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Conserved domains on  [gi|167466160|ref|NP_001107803|]
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H(+)/Cl(-) exchange transporter 7 isoform b [Homo sapiens]

Protein Classification

chloride channel protein( domain architecture ID 10132712)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 71-596 0e+00

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


:

Pssm-ID: 239657 [Multi-domain]  Cd Length: 466  Bit Score: 689.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  71 ESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIdkftEKGGLSF 150
Cdd:cd03685    1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYI----EKGRLFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 151 SLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSG 230
Cdd:cd03685   77 AFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 231 SVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMIS 310
Cdd:cd03685  157 ACIAAGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 311 TFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIH-RPCLQ 389
Cdd:cd03685  237 TFTLNFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINHkGKLLK 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 390 VIEAVLVAAVTATVAFvliyssrdcqplqggsmsyplqlfcadgeynsmaaaffntpeksvvslfhdppgsynPLTLGLF 469
Cdd:cd03685  317 VLEALLVSLVTSVVAF---------------------------------------------------------PQTLLIF 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 470 TLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGaAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEA 549
Cdd:cd03685  340 FVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFG-FTSIDPGLYALLGAAAFLGGVMRMTVSLTVILLEL 418

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 167466160 550 TSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPV 596
Cdd:cd03685  419 TNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFLHNGFPV 465
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 602-766 1.45e-41

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: 147.28  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 602 TAREVMSTPVTCLRRREKVGVIVDVLSDTasNHNGFPVVEHADDTqpaRLQGLILRSQLIVLLKHkvfversnlglvqrr 681
Cdd:cd04591    1 TAEDVMRPPLTVLARDETVGDIVSVLKTT--DHNGFPVVDSTESQ---TLVGFILRSQLILLLEA--------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 682 lrlkdfrdayprfppiqsihvsqderectmDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRK 761
Cdd:cd04591   61 ------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNN-GRLVGIVTRK 109


                 ....*
gi 167466160 762 DLARY 766
Cdd:cd04591  110 DLLRA 114
 
Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 71-596 0e+00

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


Pssm-ID: 239657 [Multi-domain]  Cd Length: 466  Bit Score: 689.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  71 ESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIdkftEKGGLSF 150
Cdd:cd03685    1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYI----EKGRLFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 151 SLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSG 230
Cdd:cd03685   77 AFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 231 SVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMIS 310
Cdd:cd03685  157 ACIAAGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 311 TFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIH-RPCLQ 389
Cdd:cd03685  237 TFTLNFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINHkGKLLK 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 390 VIEAVLVAAVTATVAFvliyssrdcqplqggsmsyplqlfcadgeynsmaaaffntpeksvvslfhdppgsynPLTLGLF 469
Cdd:cd03685  317 VLEALLVSLVTSVVAF---------------------------------------------------------PQTLLIF 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 470 TLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGaAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEA 549
Cdd:cd03685  340 FVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFG-FTSIDPGLYALLGAAAFLGGVMRMTVSLTVILLEL 418

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 167466160 550 TSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPV 596
Cdd:cd03685  419 TNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFLHNGFPV 465
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 162-571 1.54e-53

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: 188.91  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  162 FVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPhvVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGR 241
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGGRGP--LPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  242 STSLKRDFKIF----------EYFRrdtekrdfvsagaaagvsaafgAPVGGVLFSLEEGASFWNQFLTWRIFFASMIST 311
Cdd:pfam00654  79 FRLSPRDRRILlaagaaaglaAAFN----------------------APLAGVLFALEELSRSFSLRALIPVLLASVVAA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  312 FTLNFVLSIYHgnmwdlsspgLINFGrfdsEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPclQVI 391
Cdd:pfam00654 137 LVSRLIFGNSP----------LFSVG----EPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLKIP--PVL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  392 EAVLVAAVTATVAFVLiyssrdcqplqggsmsyplqlfcadgeynsmaAAFFNTPEKSVVSLFHdppGSYNPLTLGLFTL 471
Cdd:pfam00654 201 RPALGGLLVGLLGLLF--------------------------------PEVLGGGYELIQLLFN---GNTSLSLLLLLLL 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  472 VYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLtGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATS 551
Cdd:pfam00654 246 LKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALL-FPIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTG 324

