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Conserved domains on  [gi|334187188|ref|NP_001190924|]
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chloride channel E [Arabidopsis thaliana]

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
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 ...
84-494 2.32e-93

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: 296.01  E-value: 2.32e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  84 GVLTGVSVVLFNNCVHLLRDFSWDGIPDRGASWlreapiGSNWLRVILVPTIGGLVV-SILNQLRESAGKSTGDSHSSLD 162
Cdd:cd00400    1 GVLSGLGAVLFRLLIELLQNLLFGGLPGELAAG------SLSPLYILLVPVIGGLLVgLLVRLLGPARGHGIPEVIEAIA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 163 RVKAVLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGISSGFNAAVAGCF 239
Cdd:cd00400   75 LGGGRLPLrvaLVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAAGIAAAFNAPLAGAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 240 FAVESVLWPSSSTdsstslpnTTSMVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLLLGALCGLVSLALSRC 319
Cdd:cd00400  155 FAIEVLLGEYSVA--------SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 320 TSSMTSAVDSLNkdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLekrpfVKGLSADLLLQLVAVKIAATAWC 399
Cdd:cd00400  227 LYKIERLFRRLP----IPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLLLLLLLLLKLLATALT 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 400 RASGLVGGYYAPSLFIGGAAGMAYGKFIGLalaqnpdfnLSILEVASPQAYGLVGMAATLAGVCQVPLTAVLLLFELTQD 479
Cdd:cd00400  298 LGSGFPGGVFAPSLFIGAALGAAFGLLLPA---------LFPGLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGD 368
                        410
                 ....*....|....*
gi 334187188 480 YRIVLPLLGAVGMSS 494
Cdd:cd00400  369 YSLLLPLMLAVVIAY 383
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
565-692 3.71e-66

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: 214.92  E-value: 3.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARKEGNNRPKDIFVNDICSRSGGKCKVP 644
Cdd:cd04592    1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPKTILVSSICTRNGGYCRGL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334187188 645 WTVTPDMDLLAAQTIMNKHELSHVAVVSGSIDAPRIHPVGVLDRECIT 692
Cdd:cd04592   81 WTCTPDMDLLTAKMLMEARGINQLPVVKRGGEERRRRVVGLLDRDSID 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 ...
84-494 2.32e-93

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: 296.01  E-value: 2.32e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  84 GVLTGVSVVLFNNCVHLLRDFSWDGIPDRGASWlreapiGSNWLRVILVPTIGGLVV-SILNQLRESAGKSTGDSHSSLD 162
Cdd:cd00400    1 GVLSGLGAVLFRLLIELLQNLLFGGLPGELAAG------SLSPLYILLVPVIGGLLVgLLVRLLGPARGHGIPEVIEAIA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 163 RVKAVLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGISSGFNAAVAGCF 239
Cdd:cd00400   75 LGGGRLPLrvaLVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAAGIAAAFNAPLAGAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 240 FAVESVLWPSSSTdsstslpnTTSMVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLLLGALCGLVSLALSRC 319
Cdd:cd00400  155 FAIEVLLGEYSVA--------SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 320 TSSMTSAVDSLNkdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLekrpfVKGLSADLLLQLVAVKIAATAWC 399
Cdd:cd00400  227 LYKIERLFRRLP----IPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLLLLLLLLLKLLATALT 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 400 RASGLVGGYYAPSLFIGGAAGMAYGKFIGLalaqnpdfnLSILEVASPQAYGLVGMAATLAGVCQVPLTAVLLLFELTQD 479
Cdd:cd00400  298 LGSGFPGGVFAPSLFIGAALGAAFGLLLPA---------LFPGLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGD 368
                        410
                 ....*....|....*
gi 334187188 480 YRIVLPLLGAVGMSS 494
Cdd:cd00400  369 YSLLLPLMLAVVIAY 383
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
70-497 2.24e-79

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 260.46  E-value: 2.24e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  70 QPSQELAIASACLVGVLTGVSVVLFNNCVHLLRDFSWDGIPDRGASWLReapigsnWLRVILVPTIGGLVVSILNQL--R 147
Cdd:COG0038    1 RRRLLRLLLLAVLVGILAGLAAVLFRLLLELATHLFLGGLLSAAGSHLP-------PWLVLLLPPLGGLLVGLLVRRfaP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 148 ESAGKSTGDSHSSLDRVKAVLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSA 224
Cdd:COG0038   74 EARGSGIPQVIEAIHLKGGRIPLrvaPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLSPEDRRILLAAGAA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 225 AGISSGFNAAVAGCFFAVESVLwpsSSTDSSTSLPnttsmVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLL 304
Cdd:COG0038  154 AGLAAAFNAPLAGALFALEVLL---RDFSYRALIP-----VLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 305 LGALCGLVSLALSRCTSSMTSAVDSLNkdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLEkrpfvKGLSADL 384
Cdd:COG0038  226 LGILAGLVGVLFNRLLLKVERLFKRLK----LPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLN-----GELSLLL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 385 LLQLVAVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLalaqnpdfnLSILEVASPQAYGLVGMAATLAGVCQ 464
Cdd:COG0038  297 LLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNL---------LFPGLGLSPGLFALVGMAAVFAAVTR 367
                        410       420       430
                 ....*....|....*....|....*....|...
gi 334187188 465 VPLTAVLLLFELTQDYRIVLPLLGAVGMSSWIT 497
Cdd:COG0038  368 APLTAILLVLEMTGSYSLLLPLMIACVIAYLVS 400
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
136-498 1.41e-70

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: 234.36  E-value: 1.41e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  136 GGLVVSILNQL--RESAGKSTGDSHSSLDRVKAVLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNK 210
Cdd:pfam00654   1 GGLLAGWLVKRfaPEAAGSGIPEVKAALHGGRGPLPLrvlPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  211 -SPQTGFSLLAAGSAAGISSGFNAAVAGCFFAVESVLwpssstdsSTSLPNTTSMVILSAVTASVVSEIGLGSEPAFKVP 289
Cdd:pfam00654  81 lSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELS--------RSFSLRALIPVLLASVVAALVSRLIFGNSPLFSVG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  290 DYDFRSPGELPLYLLLGALCGLVSLALSRCTSSMTSAVDSLNKdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDI 369
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLK---IPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  370 LLEKRpfvkgLSADLLLQLVAVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLalaqnpdfnLSILEVASPQA 449
Cdd:pfam00654 230 LFNGN-----TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLAL---------LFPIGGLPPGA 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 334187188  450 YGLVGMAATLAGVCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSWITS 498
Cdd:pfam00654 296 FALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVSR 344
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
565-692 3.71e-66

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: 214.92  E-value: 3.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARKEGNNRPKDIFVNDICSRSGGKCKVP 644
Cdd:cd04592    1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPKTILVSSICTRNGGYCRGL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334187188 645 WTVTPDMDLLAAQTIMNKHELSHVAVVSGSIDAPRIHPVGVLDRECIT 692
Cdd:cd04592   81 WTCTPDMDLLTAKMLMEARGINQLPVVKRGGEERRRRVVGLLDRDSID 128
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
73-671 3.77e-43

