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Conserved domains on  [gi|4557473|ref|NP_000075|]
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H(+)/Cl(-) exchange transporter 5 isoform b [Homo sapiens]

Protein Classification

chloride channel protein( domain architecture ID 10132694)

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

CATH:  1.10.3080.10
Gene Ontology:  GO:0006821|GO:0005247|GO:0055085
PubMed:  11182894|9207144|9046241
SCOP:  4003598

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 72-570 0e+00

ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 was initially cloned from rat kidney. Expression of ClC-3 produces outwardly-rectifying Cl currents that are inhibited by protein kinase C activation. It has been suggested that ClC-3 may be a ubiquitous swelling-activated Cl channel that has very similar characteristics to those of native volume-regulated Cl currents. The function of ClC-4 is unclear. Studies of human ClC-4 have revealed that it gives rise to Cl currents that rapidly activate at positive voltages, and are sensitive to extracellular pH, with currents decreasing when pH falls below 6.5. ClC-4 is broadly distributed, especially in brain and heart. ClC-5 is predominantly expressed in the kidney, but can be found in the brain and liver. Mutations in the ClC-5 gene cause certain hereditary diseases, including Dent's disease, an X-chromosome linked syndrome characterised by proteinuria, hypercalciuria, and kidney stones (nephrolithiasis), leading to progressive renal failure. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl- and I-) channel proteins, that perform a variety of functions including cell volume regulation, the membrane potential stabilization, transepithelial chloride transport and charge compensation necessary for the acidification of intracellular organelles.


:

Pssm-ID: 239656  Cd Length: 445  Bit Score: 739.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   72 AGLIDISAHWMTDLKEGICtggfwfnhehccwnsehvtfeerdkcpewnswsqliistdegafayivNYFMYVLWALLFA 151
Cdd:cd03684   8 AGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYVLLALLFA 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  152 FLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCFNK 231
Cdd:cd03684  40 FIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFPK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  232 YRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEFH 311
Cdd:cd03684 120 YRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLVLFEVEYD 199

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  312 TPWHLFELVPFILLGIFGGLWGALFIRTNIAWCRKRKTTQLGKYPVIEVLVVTAITAILAFPNEYTRMSTSELISELFND 391
Cdd:cd03684 200 RDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTELLELLFNE 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  392 CGLLDSSKLCDYenrfntskggelPDRPAGVGVYSAMWQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGV 471
Cdd:cd03684 280 CEPGDDNSLCCY------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGI 347

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  472 GMEQLAYYHQEWtVFNSWCSQGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADA 551
Cdd:cd03684 348 LVEQLAYSYPDS-IFFACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWVADA 426

                       490
                ....*....|....*....
gi 4557473  552 LGREGIYDAHIRLNGYPFL 570
Cdd:cd03684 427 IGKEGIYDAHIHLNGYPFL 445
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 581-731 7.39e-46

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


:

Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 159.22  E-value: 7.39e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  581 LAMDVMKPRrndplLTVLTQDsMTVEDVETIISETTYSGFPVVVSRESQRLVGFVLRRDLIISIENarkkqdgvvstsii 660
Cdd:cd04591   1 TAEDVMRPP-----LTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557473  661 yftehspplppytpptlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKH 731
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 72-570 0e+00

ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 was initially cloned from rat kidney. Expression of ClC-3 produces outwardly-rectifying Cl currents that are inhibited by protein kinase C activation. It has been suggested that ClC-3 may be a ubiquitous swelling-activated Cl channel that has very similar characteristics to those of native volume-regulated Cl currents. The function of ClC-4 is unclear. Studies of human ClC-4 have revealed that it gives rise to Cl currents that rapidly activate at positive voltages, and are sensitive to extracellular pH, with currents decreasing when pH falls below 6.5. ClC-4 is broadly distributed, especially in brain and heart. ClC-5 is predominantly expressed in the kidney, but can be found in the brain and liver. Mutations in the ClC-5 gene cause certain hereditary diseases, including Dent's disease, an X-chromosome linked syndrome characterised by proteinuria, hypercalciuria, and kidney stones (nephrolithiasis), leading to progressive renal failure. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl- and I-) channel proteins, that perform a variety of functions including cell volume regulation, the membrane potential stabilization, transepithelial chloride transport and charge compensation necessary for the acidification of intracellular organelles.


Pssm-ID: 239656  Cd Length: 445  Bit Score: 739.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   72 AGLIDISAHWMTDLKEGICtggfwfnhehccwnsehvtfeerdkcpewnswsqliistdegafayivNYFMYVLWALLFA 151
Cdd:cd03684   8 AGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYVLLALLFA 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  152 FLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCFNK 231
Cdd:cd03684  40 FIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFPK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  232 YRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEFH 311
Cdd:cd03684 120 YRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLVLFEVEYD 199

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  312 TPWHLFELVPFILLGIFGGLWGALFIRTNIAWCRKRKTTQLGKYPVIEVLVVTAITAILAFPNEYTRMSTSELISELFND 391
Cdd:cd03684 200 RDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTELLELLFNE 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  392 CGLLDSSKLCDYenrfntskggelPDRPAGVGVYSAMWQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGV 471
Cdd:cd03684 280 CEPGDDNSLCCY------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGI 347

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  472 GMEQLAYYHQEWtVFNSWCSQGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADA 551
Cdd:cd03684 348 LVEQLAYSYPDS-IFFACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWVADA 426

                       490
                ....*....|....*....
gi 4557473  552 LGREGIYDAHIRLNGYPFL 570
Cdd:cd03684 427 IGKEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 150-550 1.86e-93

