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Conserved domains on  [gi|30695978|ref|NP_849813|]
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chloride channel F [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
PubMed:  11182894|9207144|9046241
SCOP:  4003598

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 3-348 3.27e-86

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: 272.90  E-value: 3.27e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   3 HGLLEILDQIRQsnssqRQGLdfLAGIYPVIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMMENNRERRIALTAA 82
Cdd:cd00400  64 HGIPEVIEAIAL-----GGGR--LPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVAC 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  83 GAASGIASGFNAAVAGCFFAIETVLRPLRAEnsppfTTAMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLI 162
Cdd:cd00400 137 GAAAGIAAAFNAPLAGALFAIEVLLGEYSVA-----SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLL 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 163 LGMLCGAVSVVFSRLVTWFTKSFdfikDKFGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILhtgksASAPGIWL 242
Cdd:cd00400 212 LGLLAGLVGVLFVRLLYKIERLF----RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLL 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 243 LAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGgsaaEIINRAIPGnaAVAQPQAYALVGMAATLASMCSVPL 322
Cdd:cd00400 283 LLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFG----LLLPALFPG--LVASPGAYALVGMAALLAAVLRAPL 356

                       330       340
                ....*....|....*....|....*.
gi 30695978 323 TSVLLLFELTKDYRILLPLMGAVGLA 348
Cdd:cd00400 357 TAILLVLELTGDYSLLLPLMLAVVIA 382
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 425-558 9.78e-63

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: 202.60  E-value: 9.78e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDENTCPVSSVCTKKISYrgqE 504
Cdd:cd04592   1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPKTILVSSICTRNGGY---C 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30695978 505 RGLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVihkGKRRKLLGLLHYDSIW 558
Cdd:cd04592  78 RGLWTCTPDMDLLTAKMLMEARGINQLPVVKRGGE---ERRRRVVGLLDRDSID 128
PLN02274 super family cl33447
inosine-5'-monophosphate dehydrogenase
 371-477 2.54e-04

inosine-5'-monophosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02274:

Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 43.89  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  371 RGYSSLSPSERKTEGvwrhtdnadSLELTVIENPDHNSFLDEETILEDlkVMRVMSKNYVkVSSGTTLREARNILKESHQ 450
Cdd:PLN02274 129 RGFSSVCVTETGTMG---------SKLLGYVTKRDWDFVNDRETKLSE--VMTSDDDLVT-APAGIDLEEAEAVLKDSKK 196

                         90       100
                 ....*....|....*....|....*..
gi 30695978  451 NCIMVVDDDDFLAGILTHGDIRRYLSN 477
Cdd:PLN02274 197 GKLPLVNEDGELVDLVTRTDVKRVKGY 223
 
Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 3-348 3.27e-86

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: 272.90  E-value: 3.27e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   3 HGLLEILDQIRQsnssqRQGLdfLAGIYPVIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMMENNRERRIALTAA 82
Cdd:cd00400  64 HGIPEVIEAIAL-----GGGR--LPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVAC 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  83 GAASGIASGFNAAVAGCFFAIETVLRPLRAEnsppfTTAMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLI 162
Cdd:cd00400 137 GAAAGIAAAFNAPLAGALFAIEVLLGEYSVA-----SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLL 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 163 LGMLCGAVSVVFSRLVTWFTKSFdfikDKFGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILhtgksASAPGIWL 242
Cdd:cd00400 212 LGLLAGLVGVLFVRLLYKIERLF----RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLL 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 243 LAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGgsaaEIINRAIPGnaAVAQPQAYALVGMAATLASMCSVPL 322
Cdd:cd00400 283 LLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFG----LLLPALFPG--LVASPGAYALVGMAALLAAVLRAPL 356

                       330       340
                ....*....|....*....|....*.
gi 30695978 323 TSVLLLFELTKDYRILLPLMGAVGLA 348
Cdd:cd00400 357 TAILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
31-351 1.29e-68

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 227.71  E-value: 1.29e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  31 PVIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFA-LMMENNRERRI--------ALtaagaasgiASGFNAAVAGCFF 101
Cdd:COG0038  99 APVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGrLLRLSPEDRRIllaagaaaGL---------AAAFNAPLAGALF 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 102 AIETVLRPLRAENSPPfttamIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWF 181
Cdd:COG0038 170 ALEVLLRDFSYRALIP-----VLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLLLKV 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 182 TKSFdfikDKFGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHTGksasaPGIWLLAQLAAAKVVATALCKGSG 261
Cdd:COG0038 245 ERLF----KRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGE-----LSLLLLLLLLLLKLLATALTLGSG 315

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 262 LVGGLYAPSLMIGAAVGAVFGGsaaeIINRAIPGnaAVAQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPL 341
Cdd:COG0038 316 GPGGIFAPSLFIGALLGAAFGL----LLNLLFPG--LGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389

                       330
                ....*....|
gi 30695978 342 MGAVGLAIWV 351
Cdd:COG0038 390 MIACVIAYLV 399
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 32-351 4.83e-67

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: 221.65  E-value: 4.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978    32 VIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFA--LMMENNRERRIaLTAAGAASGIASGFNAAVAGCFFAIETVLRp 109
Cdd:pfam00654  41 PVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGrrLFRLSPRDRRI-LLAAGAAAGLAAAFNAPLAGVLFALEELSR- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   110 lraeNSPPFTTAMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWFTKSFDFIK 189
Cdd:pfam00654 119 ----SFSLRALIPVLLASVVAALVSRLIFGNSPLFSVGEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   190 DKfglPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHtgksaSAPGIWLLAQLAAAKVVATALCKGSGLVGGLYAP 269
Cdd:pfam00654 195 KI---PPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFN-----GNTSLSLLLLLLLLKFLATALSLGSGAPGGIFAP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   270 SLMIGAAVGAVFGgsaaEIINRAIPGNAAvaQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPLMGAVGLAI 349
Cdd:pfam00654 267 SLAIGAALGRAFG----LLLALLFPIGGL--PPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAY 340


                  ..
gi 30695978   350 WV 351
Cdd:pfam00654 341 AV 342
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 425-558 9.78e-63

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: 202.60  E-value: 9.78e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDENTCPVSSVCTKKISYrgqE 504
Cdd:cd04592   1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPKTILVSSICTRNGGY---C 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30695978 505 RGLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVihkGKRRKLLGLLHYDSIW 558
Cdd:cd04592  78 RGLWTCTPDMDLLTAKMLMEARGINQLPVVKRGGE---ERRRRVVGLLDRDSID 128
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
28-569 5.50e-47

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 173.39  E-value: 5.50e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   28 GIYPV----IKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMMENNRERRIALTAAGAASGIASGFNAAVAGCFFAI 103
Cdd:PRK01862 111 GVVPVrqslWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGITSAYNAPIAGAFFVA 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  104 ETVLRPLRAENSPPfttamIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSvvfsrlvTWFTK 183
Cdd:PRK01862 191 EIVLGSIAMESFGP-----LVVASVVANIVMREFAGYQPPYEMPVFPAVTGWEVLLFVALGVLCGAAA-------PQFLR 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  184 SFDFIKDKFG---LPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHTgksasaPGIWL-LAQLAAAKVVATALCKG 259
Cdd:PRK01862 259 LLDASKNQFKrlpVPLPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILHA------PWTWQaLVAVLVAKLIATAATAG 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  260 SGLVGGLYAPSLMIGAAVGAVFGGSAaeiiNRAIPGnaAVAQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILL 339
Cdd:PRK01862 333 SGAVGGVFTPTLFVGAVVGSLFGLAM----HALWPG--HTSAPFAYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVL 406

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  340 PLMGAVGLAIWvpsvanqgkesdssegrsTGRGYSSLSPSErktEGVWRHTDNAdsleltvienpdhnsfldEETILEDL 419
Cdd:PRK01862 407 PLMVSCVVAYF------------------TARALGTTSMYE---ITLRRHQDEA------------------ERERLRTT 447

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  420 KVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLsnnastiLDENTCPVSSVctkkIS 499
Cdd:PRK01862 448 QMRELIQPAQTVVPPTASVADMTRVFLEYPVKYLYVVDDDGRFRGAVALKDITSDL-------LDKRDTTDKTA----AD 516