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 164.92  E-value: 3.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  73 QELAIASACLVGVLTGVSVVLFNNCVHLLRDFswdgIPDRGASWLREAPIGSNWLRViLVPTIGGLVVSILNQL--RESA 150
Cdd:PRK01862  21 AHTMLIWSAIVGIGGAFATTAFREGIELIQHL----ISGHSGSFVEMAKSLPWYVRV-WLPAAGGFLAGCVLLLanRGAR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 151 GKSTGDSHSSL---DRVKAVLRPFLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGI 227
Cdd:PRK01862  96 KGGKTDYMEAValgDGVVPVRQSLWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 228 SSGFNAAVAGCFFAVESVLwpssstdsstslpNTTSM-----VILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLY 302
Cdd:PRK01862 176 TSAYNAPIAGAFFVAEIVL-------------GSIAMesfgpLVVASVVANIVMREFAGYQPPYEMPVFPAVTGWEVLLF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 303 LLLGALCGLVSLALSRctssMTSAVDSLNKDAGIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLEKRPfvkgLSA 382
Cdd:PRK01862 243 VALGVLCGAAAPQFLR----LLDASKNQFKRLPVPLPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILHAPW----TWQ 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 383 DLLLQLVAvKIAATAWCRASGLVGGYYAPSLFIGGAAGmaygKFIGLAL-AQNPDfnlsilEVASPQAYGLVGMAATLAG 461
Cdd:PRK01862 315 ALVAVLVA-KLIATAATAGSGAVGGVFTPTLFVGAVVG----SLFGLAMhALWPG------HTSAPFAYAMVGMGAFLAG 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 462 VCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSWITSGQSKRQETRETKEtRKRKSQEAVQSLTSSddesstnnlceves 541
Cdd:PRK01862 384 ATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLR-RHQDEAERERLRTTQ-------------- 448
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 542 slclddslnqseelpksifVSEAMRTRFATVMMSTSLEEAlTRMLIEKQSCAL-IVDPDNIFLGILTLSDIQEFSKARKE 620
Cdd:PRK01862 449 -------------------MRELIQPAQTVVPPTASVADM-TRVFLEYPVKYLyVVDDDGRFRGAVALKDITSDLLDKRD 508
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 621 GNNRPkdifVNDICSRSggkckVPwTVTPDMDLLAAQTIMNKHELSHVAVV 671
Cdd:PRK01862 509 TTDKT----AADYAHTP-----FP-LLTPDMPLGDALEHFMAFQGERLPVV 549
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
551-689 2.33e-17

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 81.08  E-value: 2.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 551 QSEELPKSIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDpDNIFLGILTLSDIQEFSKARKEGNNRPkdifV 630
Cdd:COG2524   78 KELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGRDLLDAP----V 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334187188 631 NDICSRSggkckvPWTVTPDMDLLAAQTIMNKHELSHVAVVsgsiDAPRiHPVGVLDRE 689
Cdd:COG2524  153 SDIMTRD------VVTVSEDDSLEEALRLMLEHGIGRLPVV----DDDG-KLVGIITRT 200
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
561-611 8.26e-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: 8.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 334187188  561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
568-611 1.57e-05

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: 42.50  E-value: 1.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 334187188   568 RFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
555-611 2.08e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.36  E-value: 2.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187188 555 LPKSIFVSEAMRTR-FATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:PRK14869 242 INQSIPVSYIMTTEdLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHL 299
 
Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
84-494 2.32e-93

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: 296.01  E-value: 2.32e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  84 GVLTGVSVVLFNNCVHLLRDFSWDGIPDRGASWlreapiGSNWLRVILVPTIGGLVV-SILNQLRESAGKSTGDSHSSLD 162
Cdd:cd00400    1 GVLSGLGAVLFRLLIELLQNLLFGGLPGELAAG------SLSPLYILLVPVIGGLLVgLLVRLLGPARGHGIPEVIEAIA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 163 RVKAVLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGISSGFNAAVAGCF 239
Cdd:cd00400   75 LGGGRLPLrvaLVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVACGAAAGIAAAFNAPLAGAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 240 FAVESVLWPSSSTdsstslpnTTSMVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLLLGALCGLVSLALSRC 319
Cdd:cd00400  155 FAIEVLLGEYSVA--------SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 320 TSSMTSAVDSLNkdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLekrpfVKGLSADLLLQLVAVKIAATAWC 399
Cdd:cd00400  227 LYKIERLFRRLP----IPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLLLLLLLLLKLLATALT 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 400 RASGLVGGYYAPSLFIGGAAGMAYGKFIGLalaqnpdfnLSILEVASPQAYGLVGMAATLAGVCQVPLTAVLLLFELTQD 479
Cdd:cd00400  298 LGSGFPGGVFAPSLFIGAALGAAFGLLLPA---------LFPGLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGD 368
                        410
                 ....*....|....*
gi 334187188 480 YRIVLPLLGAVGMSS 494
Cdd:cd00400  369 YSLLLPLMLAVVIAY 383
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
70-497 2.24e-79

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 260.46  E-value: 2.24e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  70 QPSQELAIASACLVGVLTGVSVVLFNNCVHLLRDFSWDGIPDRGASWLReapigsnWLRVILVPTIGGLVVSILNQL--R 147
Cdd:COG0038    1 RRRLLRLLLLAVLVGILAGLAAVLFRLLLELATHLFLGGLLSAAGSHLP-------PWLVLLLPPLGGLLVGLLVRRfaP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 148 ESAGKSTGDSHSSLDRVKAVLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSA 224
Cdd:COG0038   74 EARGSGIPQVIEAIHLKGGRIPLrvaPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGRLLRLSPEDRRILLAAGAA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 225 AGISSGFNAAVAGCFFAVESVLwpsSSTDSSTSLPnttsmVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLL 304
Cdd:COG0038  154 AGLAAAFNAPLAGALFALEVLL---RDFSYRALIP-----VLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 305 LGALCGLVSLALSRCTSSMTSAVDSLNkdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLEkrpfvKGLSADL 384
Cdd:COG0038  226 LGILAGLVGVLFNRLLLKVERLFKRLK----LPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLN-----GELSLLL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 385 LLQLVAVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLalaqnpdfnLSILEVASPQAYGLVGMAATLAGVCQ 464
Cdd:COG0038  297 LLLLLLLKLLATALTLGSGGPGGIFAPSLFIGALLGAAFGLLLNL---------LFPGLGLSPGLFALVGMAAVFAAVTR 367
                        410       420       430
                 ....*....|....*....|....*....|...
gi 334187188 465 VPLTAVLLLFELTQDYRIVLPLLGAVGMSSWIT 497
Cdd:COG0038  368 APLTAILLVLEMTGSYSLLLPLMIACVIAYLVS 400
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
136-498 1.41e-70