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: 294.84  E-value: 1.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    150 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCF 229
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    230 NkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 309
Cdd:pfam00654  79 F--RLSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    310 FHTPWHLFELVPFILLGIFGGLWGALFIRTNIaWCRKRKTTQLGKYPVIEVLVVTAITAILAFPNEYTRMSTSELISELF 389
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    390 NDCGLLdssklcdyenrfntskggelpdrpagvgvysamWQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLL 469
Cdd:pfam00654 232 NGNTSL---------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAF 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    470 GVGMEQLAyyhqewtvfnswcsqGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVA 549
Cdd:pfam00654 279 GLLLALLF---------------PIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVS 343


                  .
gi 4557473    550 D 550
Cdd:pfam00654 344 R 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
133-563 2.85e-55

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 195.36  E-value: 2.85e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  133 AFAYIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLVIKTITLVLAVSSGLSLGKEG 212
Cdd:COG0038  43 AAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREG 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  213 PLVHVACCCGNILCHCFnkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTL 292
Cdd:COG0038 121 PSVQIGAAIGSLLGRLL---RLSPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVS 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  293 RSInpFGNSrlVLFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTNIAWcrKRKTTQLGKYPVIEVLVVTAITAILA- 371
Cdd:COG0038 198 RLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLLLKV--ERLFKRLKLPPWLRPAIGGLLVGLLGl 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  372 -FPnEYTRMSTsELISELFNdcglldssklcdyenrfntskgGELPdrpagvgvysaMWQLALTLILKIVITIFTFGMKI 450
Cdd:COG0038 272 fLP-QVLGSGY-GLIEALLN----------------------GELS-----------LLLLLLLLLLKLLATALTLGSGG 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  451 PSGLFIPSMAVGAIAGRLLGVGMEQLAyyhqewtvfnswcsqGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTG 530
Cdd:COG0038 317 PGGIFAPSLFIGALLGAAFGLLLNLLF---------------PGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTG 381

                       410       420       430
                ....*....|....*....|....*....|...
gi 4557473  531 GLEYIVPLMAAAMTSKWVADALGREGIYDAHIR 563
Cdd:COG0038 382 SYSLLLPLMIACVIAYLVSRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 581-731 7.39e-46

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


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 159.22  E-value: 7.39e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  581 LAMDVMKPRrndplLTVLTQDsMTVEDVETIISETTYSGFPVVVSRESQRLVGFVLRRDLIISIENarkkqdgvvstsii 660
Cdd:cd04591   1 TAEDVMRPP-----LTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557473  661 yftehspplppytpptlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKH 731
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
149-560 1.75e-26

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 113.06  E-value: 1.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   149 LFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHC 228
Cdd:PRK05277  53 VLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVLDI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   229 FNkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFTLRSINpfgNSRLVLF 306
Cdd:PRK05277 131 FR--LRSDEARHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN---GEQAVIE 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   307 YVEFHTPwHLFELVPFILLGIFGGLWGALFIRTNIA---WCRKRKTTQLGKYPVIeVLVVTAITAILAFPNEYTRMSTSE 383
Cdd:PRK05277 206 VGKFSAP-PLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRWVLM-GGAVGGLCGLLGLLAPAAVGGGFN 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   384 LISELFNdcglldssklcdyenrfntskggelpdrpagvGVYSAMwQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGA 463
Cdd:PRK05277 284 LIPIALA--------------------------------GNFSIG-MLLFIFVARFITTLLCFGSGAPGGIFAPMLALGT 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   464 IAGRLLGVGMEQLayyHQEWTvfnswcsqgadcITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAM 543
Cdd:PRK05277 331 LLGLAFGMVAAAL---FPQYH------------IEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCL 395

                        410
                 ....*....|....*..
gi 4557473   544 TSKWVADALGREGIYDA 560
Cdd:PRK05277 396 GATLLAQFLGGKPIYSA 412
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
497-732 9.58e-16

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 76.46  E-value: 9.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  497 ITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVAdALGREGIYDAHIRLNGYPFLEAKEEF 576
Cdd:COG2524   4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  577 AHKTLAMDVMkprrNDPLLTVltQDSMTVEDVETIISETTYSGFPVVvsrESQRLVGFVLRRDLIISIENARKKQDgvvs 656
Cdd:COG2524  83 VLKMKVKDIM----TKDVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557473  657 tsiiyftehspplppytpptLKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDVLKHI 732
Cdd:COG2524 150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 687-733 2.48e-08

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 50.59  E-value: 2.48e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 4557473     687 PFTVTDLTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDVLKHIA 733
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 679-733 5.00e-06

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: 44.13  E-value: 5.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557473    679 LRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDVLKHIA 733
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 680-728 5.45e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 39.95  E-value: 5.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4557473   680 RNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDV 728
Cdd:PTZ00314  99 ENGFIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
 
Name Accession Description Interval E-value
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 72-570 0e+00

ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 was initially cloned from rat kidney. Expression of ClC-3 produces outwardly-rectifying Cl currents that are inhibited by protein kinase C activation. It has been suggested that ClC-3 may be a ubiquitous swelling-activated Cl channel that has very similar characteristics to those of native volume-regulated Cl currents. The function of ClC-4 is unclear. Studies of human ClC-4 have revealed that it gives rise to Cl currents that rapidly activate at positive voltages, and are sensitive to extracellular pH, with currents decreasing when pH falls below 6.5. ClC-4 is broadly distributed, especially in brain and heart. ClC-5 is predominantly expressed in the kidney, but can be found in the brain and liver. Mutations in the ClC-5 gene cause certain hereditary diseases, including Dent's disease, an X-chromosome linked syndrome characterised by proteinuria, hypercalciuria, and kidney stones (nephrolithiasis), leading to progressive renal failure. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl- and I-) channel proteins, that perform a variety of functions including cell volume regulation, the membrane potential stabilization, transepithelial chloride transport and charge compensation necessary for the acidification of intracellular organelles.