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  500 YRGQERGLLTcyPDATVGVAKELMEARGVKQLPVVKRGEvihkgkRRKLLGLLHYDSiwtfLRDEMSRRR 569
Cdd:PRK01862 517 YAHTPFPLLT--PDMPLGDALEHFMAFQGERLPVVESEA------SPTLAGVVYKTS----LLDAYRRMN 574
CBS COG0517
CBS domain [Signal transduction mechanisms];
419-557 2.09e-25

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 101.48  E-value: 2.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 419 LKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDEntcPVSSVCTKKi 498
Cdd:COG0517   1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDT---PVSEVMTRP- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30695978 499 syrgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRGevihkgkrRKLLGLLHYDSI 557
Cdd:COG0517  77 --------PVTVSPDTSLEEAAELMEEHKIRRLPVVDDD--------GRLVGIITIKDL 119
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 421-477 6.28e-11

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 57.99  E-value: 6.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978   421 VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSN 477
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
415-494 1.41e-05

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 47.90  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  415 ILEDLK--VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI-RRYLSNNASTILDENTCPVS 491
Cdd:PRK14869  62 LIEDVKpqVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLaRAYMDILDPEILSKSPTSLE 141


                 ...
gi 30695978  492 SVC 494
Cdd:PRK14869 142 NII 144
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 430-475 1.25e-04

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 39.80  E-value: 1.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 30695978    430 VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYL 475
Cdd:smart00116   3 VTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 371-477 2.54e-04

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 43.89  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  371 RGYSSLSPSERKTEGvwrhtdnadSLELTVIENPDHNSFLDEETILEDlkVMRVMSKNYVkVSSGTTLREARNILKESHQ 450
Cdd:PLN02274 129 RGFSSVCVTETGTMG---------SKLLGYVTKRDWDFVNDRETKLSE--VMTSDDDLVT-APAGIDLEEAEAVLKDSKK 196

                         90       100
                 ....*....|....*....|....*..
gi 30695978  451 NCIMVVDDDDFLAGILTHGDIRRYLSN 477
Cdd:PLN02274 197 GKLPLVNEDGELVDLVTRTDVKRVKGY 223
 
Name Accession Description Interval E-value
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 3-348 3.27e-86

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: 272.90  E-value: 3.27e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   3 HGLLEILDQIRQsnssqRQGLdfLAGIYPVIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMMENNRERRIALTAA 82
Cdd:cd00400  64 HGIPEVIEAIAL-----GGGR--LPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRRILVAC 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  83 GAASGIASGFNAAVAGCFFAIETVLRPLRAEnsppfTTAMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLI 162
Cdd:cd00400 137 GAAAGIAAAFNAPLAGALFAIEVLLGEYSVA-----SLIPVLLASVAAALVSRLLFGAEPAFGVPLYDPLSLLELPLYLL 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 163 LGMLCGAVSVVFSRLVTWFTKSFdfikDKFGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILhtgksASAPGIWL 242
Cdd:cd00400 212 LGLLAGLVGVLFVRLLYKIERLF----RRLPIPPWLRPALGGLLLGLLGLFLPQVLGSGYGAILLAL-----AGELSLLL 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 243 LAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGgsaaEIINRAIPGnaAVAQPQAYALVGMAATLASMCSVPL 322
Cdd:cd00400 283 LLLLLLLKLLATALTLGSGFPGGVFAPSLFIGAALGAAFG----LLLPALFPG--LVASPGAYALVGMAALLAAVLRAPL 356

                       330       340
                ....*....|....*....|....*.
gi 30695978 323 TSVLLLFELTKDYRILLPLMGAVGLA 348
Cdd:cd00400 357 TAILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
31-351 1.29e-68

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 227.71  E-value: 1.29e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  31 PVIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFA-LMMENNRERRI--------ALtaagaasgiASGFNAAVAGCFF 101
Cdd:COG0038  99 APVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGrLLRLSPEDRRIllaagaaaGL---------AAAFNAPLAGALF 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 102 AIETVLRPLRAENSPPfttamIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWF 181
Cdd:COG0038 170 ALEVLLRDFSYRALIP-----VLIASVVAYLVSRLLFGNGPLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLLLKV 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 182 TKSFdfikDKFGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHTGksasaPGIWLLAQLAAAKVVATALCKGSG 261
Cdd:COG0038 245 ERLF----KRLKLPPWLRPAIGGLLVGLLGLFLPQVLGSGYGLIEALLNGE-----LSLLLLLLLLLLKLLATALTLGSG 315

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 262 LVGGLYAPSLMIGAAVGAVFGGsaaeIINRAIPGnaAVAQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPL 341
Cdd:COG0038 316 GPGGIFAPSLFIGALLGAAFGL----LLNLLFPG--LGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389

                       330
                ....*....|
gi 30695978 342 MGAVGLAIWV 351
Cdd:COG0038 390 MIACVIAYLV 399
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 32-351 4.83e-67

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: 221.65  E-value: 4.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978    32 VIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFA--LMMENNRERRIaLTAAGAASGIASGFNAAVAGCFFAIETVLRp 109
Cdd:pfam00654  41 PVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGrrLFRLSPRDRRI-LLAAGAAAGLAAAFNAPLAGVLFALEELSR- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   110 lraeNSPPFTTAMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWFTKSFDFIK 189
Cdd:pfam00654 119 ----SFSLRALIPVLLASVVAALVSRLIFGNSPLFSVGEPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   190 DKfglPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHtgksaSAPGIWLLAQLAAAKVVATALCKGSGLVGGLYAP 269
Cdd:pfam00654 195 KI---PPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLFN-----GNTSLSLLLLLLLLKFLATALSLGSGAPGGIFAP 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   270 SLMIGAAVGAVFGgsaaEIINRAIPGNAAvaQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPLMGAVGLAI 349
Cdd:pfam00654 267 SLAIGAALGRAFG----LLLALLFPIGGL--PPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAY 340


                  ..
gi 30695978   350 WV 351
Cdd:pfam00654 341 AV 342
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 425-558 9.78e-63

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: 202.60  E-value: 9.78e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDENTCPVSSVCTKKISYrgqE 504
Cdd:cd04592   1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPKTILVSSICTRNGGY---C 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30695978 505 RGLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVihkGKRRKLLGLLHYDSIW 558
Cdd:cd04592  78 RGLWTCTPDMDLLTAKMLMEARGINQLPVVKRGGE---ERRRRVVGLLDRDSID 128
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 25-351 1.06e-47

ClC chloride channel EriC. This domain is found in the EriC chloride transporters that mediate the extreme acid resistance response in eubacteria and archaea. This response allows bacteria to survive in the acidic environments by decarboxylation-linked proton utilization. As shown for Escherichia coli EriC, these channels can counterbalance the electric current produced by the outwardly directed virtual proton pump linked to amino acid decarboxylation. The EriC proteins belong to the ClC superfamily of chloride ion channels, which share a unique double-barreled architecture and voltage-dependent gating mechanism. The voltage-dependent gating is conferred by the permeating anion itself, acting as the gating charge. In Escherichia coli EriC, a glutamate residue that protrudes into the pore is thought to participate in gating by binding to a Cl- ion site within the selectivity filter.


Pssm-ID: 238504 [Multi-domain]  Cd Length: 402  Bit Score: 171.57  E-value: 1.06e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  25 FLAGIypvikaiqaaVTLGTGCSLGPEGPSVDIGKSCANGFA-LMMENNRERRIALTaAGAASGIASGFNAAVAGCFFAI 103
Cdd:cd01031  90 FVGGV----------LALGSGLSLGREGPSVQIGAAIGQGVSkWFKTSPEERRQLIA-AGAAAGLAAAFNAPLAGVLFVL 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 104 ETVLRplraeNSPPFTTAMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWFTK 183
Cdd:cd01031 159 EELRH-----SFSPLALLTALVASIAADFVSRLFFGLGPVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKSQD 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 184 SFDFIKdkfGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHTGksasaPGIWLLAQLAAAKVVATALCKGSGLV 263
Cdd:cd01031 234 LYRKLK---KLPRELRVLLPGLLIGPLGLLLPEALGGGHGLILSLAGGN-----FSISLLLLIFVLRFIFTMLSYGSGAP 305

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 264 GGLYAPSLMIGAAVGAVFGGSAAEIinraipGNAAVAQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPLMG 343
Cdd:cd01031 306 GGIFAPMLALGALLGLLFGTILVQL------GPIPISAPATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMV 379


                ....*...
gi 30695978 344 AVGLAIWV 351
Cdd:cd01031 380 VCLVAYLV 387
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
28-569 5.50e-47