                         410       420
                  ....*....|....*....|
gi 167466160  552 NVTYGFPIMLVLMTAKIVGD 571
Cdd:pfam00654 325 SLQLLLPLMLAVLIAYAVSR 344
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 602-766 1.45e-41

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: 147.28  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 602 TAREVMSTPVTCLRRREKVGVIVDVLSDTasNHNGFPVVEHADDTqpaRLQGLILRSQLIVLLKHkvfversnlglvqrr 681
Cdd:cd04591    1 TAEDVMRPPLTVLARDETVGDIVSVLKTT--DHNGFPVVDSTESQ---TLVGFILRSQLILLLEA--------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 682 lrlkdfrdayprfppiqsihvsqderectmDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRK 761
Cdd:cd04591   61 ------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNN-GRLVGIVTRK 109


                 ....*
gi 167466160 762 DLARY 766
Cdd:cd04591  110 DLLRA 114
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
96-580 2.64e-26

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 112.15  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  96 RTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIkgnidkFTEKGGLSFSLLLWATLNAAFVLVGsVIVAFIEP 175
Cdd:COG0038    1 RRRLLRLLLLAVLVGILAGLAAVLFRLLLELATHLFLGGL------LSAAGSHLPPWLVLLLPPLGGLLVG-LLVRRFAP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 176 VAAGSGIPQIKCFLNGVKipHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQgrstslkrdfkifeYF 255
Cdd:COG0038   74 EARGSGIPQVIEAIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGR--------------LL 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 256 RRDTEKRD--------------FVSagaaagvsaafgaPVGGVLFSLEE-GASFwnqflTWRIFFASMISTFTLNFVLSI 320
Cdd:COG0038  138 RLSPEDRRillaagaaaglaaaFNA-------------PLAGALFALEVlLRDF-----SYRALIPVLIASVVAYLVSRL 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 321 YHGNMWDLSSPGLINFgrfdsekmayTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQvieAVLVAAVT 400
Cdd:COG0038  200 LFGNGPLFGVPSVPAL----------SLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRLKLPPWLR---PAIGGLLV 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 401 ATVAFVLiyssrdcQPLQGGSmsyplqlfcadgeYNSMAAAFFntpeksvvslfhdppGSYNPLTLGLFTLVYFFLACWT 480
Cdd:COG0038  267 GLLGLFL-------PQVLGSG-------------YGLIEALLN---------------GELSLLLLLLLLLLKLLATALT 311

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 481 YGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIwADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIM 560
Cdd:COG0038  312 LGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLM 390

                        490       500
                 ....*....|....*....|.
gi 167466160 561 LVLMTAKIV-GDVFIEGLYDM 580
Cdd:COG0038  391 IACVIAYLVsRLLFPRSIYTA 411
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
600-766 4.12e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 72.59  E-value: 4.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 600 SLTAREVMSTPVTCLRRREKVGVIVDVLSDtaSNHNGFPVVEHADdtqpaRLQGLILRSQLIvllkhkvfversnlglvq 679
Cdd:COG3448    1 AMTVRDIMTRDVVTVSPDTTLREALELMRE--HGIRGLPVVDEDG-----RLVGIVTERDLL------------------ 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 680 RRLRLKDFRDAYPRFPPIQsihvsqderectmdLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVT 759
Cdd:COG3448   56 RALLPDRLDELEERLLDLP--------------VEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVT 121


                 ....*..
gi 167466160 760 RKDLARY 766
Cdd:COG3448  122 RTDLLRA 128
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
107-569 2.11e-12