Pssm-ID: 239656  Cd Length: 445  Bit Score: 739.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   72 AGLIDISAHWMTDLKEGICtggfwfnhehccwnsehvtfeerdkcpewnswsqliistdegafayivNYFMYVLWALLFA 151
Cdd:cd03684   8 AGLIDIIASWLSDLKEGYC------------------------------------------------NYIIYVLLALLFA 39

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  152 FLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCFNK 231
Cdd:cd03684  40 FIAVLLVKVVAPYAAGSGIPEIKTILSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISRLFPK 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  232 YRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGNSRLVLFYVEFH 311
Cdd:cd03684 120 YRRNEAKRREILSAAAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSLNPFGTGRLVLFEVEYD 199

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  312 TPWHLFELVPFILLGIFGGLWGALFIRTNIAWCRKRKTTQLGKYPVIEVLVVTAITAILAFPNEYTRMSTSELISELFND 391
Cdd:cd03684 200 RDWHYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYPVLEVLLVALITALISFPNPYTRLDMTELLELLFNE 279

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  392 CGLLDSSKLCDYenrfntskggelPDRPAGVGVYSAMWQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGV 471
Cdd:cd03684 280 CEPGDDNSLCCY------------RDPPAGDGVYKALWSLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGALFGRIVGI 347

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  472 GMEQLAYYHQEWtVFNSWCSQGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADA 551
Cdd:cd03684 348 LVEQLAYSYPDS-IFFACCTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWVADA 426

                       490
                ....*....|....*....
gi 4557473  552 LGREGIYDAHIRLNGYPFL 570
Cdd:cd03684 427 IGKEGIYDAHIHLNGYPFL 445
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 136-559 5.25e-133

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: 399.80  E-value: 5.25e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  136 YIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLV 215
Cdd:cd01036  33 YLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLV 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  216 HVACCCGNILCHCFNKYR----------KNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAA 285
Cdd:cd01036 113 HLGAMIGAGLLQGRSRTLgchvhlfqlfRNPRDRRDFLVAGAAAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAA 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  286 LVAAFTLRSINPFGNSR----------LVLFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTNIAWC---RKRKTTQL 352
Cdd:cd01036 193 LVSAFVIQIYNSFNSGFelldrssamfLSLTVFELHVPLNLYEFIPTVVIGVICGLLAALFVRLSIIFLrwrRRLLFRKT 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  353 GKYPVIEVLVVTAITAILAFPneytrmstseliselfndcglldssklcdyenrfntskggelpdrpagvgvysamWQLA 432
Cdd:cd01036 273 ARYRVLEPVLFTLIYSTIHYA-------------------------------------------------------PTLL 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  433 LTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGVGMEQLAYYHqewtvfnSWCSQGADCITPGLYAMVGAAACLG 512
Cdd:cd01036 298 LFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLVGLLVHRIAVAG-------IGAESATLWADPGVYALIGAAAFLG 370

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 4557473  513 GVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADALGrEGIYD 559
Cdd:cd01036 371 GTTRLTFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFC-ESLYH 416
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 150-550 1.86e-93

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: 294.84  E-value: 1.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    150 FAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHCF 229
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGG--RGPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    230 NkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSInpFGNSrlVLFYVE 309
Cdd:pfam00654  79 F--RLSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLI--FGNS--PLFSVG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    310 FHTPWHLFELVPFILLGIFGGLWGALFIRTNIaWCRKRKTTQLGKYPVIEVLVVTAITAILAFPNEYTRMSTSELISELF 389
Cdd:pfam00654 153 EPGSLSLLELPLFILLGILCGLLGALFNRLLL-KVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQLLF 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    390 NDCGLLdssklcdyenrfntskggelpdrpagvgvysamWQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLL 469
Cdd:pfam00654 232 NGNTSL---------------------------------SLLLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAF 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    470 GVGMEQLAyyhqewtvfnswcsqGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVA 549
Cdd:pfam00654 279 GLLLALLF---------------PIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTGSLQLLLPLMLAVLIAYAVS 343


                  .
gi 4557473    550 D 550
Cdd:pfam00654 344 R 344
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 136-570 1.26e-90

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: 291.48  E-value: 1.26e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  136 YIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLV 215
Cdd:cd03685  74 LFTAFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMI 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  216 HVACCCGNILC---------HCFN-KYRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAA 285
Cdd:cd03685 154 HIGACIAAGLSqggstslrlDFRWfRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSS 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  286 LVAAFTLRSINPFGNSR---------LVLFYVeFHTP--WHLFELVPFILLGIFGGLWGALF--IRTNIAWCRKRKTTQL 352
Cdd:cd03685 234 MIVTFTLNFFLSGCNSGkcglfgpggLIMFDG-SSTKylYTYFELIPFMLIGVIGGLLGALFnhLNHKVTRFRKRINHKG 312

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  353 GKYPVIEVLVVTAITAILAFpneytrmstseliselfndcglldssklcdyenrfntskggelpdrpagvgvysaMWQLA 432
Cdd:cd03685 313 KLLKVLEALLVSLVTSVVAF-------------------------------------------------------PQTLL 337

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  433 LTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGVGMEQlaYYHQEWtvfnswcsqgadcITPGLYAMVGAAACLG 512
Cdd:cd03685 338 IFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGS--YFGFTS-------------IDPGLYALLGAAAFLG 402

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557473  513 GVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADALgREGIYDAHIRLNGYPFL 570
Cdd:cd03685 403 GVMRMTVSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYF-NEGIYDIIIQLKGVPFL 459
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 134-570 1.67e-83

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: 271.43  E-value: 1.67e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  134 FAYIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGP 213
Cdd:cd03683  39 GNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGP 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  214 LVHVACCCGNILCH--CFNKY-RKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAF 290
Cdd:cd03683 119 FVHISSIVAALLSKltTFFSGiYENESRRMEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAF 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  291 TLRSINPF---GNSRLVLFYVEFHT--PWHLFELVPFILLGIFGGLWGALFI---RTNIAWCRKRKTTQ--LGKYPVIEV 360
Cdd:cd03683 199 TFRLLAVFfsdQETITALFKTTFFVdfPFDVQELPIFALLGIICGLLGALFVflhRKIVRFRRKNRLFSkfLKRSPLLYP 278