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 173.39  E-value: 5.50e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   28 GIYPV----IKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMMENNRERRIALTAAGAASGIASGFNAAVAGCFFAI 103
Cdd:PRK01862 111 GVVPVrqslWRSASSLLTIGSGGSIGREGPMVQLAALAASLVGRFAHFDPPRLRLLVACGAAAGITSAYNAPIAGAFFVA 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  104 ETVLRPLRAENSPPfttamIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSvvfsrlvTWFTK 183
Cdd:PRK01862 191 EIVLGSIAMESFGP-----LVVASVVANIVMREFAGYQPPYEMPVFPAVTGWEVLLFVALGVLCGAAA-------PQFLR 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  184 SFDFIKDKFG---LPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHTgksasaPGIWL-LAQLAAAKVVATALCKG 259
Cdd:PRK01862 259 LLDASKNQFKrlpVPLPVRLALGGLLVGVISVWVPEVWGNGYSVVNTILHA------PWTWQaLVAVLVAKLIATAATAG 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  260 SGLVGGLYAPSLMIGAAVGAVFGGSAaeiiNRAIPGnaAVAQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILL 339
Cdd:PRK01862 333 SGAVGGVFTPTLFVGAVVGSLFGLAM----HALWPG--HTSAPFAYAMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVL 406

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  340 PLMGAVGLAIWvpsvanqgkesdssegrsTGRGYSSLSPSErktEGVWRHTDNAdsleltvienpdhnsfldEETILEDL 419
Cdd:PRK01862 407 PLMVSCVVAYF------------------TARALGTTSMYE---ITLRRHQDEA------------------ERERLRTT 447

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  420 KVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLsnnastiLDENTCPVSSVctkkIS 499
Cdd:PRK01862 448 QMRELIQPAQTVVPPTASVADMTRVFLEYPVKYLYVVDDDGRFRGAVALKDITSDL-------LDKRDTTDKTA----AD 516

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  500 YRGQERGLLTcyPDATVGVAKELMEARGVKQLPVVKRGEvihkgkRRKLLGLLHYDSiwtfLRDEMSRRR 569
Cdd:PRK01862 517 YAHTPFPLLT--PDMPLGDALEHFMAFQGERLPVVESEA------SPTLAGVVYKTS----LLDAYRRMN 574
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
25-348 7.02e-37

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 142.34  E-value: 7.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   25 FLAGIYPV-------IKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFA-LMMENNRERRIALTAAGAASGIASGFNAAV 96
Cdd:PRK05277  80 ALEGLRPVrwwrvlpVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVLdIFRLRSDEARHTLLAAGAAAGLAAAFNAPL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   97 AGCFFAIETvLRPLRAENSPPFTtaMIILASVISSTVSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSR 176
Cdd:PRK05277 160 AGILFVIEE-MRPQFRYSLISIK--AVFIGVIMATIVFRLFNGEQAVIEVGKFSAPPLNTLWLFLLLGIIFGIFGVLFNK 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  177 LVTWFTKSFDFIKDKFGLPAIVCPALGGLGAGIIALKYPGILYWGFTNVEEILHTGKSASapgiwLLAQLAAAKVVATAL 256
Cdd:PRK05277 237 LLLRTQDLFDRLHGGNKKRWVLMGGAVGGLCGLLGLLAPAAVGGGFNLIPIALAGNFSIG-----MLLFIFVARFITTLL 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  257 CKGSGLVGGLYAPSLMIGAAVGAVFGGSAAEIINRAIPgnaavaQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYR 336
Cdd:PRK05277 312 CFGSGAPGGIFAPMLALGTLLGLAFGMVAAALFPQYHI------EPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQ 385

                        330
                 ....*....|....*.
gi 30695978  337 ILLPLM----GAVGLA 348
Cdd:PRK05277 386 LILPLIitclGATLLA 401
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 40-357 5.89e-32

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: 127.41  E-value: 5.89e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  40 VTLGTGCSLGPEGPSVDIGKSCANGFA-LMMENNRERRIaLTAAGAASGIASGFNAAVAGCFFAIETVLRPLRAENsppf 118
Cdd:cd01033  94 VTVGLGAPLGREVAPREVGALLAQRFSdWLGLTVADRRL-LVACAAGAGLAAVYNVPLAGALFALEILLRTISLRS---- 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 119 tTAMIILASVISSTVSNALLGTQSAFTVPSYDLkSAAELPLYLILGMLCGAVSVVFSRLVTWFTKSFdfIKDKFGLPAIV 198
Cdd:cd01033 169 -VVAALATSAIAAAVASLLKGDHPIYDIPPMQL-STPLLIWALLAGPVLGVVAAGFRRLSQAARAKR--PKGKRILWQMP 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 199 cpaLGGLGAGIIALKYPGILYWGFTNVEEILHTGksasaPGIWLLAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVG 278
Cdd:cd01033 245 ---LAFLVIGLLSIFFPQILGNGRALAQLAFSTT-----LTLSLLLILLVLKIVATLLALRAGAYGGLLTPSLALGALLG 316

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 279 AVFGGsaaeIINRAIPGnaavAQPQAYALVGMAATLASMCSVPLTSVLLLFELTK-DYRILLPLMGAVGLAIWVPSVANQ 357
Cdd:cd01033 317 ALLGI----VWNALLPP----LSIAAFALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGAVAVSRFILQ 388
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 45-351 5.14e-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: 110.01  E-value: 5.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  45 GCSLGPEGPSVDIGKSCANGFALMMENNRERRIA-LTAAGAASGIASGFNAAVAGCFFAIETVLRplraenSPPFTTAMI 123
Cdd:cd01034  94 GASVGREGPSVQIGAAVMLAIGRRLPKWGGLSERgLILAGGAAGLAAAFNTPLAGIVFAIEELSR------DFELRFSGL 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 124 ILASVISST-VSNALLGTQSAFTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWFTKsfdFIKDKFGLPAIVCPAL 202
Cdd:cd01034 168 VLLAVIAAGlVSLAVLGNYPYFGVAAVALPLGEAWLLVLVCGVVGGLAGGLFARLLVALSS---GLPGWVRRFRRRRPVL 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 203 GGLGAG----IIALKYPGILYW-GFTNVEEILHTGKSASApgiwllaQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAV 277
Cdd:cd01034 245 FAALCGlalaLIGLVSGGLTFGtGYLQARAALEGGGGLPL-------WFGLLKFLATLLSYWSGIPGGLFAPSLAVGAGL 317

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695978 278 GAVFGGSAAEiinraipgnaavAQPQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPLMGAVGLAIWV 351
Cdd:cd01034 318 GSLLAALLGS------------VSQGALVLLGMAAFLAGVTQAPLTAFVIVMEMTGDQQMLLPLLAAALLASGV 379
CBS COG0517
CBS domain [Signal transduction mechanisms];
419-557 2.09e-25

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 101.48  E-value: 2.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 419 LKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDEntcPVSSVCTKKi 498
Cdd:COG0517   1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDT---PVSEVMTRP- 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30695978 499 syrgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRGevihkgkrRKLLGLLHYDSI 557
Cdd:COG0517  77 --------PVTVSPDTSLEEAAELMEEHKIRRLPVVDDD--------GRLVGIITIKDL 119
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 421-565 8.99e-23

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 93.74  E-value: 8.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 421 VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLsnnASTILDENTCPVSSVCTKKisy 500
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRV---LAEGLDPLDTPVSEVMTRP--- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695978 501 rgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVIhkgkrrkllGLLHYDSIWTFLRDEM 565
Cdd:COG2905  75 ------PITVSPDDSLAEALELMEEHRIRHLPVVDDGKLV---------GIVSITDLLRALSEEL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
419-540 2.40e-20

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 87.23  E-value: 2.40e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 419 LKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDENT--CPVSSVCTK 496
Cdd:COG3448   2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLldLPVEDVMTR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30695978 497 KIsyrgqerglLTCYPDATVGVAKELMEARGVKQLPVV-KRGEVI 540
Cdd:COG3448  82 PV---------VTVTPDTPLEEAAELMLEHGIHRLPVVdDDGRLV 117
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 32-351 7.43e-20