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: 234.36  E-value: 1.41e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  136 GGLVVSILNQL--RESAGKSTGDSHSSLDRVKAVLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNK 210
Cdd:pfam00654   1 GGLLAGWLVKRfaPEAAGSGIPEVKAALHGGRGPLPLrvlPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRLFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  211 -SPQTGFSLLAAGSAAGISSGFNAAVAGCFFAVESVLwpssstdsSTSLPNTTSMVILSAVTASVVSEIGLGSEPAFKVP 289
Cdd:pfam00654  81 lSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELS--------RSFSLRALIPVLLASVVAALVSRLIFGNSPLFSVG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  290 DYDFRSPGELPLYLLLGALCGLVSLALSRCTSSMTSAVDSLNKdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDI 369
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLK---IPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  370 LLEKRpfvkgLSADLLLQLVAVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLalaqnpdfnLSILEVASPQA 449
Cdd:pfam00654 230 LFNGN-----TSLSLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLAL---------LFPIGGLPPGA 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 334187188  450 YGLVGMAATLAGVCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSWITS 498
Cdd:pfam00654 296 FALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVSR 344
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
565-692 3.71e-66

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: 214.92  E-value: 3.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARKEGNNRPKDIFVNDICSRSGGKCKVP 644
Cdd:cd04592    1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPKTILVSSICTRNGGYCRGL 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334187188 645 WTVTPDMDLLAAQTIMNKHELSHVAVVSGSIDAPRIHPVGVLDRECIT 692
Cdd:cd04592   81 WTCTPDMDLLTAKMLMEARGINQLPVVKRGGEERRRRVVGLLDRDSID 128
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
83-498 4.83e-51

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: 183.13  E-value: 4.83e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  83 VGVLTGVSVVLFNNCVHLLRDFSwdgipDRGASWLREAPIGsnWLRVILVPTIGGLVVSILNQLRESAGKSTGDSHssld 162
Cdd:cd01031    1 IGLLAGLVAVLFRLGIDKLGNLR-----LSLYDFAANNPPL--LLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQ---- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 163 rVKAVLRPFL----------KTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGISSGFN 232
Cdd:cd01031   70 -VEGVLAGLLppnwwrvlpvKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSKWFKTSPEERRQLIAAGAAAGLAAAFN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 233 AAVAGCFFAVESVLwpssstdsSTSLPNTTSMVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLLLGALCGLV 312
Cdd:cd01031  149 APLAGVLFVLEELR--------HSFSPLALLTALVASIAADFVSRLFFGLGPVLSIPPLPALPLKSYWLLLLLGIIAGLL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 313 SLALSRCTSSMTSAVDSLNKdagIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLEKRPFVKglsadLLLQLVAVK 392
Cdd:cd01031  221 GYLFNRSLLKSQDLYRKLKK---LPRELRVLLPGLLIGPLGLLLPEALGGGHGLILSLAGGNFSIS-----LLLLIFVLR 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 393 IAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLALAQNPDFnlsilevasPQAYGLVGMAATLAGVCQVPLTAVLL 472
Cdd:cd01031  293 FIFTMLSYGSGAPGGIFAPMLALGALLGLLFGTILVQLGPIPISA---------PATFAIAGMAAFFAAVVRAPITAIIL 363
                        410       420
                 ....*....|....*....|....*.
gi 334187188 473 LFELTQDYRIVLPLLgAVGMSSWITS 498
Cdd:cd01031  364 VTEMTGNFNLLLPLM-VVCLVAYLVA 388
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
73-671 3.77e-43

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 164.92  E-value: 3.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  73 QELAIASACLVGVLTGVSVVLFNNCVHLLRDFswdgIPDRGASWLREAPIGSNWLRViLVPTIGGLVVSILNQL--RESA 150
Cdd:PRK01862  21 AHTMLIWSAIVGIGGAFATTAFREGIELIQHL----ISGHSGSFVEMAKSLPWYVRV-WLPAAGGFLAGCVLLLanRGAR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 151 GKSTGDSHSSL---DRVKAVLRPFLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGI 227
Cdd:PRK01862  96 KGGKTDYMEAValgDGVVPVRQSLWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 228 SSGFNAAVAGCFFAVESVLwpssstdsstslpNTTSM-----VILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLY 302
Cdd:PRK01862 176 TSAYNAPIAGAFFVAEIVL-------------GSIAMesfgpLVVASVVANIVMREFAGYQPPYEMPVFPAVTGWEVLLF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 303 LLLGALCGLVSLALSRctssMTSAVDSLNKDAGIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDILLEKRPfvkgLSA 382
Cdd:PRK01862 243 VALGVLCGAAAPQFLR----LLDASKNQFKRLPVPLPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILHAPW----TWQ 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 383 DLLLQLVAvKIAATAWCRASGLVGGYYAPSLFIGGAAGmaygKFIGLAL-AQNPDfnlsilEVASPQAYGLVGMAATLAG 461
Cdd:PRK01862 315 ALVAVLVA-KLIATAATAGSGAVGGVFTPTLFVGAVVG----SLFGLAMhALWPG------HTSAPFAYAMVGMGAFLAG 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 462 VCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSWITSGQSKRQETRETKEtRKRKSQEAVQSLTSSddesstnnlceves 541
Cdd:PRK01862 384 ATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLR-RHQDEAERERLRTTQ-------------- 448
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 542 slclddslnqseelpksifVSEAMRTRFATVMMSTSLEEAlTRMLIEKQSCAL-IVDPDNIFLGILTLSDIQEFSKARKE 620
Cdd:PRK01862 449 -------------------MRELIQPAQTVVPPTASVADM-TRVFLEYPVKYLyVVDDDGRFRGAVALKDITSDLLDKRD 508
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 621 GNNRPkdifVNDICSRSggkckVPwTVTPDMDLLAAQTIMNKHELSHVAVV 671
Cdd:PRK01862 509 TTDKT----AADYAHTP-----FP-LLTPDMPLGDALEHFMAFQGERLPVV 549
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
80-487 8.45e-37

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 143.88  E-value: 8.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  80 ACLVGVLTGVSVVLFNNCVHLLrdFSWDgipdrgASWLREAPiGSNWLRVILVPTIGGLVVSILNQL-----RESAGkst 154
Cdd:PRK05277   4 AAVVGTLTGLVGVAFELAVDWV--QNQR------LGLLASVA-DNGLLLWIVAFLISAVLAMIGYFLvrrfaPEAGG--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 155 gdshSSLDRVKAVL---RPF-------LKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFN-KSPQTGFSLLAAGS 223
Cdd:PRK05277  72 ----SGIPEIEGALeglRPVrwwrvlpVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVLDIFRlRSDEARHTLLAAGA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 224 AAGISSGFNAAVAGCFFAVESvLWPSSSTdsstslpNTTS--MVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPL 301
Cdd:PRK05277 148 AAGLAAAFNAPLAGILFVIEE-MRPQFRY-------SLISikAVFIGVIMATIVFRLFNGEQAVIEVGKFSAPPLNTLWL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 302 YLLLGALCGLVSLALSRCtssMTSAVDSLNKDAGIPKAVFPVMG---GLSVGIIALVYPEVLYWGFQNVDILLEkrpfvK 378
Cdd:PRK05277 220 FLLLGIIFGIFGVLFNKL---LLRTQDLFDRLHGGNKKRWVLMGgavGGLCGLLGLLAPAAVGGGFNLIPIALA-----G 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 379 GLSADLLLQLVAVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYgkfiGLALAQ-NPDFNLsilevaSPQAYGLVGMAA 457
Cdd:PRK05277 292 NFSIGMLLFIFVARFITTLLCFGSGAPGGIFAPMLALGTLLGLAF----GMVAAAlFPQYHI------EPGTFAIAGMGA 361
                        410       420       430
                 ....*....|....*....|....*....|
gi 334187188 458 TLAGVCQVPLTAVLLLFELTQDYRIVLPLL 487
Cdd:PRK05277 362 LFAATVRAPLTGIVLVLEMTDNYQLILPLI 391
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
84-496 1.60e-27