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  361 LVVTAITAILAFPneytrmstseliselfndcglldssklcdyenrFNTskggelpdrpagvgvysamwqLALTLILKIV 440
Cdd:cd03683 279 AIVALLTAVLTFP---------------------------------FLT---------------------LFLFIVVKFV 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  441 ITIFTFGMKIPSGLFIPSMAVGAIAGRLLGVGMEQLAYYHQEWTVFNSwcsqgadcITPGLYAMVGAAACLGGVTRmTVS 520
Cdd:cd03683 305 LTALAITLPVPAGIFMPVFVIGAALGRLVGEIMAVLFPEGIRGGISNP--------IGPGGYAVVGAAAFSGAVTH-TVS 375

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 4557473  521 LVVIMFELTGGLEYIVPLMAAAMTSKWVADALGReGIYDAHIRLNGYPFL 570
Cdd:cd03683 376 VAVIIFELTGQISHLLPVLIAVLISNAVAQFLQP-SIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 142-545 4.86e-57

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: 199.33  E-value: 4.86e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  142 MYVLWALLFAFLAVSLVKVFAPYACGSGIPE-IKTILSGfiiRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACC 220
Cdd:cd00400  38 LYILLVPVIGGLLVGLLVRLLGPARGHGIPEvIEAIALG---GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  221 CGNILCHCFnkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFGN 300
Cdd:cd00400 115 IGSWLGRRL---RLSRNDRRILVACGAAAGIAAAFNAPLAGALFAIEVLLGEYSVASLIPVLLASVAAALVSRLLFGAEP 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  301 srlvLFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTNIAWCRKRKttQLGKYPVIEVLVVTAITAILAFPNEYTRMS 380
Cdd:cd00400 192 ----AFGVPLYDPLSLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFR--RLPIPPWLRPALGGLLLGLLGLFLPQVLGS 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  381 TSELISELFNdcglldssklcdyenrfntskgGELPdrpagvgvysaMWQLALTLILKIVITIFTFGMKIPSGLFIPSMA 460
Cdd:cd00400 266 GYGAILLALA----------------------GELS-----------LLLLLLLLLLKLLATALTLGSGFPGGVFAPSLF 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  461 VGAIAGRLLGVGMEQLAYyhqewtvfnswcsqgADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMA 540
Cdd:cd00400 313 IGAALGAAFGLLLPALFP---------------GLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLML 377


                ....*
gi 4557473  541 AAMTS 545
Cdd:cd00400 378 AVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
133-563 2.85e-55

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 195.36  E-value: 2.85e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  133 AFAYIVNYFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLVIKTITLVLAVSSGLSLGKEG 212
Cdd:COG0038  43 AAGSHLPPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIEAIHLK--GGRIPLRVAPVKFLASLLTIGSGGSLGREG 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  213 PLVHVACCCGNILCHCFnkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTL 292
Cdd:COG0038 121 PSVQIGAAIGSLLGRLL---RLSPEDRRILLAAGAAAGLAAAFNAPLAGALFALEVLLRDFSYRALIPVLIASVVAYLVS 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  293 RSInpFGNSrlVLFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTNIAWcrKRKTTQLGKYPVIEVLVVTAITAILA- 371
Cdd:COG0038 198 RLL--FGNG--PLFGVPSVPALSLLELPLYLLLGILAGLVGVLFNRLLLKV--ERLFKRLKLPPWLRPAIGGLLVGLLGl 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  372 -FPnEYTRMSTsELISELFNdcglldssklcdyenrfntskgGELPdrpagvgvysaMWQLALTLILKIVITIFTFGMKI 450
Cdd:COG0038 272 fLP-QVLGSGY-GLIEALLN----------------------GELS-----------LLLLLLLLLLKLLATALTLGSGG 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  451 PSGLFIPSMAVGAIAGRLLGVGMEQLAyyhqewtvfnswcsqGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTG 530
Cdd:COG0038 317 PGGIFAPSLFIGALLGAAFGLLLNLLF---------------PGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTG 381

                       410       420       430
                ....*....|....*....|....*....|...
gi 4557473  531 GLEYIVPLMAAAMTSKWVADALGREGIYDAHIR 563
Cdd:COG0038 382 SYSLLLPLMIACVIAYLVSRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 140-560 8.72e-49

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: 176.96  E-value: 8.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  140 YFMYVLWALLFAFLAVSLVKVFAPYACGSGIPEIKTILSGFiiRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVAC 219
Cdd:cd01031  37 LLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL--LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGA 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  220 CCGNILCHCFnkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFTLRSINPFG 299
Cdd:cd01031 115 AIGQGVSKWF---KTSPEERRQLIAAGAAAGLAAAFNAPLAGVLFVLEELRHSFSPLALLTALVASIAADFVSRLFFGLG 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  300 nsrlVLFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTNIA---WCRKRKTTQLGKYPVIEVLVVTAItaILAFPNey 376
Cdd:cd01031 192 ----PVLSIPPLPALPLKSYWLLLLLGIIAGLLGYLFNRSLLKsqdLYRKLKKLPRELRVLLPGLLIGPL--GLLLPE-- 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  377 TRMSTSELISELFndcglldssklcdyenrfntskGGELPdrpagvgvysaMWQLALTLILKIVITIFTFGMKIPSGLFI 456
Cdd:cd01031 264 ALGGGHGLILSLA----------------------GGNFS-----------ISLLLLIFVLRFIFTMLSYGSGAPGGIFA 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  457 PSMAVGAIAGRLLGVGMEQLAyyhqewtvfnswcsqGADCITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIV 536
Cdd:cd01031 311 PMLALGALLGLLFGTILVQLG---------------PIPISAPATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLL 375