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: 92.28  E-value: 7.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  32 VIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMM----ENNRERRIALTaAGAASGIASGFNAAVAGCFFAIETVl 107
Cdd:cd03684  80 LIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFpkyrRNEAKRREILS-AAAAAGVAVAFGAPIGGVLFSLEEV- 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 108 rplraenSPPFTTAMiILASVISSTVSNALL------GTQSA--FTVpSYDLK-SAAELPLYLILGMLCGAVSVVFSRLV 178
Cdd:cd03684 158 -------SYYFPLKT-LWRSFFCALVAAFTLkslnpfGTGRLvlFEV-EYDRDwHYFELIPFILLGIFGGLYGAFFIKAN 228

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 179 TWFTKSFDFIKDKFG----------LPAIVCPALGGLGAGIIALKY-------PGILYWGFTNVEEILHTGKSASapgIW 241
Cdd:cd03684 229 IKWARFRKKSLLKRYpvlevllvalITALISFPNPYTRLDMTELLEllfnecePGDDNSLCCYRDPPAGDGVYKA---LW 305

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 242 LLAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFG--------GSAAEIINRAIPGNAAVAQPQAYALVGMAAT 313
Cdd:cd03684 306 SLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGilveqlaySYPDSIFFACCTAGPSCITPGLYAMVGAAAF 385

                       330       340       350
                ....*....|....*....|....*....|....*...
gi 30695978 314 LASMCSVPLTSVLLLFELTKDYRILLPLMGAVGLAIWV 351
Cdd:cd03684 386 LGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWV 423
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
412-553 9.63e-19

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 84.94  E-value: 9.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 412 EETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRYLSNNastiLDENTCPVS 491
Cdd:COG2524  79 ELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK-LVGIITERDLLKALAEG----RDLLDAPVS 153

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695978 492 SVCTKKisyrgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRGEvihkgkrrKLLGLLH 553
Cdd:COG2524 154 DIMTRD---------VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDG--------KLVGIIT 198
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 32-351 4.14e-18

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: 86.63  E-value: 4.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  32 VIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFA--------------LMMENNRERRIALTAAGAASGIASgFNAAVA 97
Cdd:cd01036  89 IAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLqgrsrtlgchvhlfQLFRNPRDRRDFLVAGAAAGVASA-FGAPIG 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  98 GCFFAIETVLRPLRAENS-PPFTTAMI------ILASVISSTVSNALLGTQSAFTVPS-----YDLKsaaELPLYLILGM 165
Cdd:cd01036 168 GLLFVLEEVSTFFPVRLAwRVFFAALVsafviqIYNSFNSGFELLDRSSAMFLSLTVFelhvpLNLY---EFIPTVVIGV 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 166 LCGAVSVVFSRLVTWFTK---SFDFIKDKFGLPAIVCpalgglgagIIALKYPGILYWgftnveeilhtgksasapgiWL 242
Cdd:cd01036 245 ICGLLAALFVRLSIIFLRwrrRLLFRKTARYRVLEPV---------LFTLIYSTIHYA--------------------PT 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 243 LAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGGSAAEIINRAIPGNAAV--AQPQAYALVGMAATLASMCSV 320
Cdd:cd01036 296 LLLFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAGIGAESATlwADPGVYALIGAAAFLGGTTRL 375

                       330       340       350
                ....*....|....*....|....*....|.
gi 30695978 321 PLTSVLLLFELTKDYRILLPLMGAVGLAIWV 351
Cdd:cd01036 376 TFSICVIMMELTGDLHHLLPLMVAILIAKAV 406
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 24-351 5.83e-16

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: 80.37  E-value: 5.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  24 DFLAGIYPVIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMM------ENNRERRIALTAAGAASGIASGFNAAVA 97
Cdd:cd03683  89 EYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTtffsgiYENESRRMEMLAAACAVGVACTFGAPIG 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  98 GCFFAIETVLRPLRAENS-PPFTTAMI--ILASVISSTVSNALLGT----QSAFTVPSYDLKsaaELPLYLILGMLCGAV 170
Cdd:cd03683 169 GVLFSIEVTSTYFAVRNYwRGFFAATCgaFTFRLLAVFFSDQETITalfkTTFFVDFPFDVQ---ELPIFALLGIICGLL 245

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 171 SVVFSRLVTWFTK--------SFDFIKDKFGLPAIVcpalgglgAGIIA-LKYPgilywgftnveeilhtgksasapgIW 241
Cdd:cd03683 246 GALFVFLHRKIVRfrrknrlfSKFLKRSPLLYPAIV--------ALLTAvLTFP------------------------FL 293

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 242 LLAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGgsaaEIINRAIPGNAAVAQ-----PQAYALVGmAATLAS 316
Cdd:cd03683 294 TLFLFIVVKFVLTALAITLPVPAGIFMPVFVIGAALGRLVG----EIMAVLFPEGIRGGIsnpigPGGYAVVG-AAAFSG 368

                       330       340       350
                ....*....|....*....|....*....|....*
gi 30695978 317 MCSVPLTSVLLLFELTKDYRILLPLMGAVGLAIWV 351
Cdd:cd03683 369 AVTHTVSVAVIIFELTGQISHLLPVLIAVLISNAV 403
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 426-552 1.63e-15

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: 72.66  E-value: 1.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 426 SKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNastiLDENTCPVSSVCTKKIsyrgqer 505
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG----GLALDTPVAEVMTPDV------- 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30695978 506 glLTCYPDATVGVAKELMEARGVKQLPVVKRGEvihkgkrrKLLGLL 552
Cdd:cd02205  70 --ITVSPDTDLEEALELMLEHGIRRLPVVDDDG--------KLVGIV 106
PRK01610 PRK01610
putative voltage-gated ClC-type chloride channel ClcB; Provisional
 32-363 1.92e-15

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


Pssm-ID: 234963  Cd Length: 418  Bit Score: 78.66  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   32 VIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFALMMENNRERRIALTAAGAASGIASgFNAAVAGCFFAIETVLRPLR 111
Cdd:PRK01610 101 LVKSLASLLVVTSGSAIGREGAMILLAALAASCFAQRFTPRQEWKLWIACGAAAGMASA-YHAPLAGSLFIAEILFGTLM 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  112 AENSPPfttamIILASVISSTVSNALLGTQSA-FTVPSYDLKSAAELPLYLILGMLCGAVSVVFSRLVTWFTKSFdfIKD 190
Cdd:PRK01610 180 LASLGP-----VVISAVVALLTTNLLNGSDALlYNVQLSVTVQARDYALIISTGLLAGLCGPLLLTLMNASHRGF--VSL 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  191 KFGLPAIVcpALGGLGAGIIALKYPGILYWGFTNVEEILhtgksASAPGIWLLAQLAAAKVVATALCKGSGLVGGLYAPS 270
Cdd:PRK01610 253 KLAPPWQL--ALGGLIVGLLSLFTPAVWGNGYSVVQSFL-----TAPPLLMLIAGIFLCKLLAVLASSGSGAPGGVFTPT 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  271 LMIGAAVGAVFGgsaaEIINRAIPGNAAVAqpQAYALVGMAATLASMCSVPLTSVLLLFELTKDYRILLPLMgavgLAIW 350
Cdd:PRK01610 326 LFVGLAIGMLYG----RSLGLWLPDGEEIT--LLLGLTGMATLLAATTHAPIMSTLMICEMTGEYQLLPGLL----IACV 395

                        330
                 ....*....|...
gi 30695978  351 VPSVANQGKESDS 363
Cdd:PRK01610 396 IASVISRTLRRDS 408
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 425-536 2.11e-14

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 69.76  E-value: 2.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIR-RYLSNNastiLDENTCPVSSVCTKkisyrgq 503
Cdd:cd04622   1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDR-LVGMVTDRDIVvRAVAEG----KDPNTTTVREVMTG------- 68

                        90       100       110
                ....*....|....*....|....*....|...
gi 30695978 504 erGLLTCYPDATVGVAKELMEARGVKQLPVVKR 536
Cdd:cd04622  69 --DVVTCSPDDDVEEAARLMAEHQVRRLPVVDD 99
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 431-553 2.71e-14

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: 69.72  E-value: 2.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 431 KVSSGTTLREArnILKESHQN--CIMVVDDDDFLAGILTHGDIRRYLSNNastiLDENTCPVSSVCTKKIsyrgqerglL 508
Cdd:cd04604  17 LVSPDTSLKEA--LLEMTRKGlgCTAVVDEDGRLVGIITDGDLRRALEKG----LDILNLPAKDVMTRNP---------K 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30695978 509 TCYPDATVGVAKELMEARGVKQLPVVKRGevihkgkrRKLLGLLH 553
Cdd:cd04604  82 TISPDALAAEALELMEEHKITVLPVVDED--------GKPVGILH 118
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
414-552 3.76e-14