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: 115.47  E-value: 1.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  84 GVLTGVSVVLFNNCVHLLRDFSWDGipDRGASwlREAPIGSNWLRVILVPTIGGLVVSILNQLRESAGKSTGDSHSSLDR 163
Cdd:cd01033    1 GVGAGLGGGLLTLLLHGVQHLAFGY--SEGSF--LTGVAAVSPIRRALSLTVGGLIAGLGWYLLRRKGKKLVSIKQAVRG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 164 VKAVlrPFLKTVAACV----TLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGISSGFNAAVAGCF 239
Cdd:cd01033   77 KKRM--PFWETIIHAVlqivTVGLGAPLGREVAPREVGALLAQRFSDWLGLTVADRRLLVACAAGAGLAAVYNVPLAGAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 240 FAVESVLWPSsstdsstslpNTTSMVI--LSAVTASVVSEIGLGSEPAFKVPDYDFrSPGELPLYLLLGALCGLVSLALS 317
Cdd:cd01033  155 FALEILLRTI----------SLRSVVAalATSAIAAAVASLLKGDHPIYDIPPMQL-STPLLIWALLAGPVLGVVAAGFR 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 318 RCTSSMTSAVdslNKDAGIPKAVfpVMGGLSVGIIALVYPEVLywGFQNVDILLEkrpFVKGLSADLLLQLVAVKIAATA 397
Cdd:cd01033  224 RLSQAARAKR---PKGKRILWQM--PLAFLVIGLLSIFFPQIL--GNGRALAQLA---FSTTLTLSLLLILLVLKIVATL 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 398 WCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLALAQnpdfnlsilevASPQAYGLVGMAATLAGVCQVPLTAVLLLFELT 477
Cdd:cd01033  294 LALRAGAYGGLLTPSLALGALLGALLGIVWNALLPP-----------LSIAAFALIGAAAFLAATQKAPLTALILVLEFT 362
                        410       420
                 ....*....|....*....|....
gi 334187188 478 -QDYRIVLPL----LGAVGMSSWI 496
Cdd:cd01033  363 rQNPLFLIPLmlavAGAVAVSRFI 386
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
111-496 5.87e-26

ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, are putative halogen ion (Cl-, Br- and I-) transport proteins found in eubacteria. They belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. This superfamily lacks any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge.


Pssm-ID: 238506 [Multi-domain]  Cd Length: 390  Bit Score: 110.78  E-value: 5.87e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 111 DRGASWLREAPIGSNWLRVILVPTIGGLVVSILNQ-LRESAGK--------STGDSHSSLDRVKAVLRPFLKTVAACVTL 181
Cdd:cd01034   12 DLALALFQRLTATHPWLPLLLTPAGFALIAWLTRRfFPGAAGSgipqviaaLELPSAAARRRLLSLRTAVGKILLTLLGL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 182 GTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQ-TGFSLLAAGSAAGISSGFNAAVAGCFFAVESVlwpssstdSSTSLPN 260
Cdd:cd01034   92 LGGASVGREGPSVQIGAAVMLAIGRRLPKWGGlSERGLILAGGAAGLAAAFNTPLAGIVFAIEEL--------SRDFELR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 261 TTSMVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPGELPLYLLLGALCGLVSLALSRCTSSMTSavdSLNKDAGIPKAV 340
Cdd:cd01034  164 FSGLVLLAVIAAGLVSLAVLGNYPYFGVAAVALPLGEAWLLVLVCGVVGGLAGGLFARLLVALSS---GLPGWVRRFRRR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 341 FPVMG----GLSVGIIALVYPEVLYW-GFQNVDILLEKrpfvkglSADLLLQLVAVKIAATAWCRASGLVGGYYAPSLFI 415
Cdd:cd01034  241 RPVLFaalcGLALALIGLVSGGLTFGtGYLQARAALEG-------GGGLPLWFGLLKFLATLLSYWSGIPGGLFAPSLAV 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 416 GGAagmaygkfIGLALAQnpdfnlsILEVASPQAYGLVGMAATLAGVCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSW 495
Cdd:cd01034  314 GAG--------LGSLLAA-------LLGSVSQGALVLLGMAAFLAGVTQAPLTAFVIVMEMTGDQQMLLPLLAAALLASG 378

                 .
gi 334187188 496 I 496
Cdd:cd01034  379 V 379
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
80-497 1.12e-19

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 92.15  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  80 ACLVGVLTGVSVVLFNNCVHLLrdfSWDGIPDRGASWLREAPIGSNWLRViLVPTIGGLVVSIL-------NQLRESAGK 152
Cdd:PRK01610   8 ATVVGILAALAVAGFRHAMLLL---EWLFLSNDSGSLVNAATNLSPWRRL-LTPALGGLAAGLLlwgwqkfTQQRPHAPT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 153 STGDSHSSLDR--VKAVLrpfLKTVAACVTLGTGNSLGPEGPSVEIGASIAkgvnSLFNK--SPQTGFSL-LAAGSAAGI 227
Cdd:PRK01610  84 DYMEALQTDGQfdYAASL---VKSLASLLVVTSGSAIGREGAMILLAALAA----SCFAQrfTPRQEWKLwIACGAAAGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 228 SSGFNAAVAGCFFAVEsVLWpssstdsSTSLPNTTSMVILSAVTASVVSE-IGLGSEPAFKVPDYDFRSPGELPLYLLLG 306
Cdd:PRK01610 157 ASAYHAPLAGSLFIAE-ILF-------GTLMLASLGPVVISAVVALLTTNlLNGSDALLYNVQLSVTVQARDYALIISTG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 307 ALCGLVSLALSRCTSSMTSAVDSLNKDAGIPKAvfpvMGGLSVGIIALVYPEVLYWGFQNVDILLEKRPFVKGLSADLLL 386
Cdd:PRK01610 229 LLAGLCGPLLLTLMNASHRGFVSLKLAPPWQLA----LGGLIVGLLSLFTPAVWGNGYSVVQSFLTAPPLLMLIAGIFLC 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 387 QLVAVkIAATAwcraSGLVGGYYAPSLFIGGAAGMAYGKFIGLALaQNPDfNLSILevaspqaYGLVGMAATLAGVCQVP 466
Cdd:PRK01610 305 KLLAV-LASSG----SGAPGGVFTPTLFVGLAIGMLYGRSLGLWL-PDGE-EITLL-------LGLTGMATLLAATTHAP 370
                        410       420       430
                 ....*....|....*....|....*....|.
gi 334187188 467 LTAVLLLFELTQDYRIVLPLLGAVGMSSWIT 497
Cdd:PRK01610 371 IMSTLMICEMTGEYQLLPGLLIACVIASVIS 401
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
551-689 2.33e-17