                       410       420
                ....*....|....*....|....
gi 4557473  537 PLMAAAMTSKWVADALGREGIYDA 560
Cdd:cd01031 376 PLMVVCLVAYLVADLLGGKPIYEA 399
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 581-731 7.39e-46

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


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 159.22  E-value: 7.39e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  581 LAMDVMKPRrndplLTVLTQDsMTVEDVETIISETTYSGFPVVVSRESQRLVGFVLRRDLIISIENarkkqdgvvstsii 660
Cdd:cd04591   1 TAEDVMRPP-----LTVLARD-ETVGDIVSVLKTTDHNGFPVVDSTESQTLVGFILRSQLILLLEA-------------- 60

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557473  661 yftehspplppytpptlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKH 731
Cdd:cd04591  61 -----------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 132-559 2.94e-32

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: 129.27  E-value: 2.94e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  132 GAFAYIVNYFMYVLWALLFA--FLAVSLVKVFAPYACGSGIPEIKTIL---SGFIIRGYLGKWTLVIKTITLVLAVSSGL 206
Cdd:cd01034  16 ALFQRLTATHPWLPLLLTPAgfALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  207 SLGKEGPLVHVACCcgniLCHCFNKY--RKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYYFPLK----TLWR 280
Cdd:cd01034  96 SVGREGPSVQIGAA----VMLAIGRRlpKWGGLSERGLILAGGAAGLAAAFNTPLAGIVFAIEELSRDFELRfsglVLLA 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  281 SFFAALVAAFTLRSINPFGNSRLVLfyvefhTPWHLFELVPFIllGIFGGLWGALFIRTNIA---WCRKRKTTQLGKYPv 357
Cdd:cd01034 172 VIAAGLVSLAVLGNYPYFGVAAVAL------PLGEAWLLVLVC--GVVGGLAGGLFARLLVAlssGLPGWVRRFRRRRP- 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  358 ieVLVVTAITAILAFpneytrmstseliselfndCGLLDSSKlcdyenrfnTSKGGELPDRPAGVGVYSAMWQLALtliL 437
Cdd:cd01034 243 --VLFAALCGLALAL-------------------IGLVSGGL---------TFGTGYLQARAALEGGGGLPLWFGL---L 289

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  438 KIVITIFTFGMKIPSGLFIPSMAVGAiagrLLGVGMEQLAYYHQewtvfnswcsqgadcitPGLYAMVGAAACLGGVTRM 517
Cdd:cd01034 290 KFLATLLSYWSGIPGGLFAPSLAVGA----GLGSLLAALLGSVS-----------------QGALVLLGMAAFLAGVTQA 348

                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 4557473  518 TVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADALGREGIYD 559
Cdd:cd01034 349 PLTAFVIVMEMTGDQQMLLPLLAAALLASGVSRLVCPEPLYH 390
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
149-560 1.75e-26

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 113.06  E-value: 1.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   149 LFAFLAVSLVKVFAPYACGSGIPEIKTILSGfiIRGYLGKWTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILCHC 228
Cdd:PRK05277  53 VLAMIGYFLVRRFAPEAGGSGIPEIEGALEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVLDI 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   229 FNkyRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLEEV--SYYFPLKTLWRSFFAALVAAFTLRSINpfgNSRLVLF 306
Cdd:PRK05277 131 FR--LRSDEARHTLLAAGAAAGLAAAFNAPLAGILFVIEEMrpQFRYSLISIKAVFIGVIMATIVFRLFN---GEQAVIE 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   307 YVEFHTPwHLFELVPFILLGIFGGLWGALFIRTNIA---WCRKRKTTQLGKYPVIeVLVVTAITAILAFPNEYTRMSTSE 383
Cdd:PRK05277 206 VGKFSAP-PLNTLWLFLLLGIIFGIFGVLFNKLLLRtqdLFDRLHGGNKKRWVLM-GGAVGGLCGLLGLLAPAAVGGGFN 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   384 LISELFNdcglldssklcdyenrfntskggelpdrpagvGVYSAMwQLALTLILKIVITIFTFGMKIPSGLFIPSMAVGA 463
Cdd:PRK05277 284 LIPIALA--------------------------------GNFSIG-MLLFIFVARFITTLLCFGSGAPGGIFAPMLALGT 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   464 IAGRLLGVGMEQLayyHQEWTvfnswcsqgadcITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAM 543
Cdd:PRK05277 331 LLGLAFGMVAAAL---FPQYH------------IEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCL 395

                        410
                 ....*....|....*..
gi 4557473   544 TSKWVADALGREGIYDA 560
Cdd:PRK05277 396 GATLLAQFLGGKPIYSA 412
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
194-640 9.16e-21

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 96.74  E-value: 9.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   194 KTITLVLAVSSGLSLGKEGPLVHVACCCGNILchcfNKYRKNEAKR-REVLSAAAAAGVSVAFGAPIGGVLFSLEEVSYY 272
Cdd:PRK01862 121 RSASSLLTIGSGGSIGREGPMVQLAALAASLV----GRFAHFDPPRlRLLVACGAAAGITSAYNAPIAGAFFVAEIVLGS 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   273 FPLKTLWRSFFAALVAAFTLRSinpFGNSRLVLFYVEFH--TPWhlfELVPFILLGIFGGLWGALFIR-TNIAwcrKRKT 349
Cdd:PRK01862 197 IAMESFGPLVVASVVANIVMRE---FAGYQPPYEMPVFPavTGW---EVLLFVALGVLCGAAAPQFLRlLDAS---KNQF 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   350 TQLGKYPVIEVLVVTAITAILA--FP----NEYTRMSTseliselfndcgLLDSSKLcdyenrfntskggelpdrpagvg 423
Cdd:PRK01862 268 KRLPVPLPVRLALGGLLVGVISvwVPevwgNGYSVVNT------------ILHAPWT----------------------- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   424 vysamWQ-LALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGVGMEQLayyhqewtvfnsWCSQGADcitPGLY 502
Cdd:PRK01862 313 -----WQaLVAVLVAKLIATAATAGSGAVGGVFTPTLFVGAVVGSLFGLAMHAL------------WPGHTSA---PFAY 372