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 69.56  E-value: 3.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 414 TILEDLKVMRVM-SKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYlsnnastilDENTcPVSS 492
Cdd:COG4109  11 TFKEILLVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK---------DDDT-PIED 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 493 VCTKKisyrgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRgevihkgkRRKLLGLL 552
Cdd:COG4109  81 VMTKN---------PITVTPDTSLASAAHKMIWEGIELLPVVDD--------DGRLLGII 123
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 420-540 7.71e-14

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: 68.60  E-value: 7.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 420 KVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRYLSNNASTiLDENTC-------PVSS 492
Cdd:cd04584   1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGK-LVGIVTDRDLLRASPSKATS-LSIYELnyllskiPVKD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30695978 493 VCTKKisyrgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04584  79 IMTKD---------VITVSPDDTVEEAALLMLENKIGCLPVVDGGKLV 117
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 430-557 9.24e-14

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: 67.85  E-value: 9.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 430 VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNAStiLDEntcPVSSV-CTKKISyrgqergll 508
Cdd:cd04607   5 VLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGLLKGLS--LDA---PVEEVmNKNPIT--------- 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 30695978 509 tcypdATVGVAKE----LMEARGVKQLPVVKrgevihkgKRRKLLGLLHYDSI 557
Cdd:cd04607  71 -----ASPSTSREellaLMRAKKILQLPIVD--------EQGRVVGLETLDDL 110
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 425-540 4.38e-13

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: 66.68  E-value: 4.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNN----ASTILDENT------------- 487
Cdd:cd04586   1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGteprRVWWLDALLesperlaeeyvka 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30695978 488 --CPVSSVCTKKIsyrgqerglLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04586  81 hgRTVGDVMTRPV---------VTVSPDTPLEEAARLMERHRIKRLPVVDDGKLV 126
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 421-557 3.96e-12

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: 63.03  E-value: 3.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 421 VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTIldentcpvSSVCTKKIsy 500
Cdd:cd04605   2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALKKDSL--------EEIMTRNV-- 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978 501 rgqerglLTCYPDATVGVAKELMEARGVKQLPVVKrgevihkgKRRKLLGLLHYDSI 557
Cdd:cd04605  72 -------ITARPDEPIELAARKMEKHNISALPVVD--------DDRRVIGIITSDDI 113
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 425-537 1.72e-11

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: 61.39  E-value: 1.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTildenTCPVSSVCTKkisyrgqe 504
Cdd:cd09836   1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDL-----DTPVEEIMTK-------- 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 30695978 505 rGLLTCYPDATVGVAKELMEARGVKQLPVVKRG 537
Cdd:cd09836  68 -NLVTVSPDESIYEAAELMREHNIRHLPVVDGG 99
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
159-351 4.37e-11

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 65.16  E-value: 4.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 159 LYLILGMLCGAVSVVFSRLVTWFTKSF------DFIKDKFGLPAIVCPALGGLGAGIIALKY-PGILYWGFTNVEEILHT 231
Cdd:COG0038  10 LAVLVGILAGLAAVLFRLLLELATHLFlggllsAAGSHLPPWLVLLLPPLGGLLVGLLVRRFaPEARGSGIPQVIEAIHL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 232 GKSasapGIWLLaqLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGgsaaeiinRAIPGNAavAQPQAYALVGMA 311
Cdd:COG0038  90 KGG----RIPLR--VAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLG--------RLLRLSP--EDRRILLAAGAA 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30695978 312 ATLASMCSVPLTSVLLLFE-LTKD--YRILLPLMGAVGLAIWV 351
Cdd:COG0038 154 AGLAAAFNAPLAGALFALEvLLRDfsYRALIPVLIASVVAYLV 196
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 421-477 6.28e-11

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 57.99  E-value: 6.28e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978   421 VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSN 477
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
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 ...
 424-540 7.08e-11

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: 59.36  E-value: 7.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 424 VMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIR-RYLSNNASTildenTCPVSSVCTKKisyrg 502
Cdd:cd04587   1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGR-LVGIVTDRDLRnRVVAEGLDP-----DTPVSEIMTPP----- 69

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30695978 503 qergLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04587  70 ----PVTIDADALVFEALLLMLERNIHHLPVVDDGRVV 103
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 430-566 7.27e-11

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 59.52  E-value: 7.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 430 VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI-RRYLSNNastiLDENTCPVSSVCTKKIsyrgqerglL 508
Cdd:cd17781   5 LTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLaRRVVASG----LDPRSTLVSSVMTPNP---------L 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30695978 509 TCYPDATVGVAKELMEARGVKQLPVV-KRGEVIhkgkrrkllGLLHydsIWTFLRDEMS 566
Cdd:cd17781  72 CVTMDTSATDALDLMVEGKFRHLPVVdDDGDVV---------GVLD---ITKCLYDAIE 118
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 409-473 3.04e-10

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 57.64  E-value: 3.04e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695978 409 FLDEETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRR 473
Cdd:cd02205  49 ALVEGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 430-540 4.36e-10

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: 57.04  E-value: 4.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 430 VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDEntcPVSSVCTKKisyrgqergLLT 509
Cdd:cd04623   5 VTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDT---PVSEIMTRD---------VVT 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 30695978 510 CYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04623  73 CTPDDTVEECMALMTERRIRHLPVVEDGKLV 103
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 425-540 6.31e-10

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: 56.68  E-value: 6.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNnaSTILDENTCPVSSVCTKKIsyrgqe 504
Cdd:cd04629   1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLE--ASYHCEPGGTVADYMSTEV------ 72

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30695978 505 rglLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04629  73 ---LTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLV 105
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
411-477 9.10e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 57.18  E-value: 9.10e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978 411 DEETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSN 477
Cdd:COG3448  65 ELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 32-358 9.91e-10

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: 9.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  32 VIKAIQAAVTLGTGCSLGPEGPSVDIGKSCANGFA--------------LMMENNRERRiALTAAGAASGIASGFNAAVA 97
Cdd:cd03685 130 LVKIVGVILSVSGGLALGKEGPMIHIGACIAAGLSqggstslrldfrwfRYFRNDRDKR-DFVTCGAAAGVAAAFGAPVG 208

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  98 GCFFAIETVLRPLRAensppFTTAMIILASVISSTVSNALL-------------GTQSAFTVPS-YDLKSAAELPLYLIL 163
Cdd:cd03685 209 GVLFSLEEVASFWNQ-----ALTWRTFFSSMIVTFTLNFFLsgcnsgkcglfgpGGLIMFDGSStKYLYTYFELIPFMLI 283

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 164 GMLCGAVSVVFSRLVTWFTKSFDFI--KDKFG--LPAIVCPALGGLGAGIIALKYPGILYWGFtnveeilhtgksasapG 239
Cdd:cd03685 284 GVIGGLLGALFNHLNHKVTRFRKRInhKGKLLkvLEALLVSLVTSVVAFPQTLLIFFVLYYFL----------------A 347

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 240 IWllaqlaaakvvaTAlckGSGLVGGLYAPSLMIGAAVGAVFGGSAAEIInraipgNAAVAQPQAYALVGMAATLASMCS 319
Cdd:cd03685 348 CW------------TF---GIAVPSGLFIPMILIGAAYGRLVGILLGSYF------GFTSIDPGLYALLGAAAFLGGVMR 406

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 30695978 320 VPLTSVLLLFELTKDYRILLPLMGAVGLAIWVPSVANQG 358
Cdd:cd03685 407 MTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEG 445
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
410-475 1.10e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 58.36  E-value: 1.10e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695978 410 LDEETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYL 475
Cdd:COG2524 141 LAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 420-540 1.17e-09

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: 56.47  E-value: 1.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 420 KVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDdFLAGILTHGDIRRYL----------SNNASTILDEntcP 489
Cdd:cd04631   1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDG-KLVGIVTSTDIMRYLgsgeafeklkTGNIHEVLNV---P 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 30695978 490 VSSVCTKKISyrgqergllTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04631  77 ISSIMKRDII---------TTTPDTDLGEAAELMLEKNIGALPVVDDGKLV 118
CBS COG0517
CBS domain [Signal transduction mechanisms];
409-475 1.58e-09

