.01  E-value: 1.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126499250 598 EDLLAEnLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDlLEGILTYGDIRR 659
Cdd:cd17776    54 DDPFSE-IPVRAVASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLD-LVGILTATDIIR 113
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 607-726 2.48e-04

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: 341393 [Multi-domain]  Cd Length: 120  Bit Score: 41.43  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 607 VSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVD-DEDLLEGILTYGDIRRlsktSSDASTGDstiID-VNtclVST 684
Cdd:cd04630     1 VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVEKrHEHDAYGIVTYTDILK----KVIAEDRD---PDlVN---VYE 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1126499250 685 VCTREIryrgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVV 726
Cdd:cd04630    71 IMTKPA---------ISVSPDLDIKYAARLMARFNLKRAPVI 103
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 604-657 3.07e-04

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: 43.92  E-value: 3.07e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1126499250 604 NLKVSKAMSK-NYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI 657
Cdd:pfam00478 138 SQPVSEVMTKeNLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 603-659 4.33e-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: 40.47  E-value: 4.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1126499250 603 ENLKVSKAMSKNYAKV--SLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRR 659
Cdd:cd04601    52 LSTPVSEVMTPDERLVtaPEGITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK 110
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 594-653 5.79e-04

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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 40.56  E-value: 5.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 594 EAINEDLLaENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDskQNCLLVVDDEDLLEGILT 653
Cdd:cd04643    59 ERIEFEKL-SELKVEEVMNTDVPTVSPDDDLEEVLHLLVD--HPFLCVVDEDGYFLGIIT 115
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 618-734 8.51e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; 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: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 39.78  E-value: 8.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 618 VSLSLTLKEAIK--YMHDSkqNCLLVVDDEDLLEGILTYGDIRRlsktssdASTGDStiiDVNTCLVSTVCTReiryrgq 695
Cdd:cd04617     9 VDETTSVYDAIVtlFLEDV--GSLFVVDEEGYLVGVVSRKDLLK-------ATLGGQ---DLEKTPVSMIMTR------- 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1126499250 696 VRGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGGSQK 734
Cdd:cd04617    70 MPNIVTVTPDDSVLEAARKLIEHEIDSLPVVEKEDGKLK 108
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 618-730 9.52e-04

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: 42.38  E-value: 9.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 618 VSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLeGILTYGDIRrlsktssdastgdstIIDVNTCLVSTVCTREiryrgqvr 697
Cdd:pfam00478  93 LSPDATVADALALMERYGISGVPVVDDGKLV-GIVTNRDLR---------------FETDLSQPVSEVMTKE-------- 148

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1126499250 698 GLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSG 730
Cdd:pfam00478 149 NLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNG 181
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 618-750 1.65e-03

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


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 39.44  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 618 VSLSLTLKEAIKYM----------------HDSKQNCLLVVDDEDLLeGILTYGDIRRLskTSSDASTGDSTIIDVNTcl 681
Cdd:cd04620    12 VSPDTPVIEAIALMsqtrssccllsedsiiTEARSSCVLVVENQQLV-GIFTERDVVRL--TASGIDLSGVTIAEVMT-- 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126499250 682 vSTVCTreiryrgqvrglLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGgsqkdwkrRVVAILHYDSIW 750
Cdd:cd04620    87 -QPVIT------------LKESEFQDIFTVLSLLRQHQIRHLPIVDDQG--------QLVGLITPESLR 134
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 618-657 1.94e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 36.72  E-value: 1.94e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1126499250  618 VSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI 657
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 594-661 2.22e-03

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: 38.68  E-value: 2.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126499250 594 EAINEDLLAENLKVSKAMSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDIRRLS 661
Cdd:cd17775    50 EVVAKGLDPKDVTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
MFS_NIMT_like cd17409
2-nitroimidazole transporter and similar proteins of the Major Facilitator Superfamily of ...
 474-584 2.61e-03

2-nitroimidazole transporter and similar proteins of the Major Facilitator Superfamily of transporters; This subfamily is composed of Escherichia coli 2-nitroimidazole transporter (NIMT), also called YeaN, and similar proteins. NIMT confers resistance to 2-nitroimidazole, the antibacterial and antifungal antibiotic, by mediating the active efflux of this compound. The NIMT-like subfamily belongs to the 2-nitroimidazole and cyanate transporters like (NIMT/CynX-like) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340967 [Multi-domain]  Cd Length: 374  Bit Score: 40.71  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 474 VGGLYAPSLMIGA--AVGAVFGGSaaeLINSAIPGNAAVAQpQAYALV-GMAATLASVCSVPLTSI--------LLLFel 542
Cdd:cd17409    86 VWALYLGTAIIGAgiAIGNVLLPS---LLKRDFPARVATLT-GAYALTmGVGAALGSALVVPLAQVlafgwqlaLGAF-- 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1126499250 543 tkdyrIILPLmgaVGLAIWVPSVADHGKENERpGAHSLARGY 584
Cdd:cd17409   160 -----LVFPL---VAALIWLPQLRRHTSPAAD-TAKPPHGGS 192
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 616-687 3.21e-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: 38.00  E-value: 3.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126499250 616 AKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDLLEGILTYGDI--RRLSKTssdastgdstiIDVNTCLVSTVCT 687
Cdd:cd17782     5 PLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVvlRVLAAG-----------LDPATTSVVRVMT 67
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
611-756 4.76e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 40.05  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQ-----NCLLVVDDEDLLEGILTygdIRRLSKTSSDAstgdstiidvntcLVSTV 685
Cdd:COG2239   135 MTTEFVAVREDWTVGEALRYLRRQAEdpetiYYIYVVDDDGRLVGVVS---LRDLLLADPDT-------------KVSDI 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1126499250 686 CTREIRYrgqVRglltcyPDTDLAIAKDLMEAKGIKQLPVVkrsggsqkDWKRRVVAILHYDSIWNCLREE 756
Cdd:COG2239   199 MDTDVIS---VP------ADDDQEEVARLFERYDLLALPVV--------DEEGRLVGIITVDDVVDVIEEE 252
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 697-749 7.65e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 35.27  E-value: 7.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126499250 697 RGLLTCYPDTDLAIAKDLMEAKGIKQLPVVKRSGgsqkdwkrRVVAILHYDSI 749
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDG--------KLVGIVTLKDL 51
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 611-659 9.49e-03

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: 36.55  E-value: 9.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1126499250 611 MSKNYAKVSLSLTLKEAIKYMHDSKQNCLLVVDDEDlLEGILTYGDIRR 659
Cdd:cd04638    61 MSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDK-LVGIVTVADLVR 108
 
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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