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473   503 AMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVADALGREGIYDAHIRLNGYpflEAKEEFAHKTLA 582
Cdd:PRK01862 373 AMVGMGAFLAGATQAPLMAILMIFEMTLSYQVVLPLMVSCVVAYFTARALGTTSMYEITLRRHQD---EAERERLRTTQM 449

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557473   583 MDVMKPRRndpllTVLTQDSmTVEDVETIISETtysgfPV---VVSRESQRLVGFVLRRDL 640
Cdd:PRK01862 450 RELIQPAQ-----TVVPPTA-SVADMTRVFLEY-----PVkylYVVDDDGRFRGAVALKDI 499
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
497-732 9.58e-16

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 76.46  E-value: 9.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  497 ITPGLYAMVGAAACLGGVTRMTVSLVVIMFELTGGLEYIVPLMAAAMTSKWVAdALGREGIYDAHIRLNGYPFLEAKEEF 576
Cdd:COG2524   4 LLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGL-GLLLLLLLIVLQAAAVRVVAEKELGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  577 AHKTLAMDVMkprrNDPLLTVltQDSMTVEDVETIISETTYSGFPVVvsrESQRLVGFVLRRDLIISIENARKKQDgvvs 656
Cdd:COG2524  83 VLKMKVKDIM----TKDVITV--SPDTTLEEALELMLEKGISGLPVV---DDGKLVGIITERDLLKALAEGRDLLD---- 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557473  657 tsiiyftehspplppytpptLKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDVLKHI 732
Cdd:COG2524 150 --------------------APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
581-734 7.35e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 68.74  E-value: 7.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  581 LAMDVMkprrNDPLLTVltQDSMTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLIISIENARKKQDGVvstsii 660
Cdd:COG0517   2 KVKDIM----TTDVVTV--SPDATVREALELMSEKRIGGLPVV--DEDGKLVGIVTDRDLRRALAAEGKDLLDT------ 67

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557473  661 yftehspplppytpptlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLV-THNGRLLGIITKKDVLKHIAQ 734
Cdd:COG0517  68 -----------------PVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLE 125
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
584-737 1.72e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.97  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  584 DVMKPrrndPLLTVltQDSMTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLIISIENARKKQdgvvstsiiyft 663
Cdd:COG3448   6 DIMTR----DVVTV--SPDTTLREALELMREHGIRGLPVV--DEDGRLVGIVTERDLLRALLPDRLDE------------ 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557473  664 ehspplPPYTPPTLKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDVLKHIAQMAN 737
Cdd:COG3448  66 ------LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIH-RLpvVDDDGRLVGIVTRTDLLRALARLLE 134
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
584-730 3.93e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 66.86  E-value: 3.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  584 DVMKprRNDPllTVLTQDsMTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLiisienaRKKQDGVvstsiiyft 663
Cdd:COG4109  20 DIMT--LEDV--ATLSED-DTVEDALELLEKTGHSRFPVV--DENGRLVGIVTSKDI-------LGKDDDT--------- 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4557473  664 ehspplppytpptlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDVLK 730
Cdd:COG4109  77 --------------PIEDVMTKNPITVTPDTSLASAAHKMIWEGIELlPVVDDDGRLLGIISRQDVLK 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 591-730 3.43e-11

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: 60.72  E-value: 3.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  591 NDPLLTVltQDSMTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLIISIENARKKQDgvvstsiiyftehspplp 670
Cdd:cd02205   1 TRDVVTV--DPDTTVREALELMAENGIGALPVV--DDDGKLVGIVTERDILRALVEGGLALD------------------ 58

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557473  671 pytpptLKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDVLK 730
Cdd:cd02205  59 ------TPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDILR 113
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
 189-545 6.56e-11

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: 65.01  E-value: 6.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  189 WTLVIKTITLVLAVSSGLSLGKEGPLVHVACCCGNILChcfNKYRKNEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLE- 267
Cdd:cd01033  83 WETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRFS---DWLGLTVADRRLLVACAAGAGLAAVYNVPLAGALFALEi 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  268 ---EVSyyfplktlWRSFFAALVAAFTLRSINPFGNSRLVLFYVefHTPWHLFELVPF-ILLGIFGGLWGALFIRTNiAW 343
Cdd:cd01033 160 llrTIS--------LRSVVAALATSAIAAAVASLLKGDHPIYDI--PPMQLSTPLLIWaLLAGPVLGVVAAGFRRLS-QA 228

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  344 CRKRKTTqlGKYPVIEVLVVTAITAILA--FPneytrmstseliSELFNDCGLLDSSklcdyenrFNTSKGGELpdrpag 421
Cdd:cd01033 229 ARAKRPK--GKRILWQMPLAFLVIGLLSifFP------------QILGNGRALAQLA--------FSTTLTLSL------ 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  422 vgvysamwqLALTLILKIVITIFTFGMKIPSGLFIPSMAVGAIAGRLLGVgmeqlayyhqewtVFNSWCSQgadcITPGL 501
Cdd:cd01033 281 ---------LLILLVLKIVATLLALRAGAYGGLLTPSLALGALLGALLGI-------------VWNALLPP----LSIAA 334