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 69.92  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 107 ALIGILTGLVACFIDIVVENlaglkyrVIKGNIDKFTEKGGLSFSLLLWATL-NAAFVLVGSVIVAFIEPVAAGSGIPQI 185
Cdd:PRK05277   5 AVVGTLTGLVGVAFELAVDW-------VQNQRLGLLASVADNGLLLWIVAFLiSAVLAMIGYFLVRRFAPEAGGSGIPEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 186 KCFLNGVKIPHVVRLktLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISqgrstslkrdfkifEYFR-RDTEKRD- 263
Cdd:PRK05277  78 EGALEGLRPVRWWRV--LPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVL--------------DIFRlRSDEARHt 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 264 -------------FVSagaaagvsaafgaPVGGVLFSLEEgasFWNQF-LTWRIFFASMISTFTLNFVLSIYHGNmwdls 329
Cdd:PRK05277 142 llaagaaaglaaaFNA-------------PLAGILFVIEE---MRPQFrYSLISIKAVFIGVIMATIVFRLFNGE----- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 330 sPGLINFGRFDSEkmayTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQVIeaVLVAAVTATVAFVLIY 409
Cdd:PRK05277 201 -QAVIEVGKFSAP----PLNTLWLFLLLGIIFGIFGVLFNKLLLRTQDLFDRLHGGNKKRWV--LMGGAVGGLCGLLGLL 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 410 SSrdcqPLQGGSMSYPLQLFcaDGEYN-SMAAAFFntpeksvvslfhdppgsynpltLGLFTLVyffLACwtYGLTVSAG 488
Cdd:PRK05277 274 AP----AAVGGGFNLIPIAL--AGNFSiGMLLFIF----------------------VARFITT---LLC--FGSGAPGG 320

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 489 VFIPSLLIGAAWGRLFGISLSYLTGAAIwADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKI 568
Cdd:PRK05277 321 IFAPMLALGTLLGLAFGMVAAALFPQYH-IEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCLGATL 399


                 .
gi 167466160 569 V 569
Cdd:PRK05277 400 L 400
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 713-769 1.96e-11

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 59.53  E-value: 1.96e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167466160  713 LSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLG 769
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 721-768 4.04e-09

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: 52.90  E-value: 4.04e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 167466160   721 PYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRL 768
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
717-781 2.52e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 44.44  E-value: 2.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167466160 717 MNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLGKRGLEELSLAQT 781
Cdd:PRK14869  74 EIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYMDILDPEILSKSPT 138
 
Name Accession Description Interval E-value
ClC_6_like cd03685
ClC-6-like chloride channel proteins. This CD includes ClC-6, ClC-7 and ClC-B, C, D in plants. ...
 71-596 0e+00

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


Pssm-ID: 239657 [Multi-domain]  Cd Length: 466  Bit Score: 689.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  71 ESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKGNIdkftEKGGLSF 150
Cdd:cd03685    1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYI----EKGRLFT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 151 SLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSG 230
Cdd:cd03685   77 AFLVYLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 231 SVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMIS 310
Cdd:cd03685  157 ACIAAGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIV 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 311 TFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIH-RPCLQ 389
Cdd:cd03685  237 TFTLNFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINHkGKLLK 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 390 VIEAVLVAAVTATVAFvliyssrdcqplqggsmsyplqlfcadgeynsmaaaffntpeksvvslfhdppgsynPLTLGLF 469
Cdd:cd03685  317 VLEALLVSLVTSVVAF---------------------------------------------------------PQTLLIF 339

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 470 TLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGaAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEA 549
Cdd:cd03685  340 FVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFG-FTSIDPGLYALLGAAAFLGGVMRMTVSLTVILLEL 418

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 167466160 550 TSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPV 596
Cdd:cd03685  419 TNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFLHNGFPV 465
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
 110-579 8.20e-91

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: 291.17  E-value: 8.20e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 110 GILTGLVACFIDIVVENLAGLKYRVIkgnidkFTEKGGLSFSLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCFL 189
Cdd:cd01036    1 GLLMGLVAVVLDYAVESSLDAGQWLL------RRIPGSYLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 190 NGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGA 269
Cdd:cd01036   75 NGVHLPMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLGCHVHLFQLFRNPRDRRDFLVAGA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 270 AAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSiyHGNMWDL---SSPGLINFGRFDSEkMAY 346
Cdd:cd01036  155 AAGVASAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNS--FNSGFELldrSSAMFLSLTVFELH-VPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 347 TIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPC--LQVIEAVLVAAVTATVAFvliyssrdcqplqggsmsy 424
Cdd:cd01036  232 NLYEFIPTVVIGVICGLLAALFVRLSIIFLRWRRRLLFRKTarYRVLEPVLFTLIYSTIHY------------------- 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 425 plqlfcadgeynsmaaaffntpeksvvslfhdppgsynPLTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLF 504
Cdd:cd01036  293 --------------------------------------APTLLLFLLIYFWMSALAFGIAVPGGTFIPSLVIGAAIGRLV 334