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 56.03  E-value: 1.58e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978 409 FLDEETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYL 475
Cdd:COG0517  57 LAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKAL 123
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 40-331 1.89e-08

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: 56.43  E-value: 1.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  40 VTLGT------GCSLGPEGPSVDIGKSCANGFA-LMMENNRERRIALTAAGAASGIASgFNAAVAGCFFAIE-TVLRPLR 111
Cdd:cd03682  81 VLFGTvlthlfGGSAGREGTAVQMGGSLADAFGrVFKLPEEDRRILLIAGIAAGFAAV-FGTPLAGAIFALEvLVLGRLR 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 112 AEnsppfttAMI--ILASVISSTVSNALLGTQSAF---TVPSYDLKSAAELplyLILGMLCGAVSVVFSRLVTWFTKSFD 186
Cdd:cd03682 160 YS-------ALIpcLVAAIVADWVSHALGLEHTHYhivFIPTLDPLLFVKV---ILAGIIFGLAGRLFAELLHFLKKLLK 229

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 187 -FIKDKFGLPAIVcpalgglGAGIIALKYpgilywgftnveeILHTGKSaSAPGIWLLAQLAA----------AKVVATA 255
Cdd:cd03682 230 kRIKNPYLRPFVG-------GLLIILLVY-------------LLGSRRY-LGLGTPLIEDSFFggtvypydwlLKLIFTV 288

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695978 256 LCKGSGLVGGLYAPSLMIGAAVGAVFGGsaaeIINRAIPGNAAvaqpqayalVGMAATLASMCSVPLTSVLLLFEL 331
Cdd:cd03682 289 ITLGAGFKGGEVTPLFFIGATLGNALAP----ILGLPVSLLAA---------LGFVAVFAGATNTPLACIIMGIEL 351
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 425-552 2.55e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 52.19  E-value: 2.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNAstILDenTCPVSSVCTKKisyrgqe 504
Cdd:cd04613   1 MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEE--LWD--LVVVKDLATTD------- 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30695978 505 rgLLTCYPDATVGVAKELMEARGVKQLPVVKRGEvihkgkRRKLLGLL 552
Cdd:cd04613  70 --VITVTPDDDLYTALLKFTSTNLDQLPVVDDDD------PGKVLGML 109
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 424-540 3.09e-08

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: 52.21  E-value: 3.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 424 VMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLA-GILTHGDIrrylsnnASTILDENTCP----VSSVCTKKI 498
Cdd:cd04630   4 VMKTNVVTIDGLATVREALQLMKEHNVKSLIVEKRHEHDAyGIVTYTDI-------LKKVIAEDRDPdlvnVYEIMTKPA 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30695978 499 syrgqerglLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04630  77 ---------ISVSPDLDIKYAARLMARFNLKRAPVIENNELI 109
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 425-561 8.55e-08

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: 50.62  E-value: 8.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI-RRYLSNNastiLDENTCPVSSVCTkkisyrgq 503
Cdd:cd17775   1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIvVEVVAKG----LDPKDVTVGDIMS-------- 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30695978 504 eRGLLTCYPDATVGVAKELMEARGVKQLPVV-KRGEvihkgkrrkLLGLLHYDSIWTFL 561
Cdd:cd17775  69 -ADLITAREDDGLFEALERMREKGVRRLPVVdDDGE---------LVGIVTLDDILELL 117
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 410-478 2.81e-07

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 49.44  E-value: 2.81e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30695978 410 LDEETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRYLSNN 478
Cdd:COG2905  56 LAEGLDPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGK-LVGIVSITDLLRALSEE 123
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 164-351 3.42e-07

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: 52.57  E-value: 3.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 164 GMLCGAVSVVFSRLVTWFTK-------SFDFIKDKFGLPAIVCPALGGLGAGIIalkypgILYWGFTNVEEILHTGKSAS 236
Cdd:cd00400   1 GVLSGLGAVLFRLLIELLQNllfgglpGELAAGSLSPLYILLVPVIGGLLVGLL------VRLLGPARGHGIPEVIEAIA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 237 APGIWLLAQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGgsaaEIINraipgnaaVAQPQAYALV--GMAATL 314
Cdd:cd00400  75 LGGGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLG----RRLR--------LSRNDRRILVacGAAAGI 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30695978 315 ASMCSVPLTSVLLLFE-LTKDYRI--LLPLMGAVGLAIWV 351
Cdd:cd00400 143 AAAFNAPLAGALFAIEvLLGEYSVasLIPVLLASVAAALV 182
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
394-477 4.39e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 49.14  E-value: 4.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 394 DSLE--LTVIENPDHNSF--LDEETIL-------------EDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVV 456
Cdd:COG4109  34 DTVEdaLELLEKTGHSRFpvVDENGRLvgivtskdilgkdDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVV 113

                        90       100
                ....*....|....*....|.
gi 30695978 457 DDDDFLAGILTHGDIRRYLSN 477
Cdd:COG4109 114 DDDGRLLGIISRQDVLKALQK 134
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 432-540 5.18e-07

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 48.18  E-value: 5.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 432 VSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRrylsnnasTILDENTcPVSSVCTKKisyrgqERgLLTCY 511
Cdd:cd04601   7 LSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIR--------FETDLST-PVSEVMTPD------ER-LVTAP 70

                        90       100       110
                ....*....|....*....|....*....|
gi 30695978 512 PDATVGVAKELMEARGVKQLPVV-KRGEVI 540
Cdd:cd04601  71 EGITLEEAKEILHKHKIEKLPIVdDNGELV 100
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 427-552 5.41e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 48.28  E-value: 5.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 427 KNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNAST--ILDENtcpvssvctkkisyrgqe 504
Cdd:cd04583   2 TNPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNYRKAKKVgeIMERD------------------ 63

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30695978 505 rgLLTCYPDATVGVAKELMEARGVKQLPVVKrgevihkgKRRKLLGLL 552
Cdd:cd04583  64 --VFTVKEDSLLRDTVDRILKRGLKYVPVVD--------EQGRLVGLV 101
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 425-537 5.80e-07

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 48.11  E-value: 5.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRYLSNNAstildentcpVSSVCTKKIsyrgqe 504
Cdd:cd04599   1 MTRNPITISPLDSVARAAALMERQRIGGLPVVENGK-LVGIITSRDVRRAHPNRL----------VADAMSRNV------ 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 30695978 505 rglLTCYPDATVGVAKELMEARGVKQLPVVKRG 537
Cdd:cd04599  64 ---VTISPEASLWEAKELMEEHGIERLVVVEEG 93
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 430-495 1.99e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 46.86  E-value: 1.99e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978 430 VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI-RRYLSNNastiLDENTCPVSSVCT 495
Cdd:cd17782   5 PLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVvLRVLAAG----LDPATTSVVRVMT 67
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 424-540 4.65e-06

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


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 45.64  E-value: 4.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 424 VMSKNYVKVSSGTTLREA-RNILKESHqnciM---VVDDDDfLAGILTHGDIRrylsnNASTILDENTcPVSSVCTKKis 499
Cdd:cd04801   2 IMTPEVVTVTPEMTVSELlDRMFEEKH----LgypVVENGR-LVGIVTLEDIR-----KVPEVEREAT-RVRDVMTKD-- 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30695978 500 yrgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04801  69 -------VITVSPDADAMEALKLMSQNNIGRLPVVEDGELV 102
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 203-351 8.35e-06

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: 48.31  E-value: 8.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   203 GGLGAGIIALKY-PGILYWGFTNVEEILHTGKsasaPGIWLLaqLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVF 281
Cdd:pfam00654   1 GGLLAGWLVKRFaPEAAGSGIPEVKAALHGGR----GPLPLR--VLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695978   282 GgsaaEIINRAIPgnaavaqPQAYALV--GMAATLASMCSVPLTSVLLLFELTK---DYRILLPLMGAVGLAIWV 351
Cdd:pfam00654  75 G----RRLFRLSP-------RDRRILLaaGAAAGLAAAFNAPLAGVLFALEELSrsfSLRALIPVLLASVVAALV 138
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
415-494 1.41e-05

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 47.90  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  415 ILEDLK--VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI-RRYLSNNASTILDENTCPVS 491
Cdd:PRK14869  62 LIEDVKpqVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLaRAYMDILDPEILSKSPTSLE 141


                 ...
gi 30695978  492 SVC 494
Cdd:PRK14869 142 NII 144
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 425-540 1.66e-05