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 4557473  502 YAMVGAAACLGGVTRMTVSLVVIMFELTG-GLEYIVPLMAAAMTS 545
Cdd:cd01033 335 FALIGAAAFLAATQKAPLTALILVLEFTRqNPLFLIPLMLAVAGA 379
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 584-735 1.05e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 54.06  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  584 DVMkprrNDPLLTVltQDSMTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLIISIENARKKQDGVvstsiiyft 663
Cdd:COG2905   3 DIM----SRDVVTV--SPDATVREAARLMTEKGVGSLVVV--DDDGRLVGIITDRDLRRRVLAEGLDPLDT--------- 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557473  664 ehspplppytpptlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKHIAQM 735
Cdd:COG2905  66 --------------PVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 687-733 2.48e-08

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 50.59  E-value: 2.48e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 4557473     687 PFTVTDLTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDVLKHIA 733
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDeEGRLVGIVTRRDIIKALA 49
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 593-730 2.01e-07

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 49.80  E-value: 2.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  593 PLLTVLtqDSMTVEDVETIISETTYSGFPVVvsrESQRLVGFVLRRDliisIENARKKQDGvvstsiiyfteHSpplppy 672
Cdd:cd04595   3 PVKTVS--PDTTIEEARKIMLRYGHTGLPVV---EDGKLVGIISRRD----VDKAKHHGLG-----------HA------ 56

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557473  673 tpptlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLK 730
Cdd:cd04595  57 -----PVKGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLR 109
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 602-732 4.80e-07

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: 49.25  E-value: 4.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  602 SMTVEDV-ETI-----ISETTYSGFpvVVSREsQRLVGFVLRRDLIISIENArkkqdgvvstsiiyftehspplppytpp 675
Cdd:cd04606  17 DWTVEEAlEYLrrlapDPETIYYIY--VVDED-RRLLGVVSLRDLLLADPDT---------------------------- 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557473  676 tlKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLrqcL----VTHNGRLLGIITKKDVLKHI 732
Cdd:cd04606  66 --KVSDIMDTDVISVSADDDQEEVARLFAKYDL---LalpvVDEEGRLVGIITVDDVLDVI 121
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 593-645 1.10e-06

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: 45.97  E-value: 1.10e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 4557473     593 PLLTVltQDSMTVEDVETIISETTYSGFPVVVSResQRLVGFVLRRDLIISIE 645
Cdd:smart00116   1 DVVTV--SPDTTLEEALELLRENGIRRLPVVDEE--GRLVGIVTRRDIIKALA 49
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 602-730 2.54e-06

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: 46.55  E-value: 2.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  602 SMTVEDVETIISETTYSGFPVVvsrESQRLVGFVLRRDLIISIENarkkqdgvvstsiiyftehspplppytpptLKLRN 681
Cdd:cd04610  11 DDTVKDVIKLIKETGHDGFPVV---DDGKVVGYVTAKDLLGKDDD------------------------------EKVSE 57

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 4557473  682 IldLSPFTVTDLTPMEIvVDIFRKLgLRQCL-----VTHNGRLLGIITKKDVLK 730
Cdd:cd04610  58 I--MSRDTVVADPDMDI-TDAARVI-FRSGIsklpvVDDEGNLVGIITNMDVIR 107
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 679-733 5.00e-06

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: 44.13  E-value: 5.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557473    679 LRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQ-CLVTHNGRLLGIITKKDVLKHIA 733
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRlPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 603-730 7.03e-06

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: 46.27  E-value: 7.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  603 MTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLIisienaRKKQDGVVSTSIIYFTEHSPPLPPYTPPTLKLRNI 682
Cdd:cd04586  12 TSVREAARLLLEHRISGLPVV--DDDGKLVGIVSEGDLL------RREEPGTEPRRVWWLDALLESPERLAEEYVKAHGR 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 4557473  683 L--DL---SPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLK 730
Cdd:cd04586  84 TvgDVmtrPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 621-730 7.52e-06

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 45.88  E-value: 7.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  621 PVVvsrESQRLVGFVLRRDLiisienaRKkqdgvVSTSIiyFTEHSPPLPPYTPPTLKLRNILDLSPFTVTDLTPMEIVV 700
Cdd:cd04584  35 PVV---DDGKLVGIVTDRDL-------LR-----ASPSK--ATSLSIYELNYLLSKIPVKDIMTKDVITVSPDDTVEEAA 97

                        90       100       110
                ....*....|....*....|....*....|...
gi 4557473  701 DIFR--KLGlrqCL-VTHNGRLLGIITKKDVLK 730
Cdd:cd04584  98 LLMLenKIG---CLpVVDGGKLVGIITETDILR 127
ClC_sycA_like cd03682
ClC sycA-like chloride channel proteins. This ClC family presents in bacteria, where it ...
 205-372 1.40e-05

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: 47.96  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  205 GLSLGKEGPLVHVacccGNILCHCFNKYRK-NEAKRREVLSAAAAAGVSVAFGAPIGGVLFSLE-------EVSYYFPlk 276
Cdd:cd03682  92 GGSAGREGTAVQM----GGSLADAFGRVFKlPEEDRRILLIAGIAAGFAAVFGTPLAGAIFALEvlvlgrlRYSALIP-- 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  277 tlwrSFFAALVAAFTLRSinpFGNSRLVlFYVEFHTPWHLFELVPFILLGIFGGLWGALFIRTnIAWCrKRKTTQLGKYP 356
Cdd:cd03682 166 ----CLVAAIVADWVSHA---LGLEHTH-YHIVFIPTLDPLLFVKVILAGIIFGLAGRLFAEL-LHFL-KKLLKKRIKNP 235

                       170
                ....*....|....*.
gi 4557473  357 VIEVLVVTAITAILAF 372
Cdd:cd03682 236 YLRPFVGGLLIILLVY 251
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 584-730 2.86e-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: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 43.71  E-value: 2.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  584 DVMKPRrndpllTVLTQDSMTVEDVETIISETTYSGFPVVvsrESQRLVGfvlrrdlIISIENARKKQDgvvstsiiyfT 663
Cdd:cd04801   1 DIMTPE------VVTVTPEMTVSELLDRMFEEKHLGYPVV---ENGRLVG-------IVTLEDIRKVPE----------V 54