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 81.08  E-value: 2.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 551 QSEELPKSIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDpDNIFLGILTLSDIQEFSKARKEGNNRPkdifV 630
Cdd:COG2524   78 KELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGRDLLDAP----V 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 334187188 631 NDICSRSggkckvPWTVTPDMDLLAAQTIMNKHELSHVAVVsgsiDAPRiHPVGVLDRE 689
Cdd:COG2524  153 SDIMTRD------VVTVSEDDSLEEALRLMLEHGIGRLPVV----DDDG-KLVGIITRT 200
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
558-688 9.28e-17

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 77.21  E-value: 9.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 558 SIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARK--EGNNRPKDIFVNDICS 635
Cdd:COG3448    1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRldELEERLLDLPVEDVMT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334187188 636 RsggkcKVPwTVTPDMDLLAAQTIMNKHELSHVAVVsgsiDAPRiHPVGVLDR 688
Cdd:COG3448   81 R-----PVV-TVTPDTPLEEAAELMLEHGIHRLPVV----DDDG-RLVGIVTR 122
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
168-496 3.25e-16

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: 81.62  E-value: 3.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 168 LRPFLKTVAACV-TLGTGNSLGPEGPSVEIGASIAKGVNSLFN-------------KSPQTGFSLLAAGSAAGISSGFNA 233
Cdd:cd01036   85 IRTLIAKTISCIcAVASGLPLGKEGPLVHLGAMIGAGLLQGRSrtlgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGA 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 234 AVAGCFFAVE--SVLWPSSSTDSSTsLPNTTSMVILSAVTASVVSEIGLGSEPAFKVPDYDFRSPG-----ELPLYLLLG 306
Cdd:cd01036  165 PIGGLLFVLEevSTFFPVRLAWRVF-FAALVSAFVIQIYNSFNSGFELLDRSSAMFLSLTVFELHVplnlyEFIPTVVIG 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 307 ALCGLVSLALSRCTSSMTSAV-DSLNKDAGIPKAVFPVmgglsvgIIALVYPEVLYWGfqnvdillekrpfvkglsaDLL 385
Cdd:cd01036  244 VICGLLAALFVRLSIIFLRWRrRLLFRKTARYRVLEPV-------LFTLIYSTIHYAP-------------------TLL 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 386 LQLVaVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLALAQNPDFNlSILEVASPQAYGLVGMAATLAGVCQV 465
Cdd:cd01036  298 LFLL-IYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIGAE-SATLWADPGVYALIGAAAFLGGTTRL 375
                        330       340       350
                 ....*....|....*....|....*....|.
gi 334187188 466 PLTAVLLLFELTQDYRIVLPLLGAVGMSSWI 496
Cdd:cd01036  376 TFSICVIMMELTGDLHHLLPLMVAILIAKAV 406
CBS COG0517
CBS domain [Signal transduction mechanisms];
561-688 3.75e-16

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 75.29  E-value: 3.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI-QEFSKARKEGNNRPkdifVNDICSRSgg 639
Cdd:COG0517    3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLrRALAAEGKDLLDTP----VSEVMTRP-- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 334187188 640 kckvPWTVTPDMDLLAAQTIMNKHELSHVAVVSGSidaprIHPVGVLDR 688
Cdd:COG0517   77 ----PVTVSPDTSLEEAAELMEEHKIRRLPVVDDD-----GRLVGIITI 116
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
561-688 1.60e-15

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 73.32  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARKEgnnRPKDIFVNDICSRSggk 640
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGL---DPLDTPVSEVMTRP--- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 334187188 641 ckvPWTVTPDMDLLAAQTIMNKHELSHVAVVSGSidapriHPVGVLDR 688
Cdd:COG2905   75 ---PITVSPDDSLAEALELMEEHRIRHLPVVDDG------KLVGIVSI 113
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
566-673 4.65e-13

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: 66.11  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 566 RTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARKEGNNRPkdifVNDICSRSggkckvPW 645
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTP----VAEVMTPD------VI 70
                         90       100
                 ....*....|....*....|....*...
gi 334187188 646 TVTPDMDLLAAQTIMNKHELSHVAVVSG 673
Cdd:cd02205   71 TVSPDTDLEEALELMLEHGIRRLPVVDD 98
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
167-496 9.08e-13

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: 71.10  E-value: 9.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 167 VLRPFL-------KTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGF---SLLAAGSAAGISSGFNAAVA 236
Cdd:cd03684   69 IIRGFLgkwtlliKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFPKYRRNEAkrrEILSAAAAAGVAVAFGAPIG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 237 GCFFAVESVlwpssstdsSTSLPNTTSM-----VILSAVTASVVSEIGLGSEPAFKVpDYDFR-SPGELPLYLLLGALCG 310
Cdd:cd03684  149 GVLFSLEEV---------SYYFPLKTLWrsffcALVAAFTLKSLNPFGTGRLVLFEV-EYDRDwHYFELIPFILLGIFGG 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 311 LVSLALSRCTSSMTSAV-DSLNKDAGIPKAVFPVmggLSVGIIALVYP-------EVLYWGFQ---------NVDILLEK 373
Cdd:cd03684  219 LYGAFFIKANIKWARFRkKSLLKRYPVLEVLLVA---LITALISFPNPytrldmtELLELLFNecepgddnsLCCYRDPP 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 374 RPFVKGLSADLLLQLVAVKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLALAQNPDFNLSILEVA-----SPQ 448
Cdd:cd03684  296 AGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGILVEQLAYSYPDSIFFACCTAgpsciTPG 375
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 334187188 449 AYGLVGMAATLAGVCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSWI 496
Cdd:cd03684  376 LYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWV 423
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
173-493 1.18e-09