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


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 44.32  E-value: 1.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLRE-ARNILKeshqNCI--MVVDDDDFLAGILTHGDIRRylsnnASTILDEntcPVSSVCTKKISyr 501
Cdd:cd17776   1 MTTDVVTVDADASLEDaAERMLR----NRVgsVVVTDDGTPAGILTETDALH-----AGYATDD---PFSEIPVRAVA-- 66

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30695978 502 gqERGLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd17776  67 --SRPLVTISPTATLREAAERMVDEGVKKLPVVDGLDLV 103
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 415-475 2.21e-05

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 44.33  E-value: 2.21e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695978 415 ILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRYL 475
Cdd:cd04584  70 LLSKIPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGK-LVGIITETDILRAF 129
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 427-540 4.00e-05

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


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 43.18  E-value: 4.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 427 KNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLsnnastILDENT--CPVSSVCTKKIsyrgqe 504
Cdd:cd17784   2 KNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNL------ILDKYElgTTVEEVMVKDV------ 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30695978 505 rglLTCYPDATVGVAKELMEARG-----VKQLPVVKRGEVI 540
Cdd:cd17784  70 ---ATVHPDETLLEAIKKMDSNApdeeiINQLPVVDDGKLV 107
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 ...
 425-540 6.47e-05

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: 42.69  E-value: 6.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSnNASTILDEntcPVSSVCTkkisyrgqe 504
Cdd:cd17771   2 IRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVA-LPQIDLDA---PISEVMT--------- 68

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30695978 505 RGLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd17771  69 PDPVRLPPSASAFEAALLMAEHGFRHVCVVDNGRLV 104
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 424-561 8.58e-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: 42.17  E-value: 8.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 424 VMSKNYVKVSSGTTLREARN--ILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNN-ASTILDENTCPVSSvctkkisy 500
Cdd:cd04639   2 AMVTEFPIVDADLTLREFADdyLIGKKSWREFLVTDEAGRLVGLITVDDLRAIPTSQwPDTPVRELMKPLEE-------- 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695978 501 rgqergLLTCYPDATVGVAKELMEARGVKQLPVVKRGEVihkgkrrkLLGLLHYDSIWTFL 561
Cdd:cd04639  74 ------IPTVAADQSLLEVVKLLEEQQLPALAVVSENGT--------LVGLIEKEDIIELL 120
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 406-476 8.67e-05

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


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 42.41  E-value: 8.67e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695978 406 HNSFLDEETIleDLKVMRVMSKNYVKVSSGTTLREA-----RNILKESHQNCIMVVDDDDfLAGILTHGDIRRYLS 476
Cdd:cd17784  48 HNLILDKYEL--GTTVEEVMVKDVATVHPDETLLEAikkmdSNAPDEEIINQLPVVDDGK-LVGIISDGDIIRAIK 120
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 430-475 1.25e-04

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 39.80  E-value: 1.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 30695978    430 VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYL 475
Cdd:smart00116   3 VTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 430-538 1.50e-04

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 41.93  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 430 VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI------------RRYLSNNASTILDEntcPVSSVCTkk 497
Cdd:cd04632   5 ITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIvdfvvrpgtktrGGDRGGEKERMLDL---PVYDIMS-- 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30695978 498 isyrgqeRGLLTCYPDATVGVAKELMEARGVKQLPVVKRGE 538
Cdd:cd04632  80 -------SPVVTVTRDATVADAVERMLENDISGLVVTPDDN 113
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 426-534 1.50e-04

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: 41.36  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 426 SKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRYLSNNastilDENTcPVSSVCTKKIsyrgqer 505
Cdd:cd04588   1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDGK-LVGIVTLTDIAKALAEG-----KENA-KVKDIMTKDV------- 66

                        90       100
                ....*....|....*....|....*....
gi 30695978 506 glLTCYPDATVGVAKELMEARGVKQLPVV 534
Cdd:cd04588  67 --ITIDKDEKIYDAIRLMNKHNIGRLIVV 93
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 423-491 1.69e-04

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


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 41.55  E-value: 1.69e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30695978 423 RVMSKNYVKVSSGTTLREARNILKESHQ-----NCIMVVDDDDFLAGILThgdIRRYLSNNASTILDE--NTCPVS 491
Cdd:cd04606   5 RLMTTEFVAVRPDWTVEEALEYLRRLAPdpetiYYIYVVDEDRRLLGVVS---LRDLLLADPDTKVSDimDTDVIS 77
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 371-477 2.54e-04

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 43.89  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978  371 RGYSSLSPSERKTEGvwrhtdnadSLELTVIENPDHNSFLDEETILEDlkVMRVMSKNYVkVSSGTTLREARNILKESHQ 450
Cdd:PLN02274 129 RGFSSVCVTETGTMG---------SKLLGYVTKRDWDFVNDRETKLSE--VMTSDDDLVT-APAGIDLEEAEAVLKDSKK 196

                         90       100
                 ....*....|....*....|....*..
gi 30695978  451 NCIMVVDDDDFLAGILTHGDIRRYLSN 477
Cdd:PLN02274 197 GKLPLVNEDGELVDLVTRTDVKRVKGY 223
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 432-540 2.62e-04

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 40.56  E-value: 2.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 432 VSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRylsnnaSTILDENTCPVSSVCTKKIsyrgqerglLTCY 511
Cdd:cd04595   7 VSPDTTIEEARKIMLRYGHTGLPVVEDGK-LVGIISRRDVDK------AKHHGLGHAPVKGYMSTNV---------ITID 70

                        90       100
                ....*....|....*....|....*....
gi 30695978 512 PDATVGVAKELMEARGVKQLPVVKRGEVI 540
Cdd:cd04595  71 PDTSLEEAQELMVEHDIGRLPVVEEGKLV 99
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 418-497 3.28e-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: 40.59  E-value: 3.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 418 DLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYLSNNASTILDentcPVSSVCTKK 497
Cdd:cd04608   1 DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSD----PVSKAMYKQ 76
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 418-471 3.67e-04

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 43.15  E-value: 3.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 30695978   418 DLKVMRVMSK-NYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI 471
Cdd:pfam00478 138 SQPVSEVMTKeNLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 418-475 4.37e-04

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 40.67  E-value: 4.37e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30695978 418 DLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVdDDDFLAGILTHGDIRRYL 475
Cdd:cd04631  74 NVPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVV-DDGKLVGIITERDILRAI 130
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 420-540 4.83e-04

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: 40.39  E-value: 4.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 420 KVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRRYLSNNAsTILDENTCPVSSVCTKKIS 499
Cdd:cd17778   1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK-LVGIVTAMDIVKYFGSHE-AKKRLTTGDIDEAYSTPVE 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30695978 500 YRGQERgLLTCYPDATVGVAKELMEARGVKQLPVV-KRGEVI 540
Cdd:cd17778  79 EIMSKE-VVTIEPDADIAEAARLMIKKNVGSLLVVdDEGELK 119
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 425-534 5.33e-04

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 42.76  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978   425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRrylsnnastILDENTCPVSSVCTKKisyrgqe 504
Cdd:pfam00478  86 MITDPVTLSPDATVADALALMERYGISGVPVVDDGK-LVGIVTNRDLR---------FETDLSQPVSEVMTKE------- 148

                          90       100       110
                  ....*....|....*....|....*....|
gi 30695978   505 rGLLTCYPDATVGVAKELMEARGVKQLPVV 534
Cdd:pfam00478 149 -NLVTAPEGTTLEEAKEILHKHKIEKLPVV 177
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 164-355 5.68e-04

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: 42.53  E-value: 5.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 164 GMLCGAVSVVFSRLV----TWFTKSFDFIKDKFG--LPAIVCPALGGLGAG-IIALKYPGILYWGFTNVEEILhtgkSAS 236
Cdd:cd01031   2 GLLAGLVAVLFRLGIdklgNLRLSLYDFAANNPPllLVLPLISAVLGLLAGwLVKKFAPEAKGSGIPQVEGVL----AGL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 237 APGIWLlaQLAAAKVVATALCKGSGLVGGLYAPSLMIGAAVGAVFGGsaaeiINRAIPGnaavaqpQAYALV--GMAATL 314
Cdd:cd01031  78 LPPNWW--RVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVSK-----WFKTSPE-------ERRQLIaaGAAAGL 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30695978 315 ASMCSVPLTSVLLLFE-LTKDYRILLpLMGAVGLAIWVPSVA 355
Cdd:cd01031 144 AAAFNAPLAGVLFVLEeLRHSFSPLA-LLTALVASIAADFVS 184
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 417-473 6.32e-04