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  664 EHSPPlppytpptlKLRNILDLSPFTVTDLTPmeiVVDIFRKL---GLRQCLVTHNGRLLGIITKKDVLK 730
Cdd:cd04801  55 EREAT---------RVRDVMTKDVITVSPDAD---AMEALKLMsqnNIGRLPVVEDGELVGIISRTDLMR 112
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 600-730 3.36e-05

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 43.61  E-value: 3.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  600 QDSMTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLIisienarKKQDGVvstsiiyftehspplppytpptlKL 679
Cdd:cd04596   8 RETDTVRDYKQLSEETGHSRFPVV--DEENRVVGIVTAKDVI-------GKEDDT-----------------------PI 55

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557473  680 RNILDLSPFTVTDLTP-------M-----EI--VVDIfrklglrqclvthNGRLLGIITKKDVLK 730
Cdd:cd04596  56 EKVMTKNPITVKPKTSvasaahmMiwegiELlpVVDE-------------NRKLLGVISRQDVLK 107
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 602-732 6.41e-05

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: 46.23  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473    602 SMTVEDVETIISETTYSGFPVVvsrESQRLVGFVLRRDLIISIENARKKQDGVVSTSIIyftehspplppytpptlklrn 681
Cdd:pfam00478  96 DATVADALALMERYGISGVPVV---DDGKLVGIVTNRDLRFETDLSQPVSEVMTKENLV--------------------- 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4557473    682 ildlspfTVTDLTPMEIVVDIFRKLGL-RQCLVTHNGRLLGIITKKDVLKHI 732
Cdd:pfam00478 152 -------TAPEGTTLEEAKEILHKHKIeKLPVVDDNGRLVGLITIKDIEKAK 196
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 582-729 1.14e-04

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 42.10  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  582 AMDVMKPRRNdplLTVLtQDSMTVEDVETIISETTYSGFPvVVSRESQRLVGFVLRRDLIISIENARKKQDgvvstsiiy 661
Cdd:cd04590   2 VREVMTPRTD---VVAL-DADATLEELLELILESGYSRFP-VYEGDLDNIIGVLHVKDLLAALLEGREKLD--------- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557473  662 ftehspplppytpptlkLRNILDlSPFTVTDLTPMEIVVDIFRKLGLRQCLVT-HNGRLLGIITKKDVL 729
Cdd:cd04590  68 -----------------LRALLR-PPLFVPETTPLDDLLEEFRKERSHMAIVVdEYGGTAGIVTLEDIL 118
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
603-739 1.37e-04

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 45.06  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  603 MTVEDV------ETIISETTYSGFpvVVSREsQRLVGFVLRRDLIISIENArkkqdgvvstsiiyftehspplppytppt 676
Cdd:COG2239 146 WTVGEAlrylrrQAEDPETIYYIY--VVDDD-GRLVGVVSLRDLLLADPDT----------------------------- 193

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557473  677 lKLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRqCL--VTHNGRLLGIITKKDVLKHIAQMANQD 739
Cdd:COG2239 194 -KVSDIMDTDVISVPADDDQEEVARLFERYDLL-ALpvVDEEGRLVGIITVDDVVDVIEEEATED 256
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 584-641 2.70e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 39.50  E-value: 2.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557473    584 DVMKPrrndPLLTVltQDSMTVEDVETIISETTYSGFPVVVsrESQRLVGFVLRRDLI 641
Cdd:pfam00571   3 DIMTK----DVVTV--SPDTTLEEALELMREHGISRLPVVD--EDGKLVGIVTLKDLL 52
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 579-641 3.35e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS 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.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 40.41  E-value: 3.35e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557473  579 KTLAMDVMKPRRNDPLLTVLTQDsmTVEDVETIISETTYSGFPVVvsRESQRLVGFVLRRDLI 641
Cdd:cd04597  47 SDIARTVDYIMTKDNLIVFKEDD--YLDEVKEIMLNTNFRNYPVV--DENNKFLGTISRKHLI 105
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 687-743 2.25e-03

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: 38.38  E-value: 2.25e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4557473  687 PFTVTDLTPMEIVVDIFRKLGLRQCLVTH-NGRLLGIITKKDVLKHIAQMANQDPDSI 743
Cdd:cd02205   4 VVTVDPDTTVREALELMAENGIGALPVVDdDGKLVGIVTERDILRALVEGGLALDTPV 61
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
678-734 2.39e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 39.87  E-value: 2.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557473  678 KLRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKHIAQ 734
Cdd:COG2524  87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 687-736 2.56e-03

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: 38.56  E-value: 2.56e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4557473  687 PFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLKHIAQMA 736
Cdd:cd04584  10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKA 59
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 680-728 5.45e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 39.95  E-value: 5.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4557473   680 RNILDLSPFTVTDLTPMEIVVDIFRKLGLRQCLVTHNGR----LLGIITKKDV 728
Cdd:PTZ00314  99 ENGFIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKvggkLLGIVTSRDI 151
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 679-743 6.18e-03

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


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 37.52  E-value: 6.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557473  679 LRNILDLSPFTVTDLTPMEIVVDIFRKLGLRQC----------------LVTHNGRLLGIITKKDVLKHIAQMANQDPDS 742
Cdd:cd04620   1 LEQAIDRHPLTVSPDTPVIEAIALMSQTRSSCCllsedsiitearsscvLVVENQQLVGIFTERDVVRLTASGIDLSGVT 80


                .
gi 4557473  743 I 743
Cdd:cd04620  81 I 81
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 686-730 9.85e-03

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 36.32  E-value: 9.85e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 4557473  686 SP-FTVTDLTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDVLK 730
Cdd:cd04595   2 SPvKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDVDK 47
 
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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