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: 61.11  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 173 KTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSL-----FNKSPQTGFS-LLAAGSAAGISSGFNAAVAGCFFAVESV- 245
Cdd:cd03683   99 KVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLttffsGIYENESRRMeMLAAACAVGVACTFGAPIGGVLFSIEVTs 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 246 -------LWPssstdssTSLPNTTSMVILSAVTASVVSEIGLGSepAFKVPDYDFRSPG--ELPLYLLLGALCGLVSLAL 316
Cdd:cd03683  179 tyfavrnYWR-------GFFAATCGAFTFRLLAVFFSDQETITA--LFKTTFFVDFPFDvqELPIFALLGIICGLLGALF 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 317 SRCTSSMTSAVDSLNKDAGIPKAVFPVMgglsVGIIALVYPEVLYwgfqnvdillekrPFVkglsadLLLQLVAVKIAAT 396
Cdd:cd03683  250 VFLHRKIVRFRRKNRLFSKFLKRSPLLY----PAIVALLTAVLTF-------------PFL------TLFLFIVVKFVLT 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 397 AWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGLALAQN-PDFNLSILEvasPQAYGLVGMAATLAGVCQVPLTAVlLLFE 475
Cdd:cd03683  307 ALAITLPVPAGIFMPVFVIGAALGRLVGEIMAVLFPEGiRGGISNPIG---PGGYAVVGAAAFSGAVTHTVSVAV-IIFE 382
                        330
                 ....*....|....*...
gi 334187188 476 LTQDYRIVLPLLGAVGMS 493
Cdd:cd03683  383 LTGQISHLLPVLIAVLIS 400
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
80-496 1.47e-09

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: 61.13  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  80 ACLVGVLTGVSVVLFNNCVHLLRDFSW----DGIPDRGASWLREAPIGSNwlrvILVPTIGGLVVSILNQLreSAGKSTG 155
Cdd:cd03685   36 CLLIGIFTGLVAYFIDLAVENLAGLKFlvvkNYIEKGRLFTAFLVYLGLN----LVLVLVAALLVAYIAPT--AAGSGIP 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 156 DSHSSLDRVKA--VLRP---FLKTVAACVTLGTGNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLL----------- 219
Cdd:cd03685  110 EVKGYLNGVKIphILRLktlLVKIVGVILSVSGGLALGKEGPMIHIGACIAAGLSQGGSTSLRLDFRWFryfrndrdkrd 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 220 --AAGSAAGISSGFNAAVAGCFFAVESV--------LWPSSStdsstslpntTSMVilSAVTASVVSEIglgsepafkvp 289
Cdd:cd03685  190 fvTCGAAAGVAAAFGAPVGGVLFSLEEVasfwnqalTWRTFF----------SSMI--VTFTLNFFLSG----------- 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 290 dydFRSpgelplylllgALCGLVSLALSRCTSsmtsaVDSLNKDAGIPKAVFPVMGGLSVGIIALVYPEVLYWGFQNVDI 369
Cdd:cd03685  247 ---CNS-----------GKCGLFGPGGLIMFD-----GSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKR 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 370 LLEKRPFVKGLSAdLLLQLV--AVKIAATAW----------CRASGLV--GGYYAPSLFIGGaagmAYGKFIGLALAQNP 435
Cdd:cd03685  308 INHKGKLLKVLEA-LLVSLVtsVVAFPQTLLiffvlyyflaCWTFGIAvpSGLFIPMILIGA----AYGRLVGILLGSYF 382
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187188 436 DFnlsilEVASPQAYGLVGMAATLAGVCQVPLTAVLLLFELTQDYRIVLPLLGAVGMSSWI 496
Cdd:cd03685  383 GF-----TSIDPGLYALLGAAAFLGGVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWV 438
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
545-611 2.87e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 56.03  E-value: 2.87e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187188 545 LDDSLNQSEELPKSIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:COG3448   59 LPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDL 125
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
561-611 8.26e-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: 8.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 334187188  561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
558-671 1.06e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 51.45  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 558 SIFVSEAMRTR-FATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFSKARKegnnrpkdifVNDICSR 636
Cdd:COG4109   15 ILLVEDIMTLEdVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTP----------IEDVMTK 84
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 334187188 637 SggkckvPWTVTPDMDLLAAQTIMNKHELSHVAVV 671
Cdd:COG4109   85 N------PITVTPDTSLASAAHKMIWEGIELLPVV 113
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
82-476 1.48e-07

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: 54.12  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188  82 LVGVLTGVSVVLFNNCVHLLRDFswdgipdrgaswlREApigsNWLRVILVPtIGGLVVSILNQLreSAGKSTGDSHSSL 161
Cdd:cd03682    4 LIGLLVGSASALFLWSLDWATEF-------------REA----HPWLLPFLP-LAGLLIGYLYQK--FGKNSEKGNNLII 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 162 DRVKAVLRPFLKTVAACVTLGT------GNSLGPEGPSVEIGASIAKGVNSLFNKSPQTGFSLLAAGSAAGISSGFNAAV 235
Cdd:cd03682   64 EEIHGPEEGIPLRMAPLVLFGTvlthlfGGSAGREGTAVQMGGSLADAFGRVFKLPEEDRRILLIAGIAAGFAAVFGTPL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 236 AGCFFAVE---------SVLWPSsstdsstslpnttsmvILSAVTASVVSEIgLGSEPAFKVPDYDFRSPGELPLYLLLG 306
Cdd:cd03682  144 AGAIFALEvlvlgrlrySALIPC----------------LVAAIVADWVSHA-LGLEHTHYHIVFIPTLDPLLFVKVILA 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 307 ALC-GLVSLALSRCTSSMTSAVDSLnkdagIPKAVF-PVMGGLSvgIIALVYpevlywgfqnvdiLLEKRPFVkGLSADL 384
Cdd:cd03682  207 GIIfGLAGRLFAELLHFLKKLLKKR-----IKNPYLrPFVGGLL--IILLVY-------------LLGSRRYL-GLGTPL 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 385 LLQLVA----------VKIAATAWCRASGLVGGYYAPSLFIGGAAGMAYGKFIGlalaqnpdfnLSILEVASpqayglVG 454
Cdd:cd03682  266 IEDSFFggtvypydwlLKLIFTVITLGAGFKGGEVTPLFFIGATLGNALAPILG----------LPVSLLAA------LG 329
                        410       420
                 ....*....|....*....|..
gi 334187188 455 MAATLAGVCQVPLTAVLLLFEL 476
Cdd:cd03682  330 FVAVFAGATNTPLACIIMGIEL 351
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
576-688 2.88e-07

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: 49.45  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 576 TSLEEAlTRMLIEKQ-SCALIVDPDNIfLGILTLSDIqefSKARKEGNnrpKDIFVNDICSrsggkcKVPWTVTPDMDLL 654
Cdd:cd04588   11 ATIKDA-AKLLSENNiHGAPVVDDGKL-VGIVTLTDI---AKALAEGK---ENAKVKDIMT------KDVITIDKDEKIY 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 334187188 655 AAQTIMNKHELSHVAVVSGSIDaprihPVGVLDR 688
Cdd:cd04588   77 DAIRLMNKHNIGRLIVVDDNGK-----PVGIITR 105
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
561-611 4.60e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 49.53  E-value: 4.60e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:COG4109   78 IEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
561-611 8.24e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 50.27  E-value: 8.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:COG2524  152 VSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
CBS COG0517
CBS domain [Signal transduction mechanisms];
561-611 1.34e-06

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 47.94  E-value: 1.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:COG0517   69 VSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDL 119
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
561-673 1.49e-06