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 39.70  E-value: 6.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30695978 417 EDLKVMRVMSKNY--VKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRR 473
Cdd:cd04601  52 LSTPVSEVMTPDErlVTAPEGITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK 110
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 418-474 6.79e-04

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 40.01  E-value: 6.79e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978 418 DLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRY 474
Cdd:cd04632  71 DLPVYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 421-475 8.21e-04

signal transduction protein with CBS domains; 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: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 39.91  E-value: 8.21e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30695978 421 VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRRYL 475
Cdd:cd17779  82 VREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 400-473 1.07e-03

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


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 38.86  E-value: 1.07e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695978 400 VIENPDhnsfldEETILedlkvmRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRR 473
Cdd:cd04638  48 LLRNPD------EEQIA------LLMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDK-LVGIVTVADLVR 108
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 453-550 1.27e-03

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 39.01  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 453 IMVVDDDDFLAGILTHGDIRRYLSNNAstilDENTCPVSSVCTK--KIsyrgqerglLTCYPDATVGVAKELMEARGVKQ 530
Cdd:cd04617  30 LFVVDEEGYLVGVVSRKDLLKATLGGQ----DLEKTPVSMIMTRmpNI---------VTVTPDDSVLEAARKLIEHEIDS 96

                        90       100
                ....*....|....*....|
gi 30695978 531 LPVVKRGEvihkgKRRKLLG 550
Cdd:cd04617  97 LPVVEKED-----GKLKVVG 111
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 496-540 1.57e-03

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: 38.67  E-value: 1.57e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30695978 496 KKISYRGQERGLLTCYPDATVGVAKELMEARGVKQLPVVKR-GEVI 540
Cdd:cd04608   1 DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEdGRVV 46
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 416-471 1.88e-03

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 38.28  E-value: 1.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30695978 416 LEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI 471
Cdd:cd04588  53 KENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDI 108
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 417-467 2.49e-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: 37.88  E-value: 2.49e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 30695978 417 EDLKVMRVMSKNYVKVSSGTTLREA-RNILKESHQNcIMVVDDDDFLAGILT 467
Cdd:cd04583  52 KAKKVGEIMERDVFTVKEDSLLRDTvDRILKRGLKY-VPVVDEQGRLVGLVT 102
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 421-554 2.53e-03

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: 38.47  E-value: 2.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 421 VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLaGILTHGDIRRYLSNNastilDENTcPVSSVCTkkisy 500
Cdd:cd04611   7 VGSAMNRSPLVLPGDASLAEAARRMRSHRADAAVIECPDGGL-GILTERDLVRFIARH-----PGNT-PVGELAS----- 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30695978 501 rgqeRGLLTCYPDATVGVAKELMEARGVKQLPVVkrgevihkGKRRKLLGLLHY 554
Cdd:cd04611  75 ----RPLLTVGAEDSLIHARDLLIDHRIRHLAVV--------DEDGQVTGLLGF 116
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
421-467 2.77e-03

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 40.66  E-value: 2.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 30695978  421 VMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILT 467
Cdd:PRK07807 150 VRDVMSTDLVTLPAGTDPREAFDLLEAARVKLAPVVDADGRLVGVLT 196
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 420-473 2.84e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 38.61  E-value: 2.84e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 30695978 420 KVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDIRR 473
Cdd:cd17789  87 VVGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVR 140
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 425-534 2.98e-03

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 37.69  E-value: 2.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLaGILTHGDIRRYLSNNAstildentcpVSSVCTkkisyrgqe 504
Cdd:cd04610   1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVV-GYVTAKDLLGKDDDEK----------VSEIMS--------- 60

                        90       100       110
                ....*....|....*....|....*....|
gi 30695978 505 RGLLTCYPDATVGVAKELMEARGVKQLPVV 534
Cdd:cd04610  61 RDTVVADPDMDITDAARVIFRSGISKLPVV 90
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 490-557 3.19e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.04  E-value: 3.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30695978   490 VSSVCTKKIsyrgqerglLTCYPDATVGVAKELMEARGVKQLPVVKRGEvihkgkrrKLLGLLHYDSI 557
Cdd:pfam00571   1 VKDIMTKDV---------VTVSPDTTLEEALELMREHGISRLPVVDEDG--------KLVGIVTLKDL 51
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 411-471 4.16e-03

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


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 37.31  E-value: 4.16e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30695978 411 DEETILEDLkvmrvMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI 471
Cdd:cd04606  62 DPDTKVSDI-----MDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDV 117
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 507-540 4.17e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 35.57  E-value: 4.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 30695978    507 LLTCYPDATVGVAKELMEARGVKQLPVV-KRGEVI 540
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLV 36
MFS_NIMT_like cd17409
2-nitroimidazole transporter and similar proteins of the Major Facilitator Superfamily of ...
 260-366 5.44e-03

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


Pssm-ID: 340967 [Multi-domain]  Cd Length: 374  Bit Score: 39.17  E-value: 5.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 260 SGLVGGLYAPSLMIGA--AVGAVFGGSaaeIINRAIPGNAAVAQpQAYALV-GMAATLASMCSVPLTSVLLL-FELTKDY 335
Cdd:cd17409  83 TGSVWALYLGTAIIGAgiAIGNVLLPS---LLKRDFPARVATLT-GAYALTmGVGAALGSALVVPLAQVLAFgWQLALGA 158

                        90       100       110
                ....*....|....*....|....*....|.
gi 30695978 336 RILLPLmgaVGLAIWVPSVANQGKESDSSEG 366
Cdd:cd17409 159 FLVFPL---VAALIWLPQLRRHTSPAADTAK 186
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
399-471 5.91e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 39.43  E-value: 5.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30695978  399 TVIENPdHNSFLDEETILEDLKVMRVMSK-NYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI 471
Cdd:PRK14869 227 TVISTP-YDTFTTARLINQSIPVSYIMTTeDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHL 299
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 418-476 6.79e-03

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 36.73  E-value: 6.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30695978 418 DLKVMRVMSKNYVKVSSGTTLREARNILKE---SHqncIMVVDDDDFLAGILTHGDIRRYLS 476
Cdd:cd09836  58 DTPVEEIMTKNLVTVSPDESIYEAAELMREhniRH---LPVVDGGGKLVGVISIRDLARELS 116
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 410-466 6.86e-03

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: 36.98  E-value: 6.86e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978 410 LDEETILEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGIL 466
Cdd:cd04604  61 LEKGLDILNLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGIL 117
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 407-467 7.07e-03

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


Pssm-ID: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 37.09  E-value: 7.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30695978 407 NSFLDEETI----LEDLKVMRVMSKNYVKVSSGTTLREARNILkeSHQNCIMVVDDDDFLAGILT 467
Cdd:cd04643  53 DAILGLERIefekLSELKVEEVMNTDVPTVSPDDDLEEVLHLL--VDHPFLCVVDEDGYFLGIIT 115
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 416-471 7.23e-03

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 36.63  E-value: 7.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30695978 416 LEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGDI 471
Cdd:cd04622  57 PNTTTVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 425-470 8.53e-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: 36.77  E-value: 8.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30695978 425 MSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDFLAGILTHGD 470
Cdd:cd04600   1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLAD 46
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
423-564 8.73e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 38.89  E-value: 8.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30695978 423 RVMSKNYVKVSSGTTLREARNILKESHQ-----NCIMVVDDDDFLAGILThgdIRRYLSNNASTildentcPVSSVCTKK 497
Cdd:COG2239 133 RLMTTEFVAVREDWTVGEALRYLRRQAEdpetiYYIYVVDDDGRLVGVVS---LRDLLLADPDT-------KVSDIMDTD 202

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30695978 498 IsyrgqerglLTCYPDATVGVAKELMEARGVKQLPVVkrgevihkGKRRKLLGLLHYDSIWTFLRDE 564
Cdd:COG2239 203 V---------ISVPADDDQEEVARLFERYDLLALPVV--------DEEGRLVGIITVDDVVDVIEEE 252
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 416-473 9.69e-03

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


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 36.23  E-value: 9.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30695978 416 LEDLKVMRVMSKNYVKVSSGTTLREARNILKESHQNCIMVVDDDDfLAGILTHGDIRR 473
Cdd:cd17776  57 FSEIPVRAVASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLD-LVGILTATDIIR 113
 
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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