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


Pssm-ID: 341393 [Multi-domain]  Cd Length: 120  Bit Score: 47.59  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALtRMLIEKQSCALIV---DPDNIFlGILTLSDIQEFSKArKEGNnrPKDIFVNDICSrs 637
Cdd:cd04630    1 VRDVMKTNVVTIDGLATVREAL-QLMKEHNVKSLIVekrHEHDAY-GIVTYTDILKKVIA-EDRD--PDLVNVYEIMT-- 73
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 334187188 638 ggkcKVPWTVTPDMDLLAAQTIMNKHELSHVAVVSG 673
Cdd:cd04630   74 ----KPAISVSPDLDIKYAARLMARFNLKRAPVIEN 105
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
561-611 2.63e-06

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 46.85  E-value: 2.63e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:cd02205   61 VAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
565-686 3.12e-06

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: 46.75  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIqefSKARKEGnnRPKDIFVNDICSRSggkckvP 644
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDI---VRAVAEG--IDLDTPVEEIMTKN------L 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 334187188 645 WTVTPDMDLLAAQTIMNKHELSHVAVVSGSIDaprihPVGVL 686
Cdd:cd09836   70 VTVSPDESIYEAAELMREHNIRHLPVVDGGGK-----LVGVI 106
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
561-686 3.76e-06

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: 46.61  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 561 VSEAMRT--RFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIqefskaRK--EGNNRPKDIFVNDICSR 636
Cdd:cd04604    5 VSDLMHTgdELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDL------RRalEKGLDILNLPAKDVMTR 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334187188 637 SggkckvPWTVTPDMdlLAAQ--TIMNKHELSHVAVVsgsiDAPRiHPVGVL 686
Cdd:cd04604   79 N------PKTISPDA--LAAEalELMEEHKITVLPVV----DEDG-KPVGIL 117
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
563-691 1.25e-05

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: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 44.87  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 563 EAMRTRFATVMMSTSLEEALTRMLIEKQSCA--LIVDPDNIFLGILTLSDIQEFSkaRKEGNNRPkdifVNDIcSRSGGK 640
Cdd:cd04639    1 DAMVTEFPIVDADLTLREFADDYLIGKKSWRefLVTDEAGRLVGLITVDDLRAIP--TSQWPDTP----VREL-MKPLEE 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 641 CKvpwTVTPDMDLLAAQTIMNKHELSHVAVVSGSidaprIHPVGVLDRECI 691
Cdd:cd04639   74 IP---TVAADQSLLEVVKLLEEQQLPALAVVSEN-----GTLVGLIEKEDI 116
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
560-692 1.46e-05

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: 44.92  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 560 FVSEAMRTRFATVMMSTSLEEAlTRMLIEKQSCAL-IVDPDNIFLGILTLSDIqefSKARKEGNNRPKDIFVNDICsrsg 638
Cdd:cd04605    1 LVEDIMSKDVATIREDISIEEA-AKIMIDKNVTHLpVVSEDGKLIGIVTSWDI---SKAVALKKDSLEEIMTRNVI---- 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334187188 639 gkckvpwTVTPDMDLLAAQTIMNKHELSHVAVVsgsiDAPRiHPVGVLDRECIT 692
Cdd:cd04605   73 -------TARPDEPIELAARKMEKHNISALPVV----DDDR-RVIGIITSDDIS 114
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
568-611 1.57e-05

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: 42.50  E-value: 1.57e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 334187188   568 RFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
571-673 2.48e-05

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: 43.94  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 571 TVMMSTSLEEALtRMLIEKQSCALIV-DPDNIFLGILTLSDIqefskARKEGNNRP--KDIFVNDICSRSggkckvPWTV 647
Cdd:cd04623    6 TVSPDATVAEAL-RLLAEKNIGALVVvDDGGRLVGILSERDY-----VRKLALRGAssLDTPVSEIMTRD------VVTC 73
                         90       100
                 ....*....|....*....|....*.
gi 334187188 648 TPDMDLLAAQTIMNKHELSHVAVVSG 673
Cdd:cd04623   74 TPDDTVEECMALMTERRIRHLPVVED 99
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
561-607 2.81e-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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 44.41  E-value: 2.81e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALtRMLIeKQSCALIVDPDNIFLGILT 607
Cdd:cd04643   71 VEEVMNTDVPTVSPDDDLEEVL-HLLV-DHPFLCVVDEDGYFLGIIT 115
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
561-674 4.46e-05

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: 43.76  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 561 VSEAMRTRFATVMMSTSLEEAlTRMLIEKQSCALIVDPDNIFLGILTLSDIQE-------FSK-----ARKEGNNRPKDI 628
Cdd:cd04631    2 VEDYMTKNVITATPGTPIEDV-AKIMVRNGFRRLPVVSDGKLVGIVTSTDIMRylgsgeaFEKlktgnIHEVLNVPISSI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 334187188 629 FVNDICsrsggkckvpwTVTPDMDLLAAQTIMNKHELSHVAVVSGS 674
Cdd:cd04631   81 MKRDII-----------TTTPDTDLGEAAELMLEKNIGALPVVDDG 115
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 ...
565-694 5.42e-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: 43.18  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIfLGILTLSDIqefskaRK----EGnnRPKDIFVNDICSRSggk 640
Cdd:cd04587    2 MSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRL-VGIVTDRDL------RNrvvaEG--LDPDTPVSEIMTPP--- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334187188 641 ckvPWTVTPDMDLLAAQTIMNKHELSHVAVVSGSIdaprihPVGVldrecITLT 694
Cdd:cd04587   70 ---PVTIDADALVFEALLLMLERNIHHLPVVDDGR------VVGV-----VTAT 109
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
565-683 2.07e-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: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 41.27  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSD-IQEFSKARKEGNNRPKdifVNDICSRSggkckv 643
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDcLKALLEASYHCEPGGT---VADYMSTE------ 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 334187188 644 PWTVTPDMDLL-AAQTIMNKHelshvavvsgsidaPRIHPV 683
Cdd:cd04629   72 VLTVSPDTSIVdLAQLFLKNK--------------PRRYPV 98
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
560-686 2.51e-04

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 41.64  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 560 FVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDpDNIFLGILTLSDIQEF--SKA----RKEGNNRPKDIFVNDI 633
Cdd:cd04584    1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRAspSKAtslsIYELNYLLSKIPVKDI 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334187188 634 CSRSggkckvPWTVTPDMDLLAAQTIMNKHELSHVAVVSGSidapriHPVGVL 686
Cdd:cd04584   80 MTKD------VITVSPDDTVEEAALLMLENKIGCLPVVDGG------KLVGII 120
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
561-611 2.68e-04

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 41.36  E-value: 2.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334187188 561 VSEAMRTRFATVMMSTSLEeALTRMLiEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:cd04608   69 VSKAMYKQFKQVDLDTPLG-ALSRIL-ERDHFALVVDGQGKVLGIVTRIDL 117
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
561-672 4.04e-04

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: 41.17  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLiEKQSCALIVDPDNIFLGILTLSDIQEFSkARKEGNNrpkdiFVNDICSRsggk 640
Cdd:cd04611    7 VGSAMNRSPLVLPGDASLAEAARRMR-SHRADAAVIECPDGGLGILTERDLVRFI-ARHPGNT-----PVGELASR---- 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 334187188 641 ckvPW-TVTPDMDLLAAQTIMNKHELSHVAVVS 672
Cdd:cd04611   76 ---PLlTVGAEDSLIHARDLLIDHRIRHLAVVD 105
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
571-671 5.30e-04

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 40.17  E-value: 5.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 571 TVMMSTSLEEALtRMLIEKQSCALIVDPDNIFLGILTLSDIQefsKARKEG-NNRPkdifVNDICSRSggkckvPWTVTP 649
Cdd:cd04595    6 TVSPDTTIEEAR-KIMLRYGHTGLPVVEDGKLVGIISRRDVD---KAKHHGlGHAP----VKGYMSTN------VITIDP 71
                         90       100
                 ....*....|....*....|..
gi 334187188 650 DMDLLAAQTIMNKHELSHVAVV 671
Cdd:cd04595   72 DTSLEEAQELMVEHDIGRLPVV 93
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
565-673 6.06e-04

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: 40.49  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALtRMLIEKQ-SCALIVDPDNIFLGILTLSDI-----------------------QEFSKARKE 620
Cdd:cd04586    1 MTTDVVTVTPDTSVREAA-RLLLEHRiSGLPVVDDDGKLVGIVSEGDLlrreepgteprrvwwldallespERLAEEYVK 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334187188 621 GNNRPkdifVNDICSRsggkcKVPwTVTPDMDLLAAQTIMNKHELSHVAVVSG 673
Cdd:cd04586   80 AHGRT----VGDVMTR-----PVV-TVSPDTPLEEAARLMERHRIKRLPVVDD 122
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
571-687 6.58e-04

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: 39.88  E-value: 6.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 571 TVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIqefskARK---EGNNrPKDIFVNDICSRSggkckvPWTV 647
Cdd:cd17781    6 TVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDL-----ARRvvaSGLD-PRSTLVSSVMTPN------PLCV 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 334187188 648 TPDMDLLAAQTIMNKHELSHVAVVS--GSIdaprihpVGVLD 687
Cdd:cd17781   74 TMDTSATDALDLMVEGKFRHLPVVDddGDV-------VGVLD 108
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
565-671 7.19e-04

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: 39.83  E-value: 7.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 565 MRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIqeFSKARKEGNNrPKDIFVNDICSRSggkckvP 644
Cdd:cd17775    1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDI--VVEVVAKGLD-PKDVTVGDIMSAD------L 71
                         90       100
                 ....*....|....*....|....*..
gi 334187188 645 WTVTPDMDLLAAQTIMNKHELSHVAVV 671
Cdd:cd17775   72 ITAREDDGLFEALERMREKGVRRLPVV 98
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
566-633 7.76e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in proteobacteria; 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: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 40.24  E-value: 7.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187188 566 RTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQE---FSKARKEGNNRpKDIFVNDI 633
Cdd:cd04640    4 RVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGekpLKIVQERGIPR-EELLVADV 73
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
576-671 9.45e-04

CBS domain protein; 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 39.61  E-value: 9.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 576 TSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIqefsKARKEGNNRPKDIFVNDICSRSggkckvPWTVTPDMDLLA 655
Cdd:cd17771   13 TPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDL----LSRVALPQIDLDAPISEVMTPD------PVRLPPSASAFE 82
                         90
                 ....*....|....*.
gi 334187188 656 AQTIMNKHELSHVAVV 671
Cdd:cd17771   83 AALLMAEHGFRHVCVV 98
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
571-671 1.42e-03

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: 39.04  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 571 TVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEfskarkegnNRPKDIFVNDICSRSggkckvPWTVTPD 650
Cdd:cd04583    6 TITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINR---------NYRKAKKVGEIMERD------VFTVKED 70
                         90       100
                 ....*....|....*....|.
gi 334187188 651 MDLLAAQTIMNKHELSHVAVV 671
Cdd:cd04583   71 SLLRDTVDRILKRGLKYVPVV 91
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
555-611 2.08e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.36  E-value: 2.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334187188 555 LPKSIFVSEAMRTR-FATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:PRK14869 242 INQSIPVSYIMTTEdLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHL 299
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
556-611 2.92e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 38.27  E-value: 2.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334187188 556 PKSIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDpDNIFLGILTLSDI 611
Cdd:COG2905   62 PLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDL 116
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
571-671 3.09e-03

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 38.31  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 571 TVMMSTSLEEALtRMLIEKQSCAL-IVDPDNIFLGILTLSDI-----------QEFSKARKEGNNRPKDIFVNDICSRSg 638
Cdd:cd04600    7 TVTPDTSLEEAW-RLLRRHRIKALpVVDRARRLVGIVTLADLlkhadldpprgLRGRLRRTLGLRRDRPETVGDIMTRP- 84
                         90       100       110
                 ....*....|....*....|....*....|...
gi 334187188 639 gkckVPwTVTPDMDLLAAQTIMNKHELSHVAVV 671
Cdd:cd04600   85 ----VV-TVRPDTPIAELVPLFSDGGLHHIPVV 112
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
553-615 4.87e-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: 37.52  E-value: 4.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187188 553 EELPKSIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDIQEFS 615
Cdd:cd17775   55 GLDPKDVTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
554-624 4.87e-03

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 40.06  E-value: 4.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187188  554 ELPKSIFVSEAM-RTRFATVMMSTSLEEALTRML---IEKqscALIVDPDNIFLGILTLSDI---QEFSKARKEGNNR 624
Cdd:pfam00478 134 ETDLSQPVSEVMtKENLVTAPEGTTLEEAKEILHkhkIEK---LPVVDDNGRLVGLITIKDIekaKEYPNAAKDEQGR 208
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
558-611 5.14e-03

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: 37.70  E-value: 5.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334187188 558 SIFVSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDPDNIFLGILTLSDI 611
Cdd:cd17778   74 STPVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDV 127
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
575-671 5.57e-03

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: 37.04  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187188 575 STSLEEALTRmlIEKQS--CALIVDPDNIFLGILTLSDIqefskaRKeG--NNRPKDIFVNDICsrsggkCKVPWTVTPD 650
Cdd:cd04607   10 DTTIREAIEV--IDKGAlqIALVVDENRKLLGTVTDGDI------RR-GllKGLSLDAPVEEVM------NKNPITASPS 74
                         90       100
                 ....*....|....*....|.
gi 334187188 651 MDLLAAQTIMNKHELSHVAVV 671
Cdd:cd04607   75 TSREELLALMRAKKILQLPIV 95
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
561-613 6.54e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; 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 archaea. 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: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 36.94  E-value: 6.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334187188 561 VSEAMRTRFATVMMSTSLEEALTRMLIEKQSCALIVDpDNIFLGILTLSDIQE 613
Cdd:cd04594   54 VGKYVVRGSPYVTPTSSLEEAWEIMMRNKSRWVAVVE-KGKFLGIITLDDLLE 105
 
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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