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 505 GISLSYL-------TGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGL 577
Cdd:cd01036  335 GLLVHRIavagigaESATLWADPGVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLLPLMVAILIAKAVADAFCESL 414


                 ..
gi 167466160 578 YD 579
Cdd:cd01036  415 YH 416
ClC_3_like cd03684
ClC-3-like chloride channel proteins. This CD includes ClC-3, ClC-4, ClC-5 and ClC-Y1. ClC-3 ...
 110-590 4.85e-75

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: 250.60  E-value: 4.85e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 110 GILTGLVACFIDIVVENLAGLKyrvikgnidkfteKGGLSFSL-LLWATLnaaFVLVGSVIVAFIEPVAAGSGIPQIKCF 188
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLK-------------EGYCNYIIyVLLALL---FAFIAVLLVKVVAPYAAGSGIPEIKTI 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 189 LNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISqgrstslkrdfKIFEYFRR-DTEKRDFVSA 267
Cdd:cd03684   65 LSGFIIRGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIIS-----------RLFPKYRRnEAKRREILSA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 268 GAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFvLSIYHGNMwdlsspgLINFG-RFDSEkmaY 346
Cdd:cd03684  134 AAAAGVAVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKS-LNPFGTGR-------LVLFEvEYDRD---W 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 347 TIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHR--PclqVIEAVLVAAVTATVAFVLIYSSRDCQPLQGgsmsy 424
Cdd:cd03684  203 HYFELIPFILLGIFGGLYGAFFIKANIKWARFRKKSLLKryP---VLEVLLVALITALISFPNPYTRLDMTELLE----- 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 425 plQLF--CADGEYNSMAAAFFNTPEKSVvslfhdpPGSYNPLTLGLFtlVYFFLACWTYGLTVSAGVFIPSLLIGAAWGR 502
Cdd:cd03684  275 --LLFneCEPGDDNSLCCYRDPPAGDGV-------YKALWSLLLALI--IKLLLTIFTFGIKVPAGIFVPSMAVGALFGR 343

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 503 LFGISLSYL-------------TGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIV 569
Cdd:cd03684  344 IVGILVEQLaysypdsiffaccTAGPSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVMVSKWV 423

                        490       500
                 ....*....|....*....|..
gi 167466160 570 GDVFI-EGLYDMHIQLQSVPFL 590
Cdd:cd03684  424 ADAIGkEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
 162-571 1.54e-53

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: 188.91  E-value: 1.54e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  162 FVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPhvVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGR 241
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGGRGP--LPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLGRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  242 STSLKRDFKIF----------EYFRrdtekrdfvsagaaagvsaafgAPVGGVLFSLEEGASFWNQFLTWRIFFASMIST 311
Cdd:pfam00654  79 FRLSPRDRRILlaagaaaglaAAFN----------------------APLAGVLFALEELSRSFSLRALIPVLLASVVAA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  312 FTLNFVLSIYHgnmwdlsspgLINFGrfdsEKMAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPclQVI 391
Cdd:pfam00654 137 LVSRLIFGNSP----------LFSVG----EPGSLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLKIP--PVL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  392 EAVLVAAVTATVAFVLiyssrdcqplqggsmsyplqlfcadgeynsmaAAFFNTPEKSVVSLFHdppGSYNPLTLGLFTL 471
Cdd:pfam00654 201 RPALGGLLVGLLGLLF--------------------------------PEVLGGGYELIQLLFN---GNTSLSLLLLLLL 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  472 VYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLtGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATS 551
Cdd:pfam00654 246 LKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALL-FPIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIVFELTG 324

                         410       420
                  ....*....|....*....|
gi 167466160  552 NVTYGFPIMLVLMTAKIVGD 571
Cdd:pfam00654 325 SLQLLLPLMLAVLIAYAVSR 344
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
 103-590 2.18e-48

ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ClC-1 is expressed in skeletal muscle and its mutation leads to both recessively and dominantly-inherited forms of muscle stiffness or myotonia. ClC-K is exclusively expressed in kidney. Similarly, mutation of ClC-K leads to nephrogenic diabetes insipidus in mice and Bartter's syndrome in human. These proteins belong to the ClC superfamily of chloride ion channels, which share the unique double-barreled architecture and voltage-dependent gating mechanism. The gating is conferred by the permeating anion itself, acting as the gating charge. This domain is found in the eukaryotic halogen ion (Cl-, Br- and I-) channel proteins, that perform a variety of functions including cell volume regulation, regulation of intracelluar chloride concentration, membrane potential stabilization, charge compensation necessary for the acidification of intracellular organelles and transepithelial chloride transport.


Pssm-ID: 239655 [Multi-domain]  Cd Length: 426  Bit Score: 177.05  E-value: 2.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 103 WVICALIGILTGLVACFIDIVVENLAGLK---YRVIKGNIdkftekgGLSFslLLWATLNAAFVLVGSVIVAFIEPVAAG 179
Cdd:cd03683    2 WLFLALLGILMALISIAMDFAVEKLLNARrwlYSLLTGNS-------LLQY--LVWVAYPVALVLFSALFCKYISPQAVG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 180 SGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTslkrdfkiFEYFRRDT 259
Cdd:cd03683   73 SGIPEMKTILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTTF--------FSGIYENE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 260 EKR-DFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLnFVLSIYHGNMWDLSSPGLINFGR 338
Cdd:cd03683  145 SRRmEMLAAACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTF-RLLAVFFSDQETITALFKTTFFV 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 339 FDSekmaYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRY-IHRPCLQVIEAVLVAAVTATVAfvliyssrdcqpl 417
Cdd:cd03683  224 DFP----FDVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNrLFSKFLKRSPLLYPAIVALLTA------------- 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 418 qggSMSYPLqlfcadgeynsmaaaffntpeksvvslfhdppgsynpLTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIG 497
Cdd:cd03683  287 ---VLTFPF-------------------------------------LTLFLFIVVKFVLTALAITLPVPAGIFMPVFVIG 326

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 498 AAWGRLFGISLSYLTGAAIWAD------PGKYALMGAAAQLGGIVRmTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGD 571
Cdd:cd03683  327 AALGRLVGEIMAVLFPEGIRGGisnpigPGGYAVVGAAAFSGAVTH-TVSVAVIIFELTGQISHLLPVLIAVLISNAVAQ 405

                        490
                 ....*....|....*....
gi 167466160 572 VFIEGLYDMHIQLQSVPFL 590
Cdd:cd03683  406 FLQPSIYDSIIKIKKLPYL 424
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 602-766 1.45e-41

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: 147.28  E-value: 1.45e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 602 TAREVMSTPVTCLRRREKVGVIVDVLSDTasNHNGFPVVEHADDTqpaRLQGLILRSQLIVLLKHkvfversnlglvqrr 681
Cdd:cd04591    1 TAEDVMRPPLTVLARDETVGDIVSVLKTT--DHNGFPVVDSTESQ---TLVGFILRSQLILLLEA--------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 682 lrlkdfrdayprfppiqsihvsqderectmDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRK 761
Cdd:cd04591   61 ------------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNN-GRLVGIVTRK 109


                 ....*
gi 167466160 762 DLARY 766
Cdd:cd04591  110 DLLRA 114
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
 109-571 4.06e-28

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: 117.64  E-value: 4.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 109 IGILTGLVACFIDIVVENLAGLKYRVikgnidkFTEKGGLSFSLLLWATLNAAFVLVGSVIVAFIEPVAAGSGIPQIKCF 188
Cdd:cd01031    1 IGLLAGLVAVLFRLGIDKLGNLRLSL-------YDFAANNPPLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 189 LNGVKIPHvvRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISqgrstslkrdfkifEYFRRDTEKRD----- 263
Cdd:cd01031   74 LAGLLPPN--WWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGVS--------------KWFKTSPEERRqliaa 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 264 ---------FVSagaaagvsaafgaPVGGVLFSLEEgasfWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPgli 334
Cdd:cd01031  138 gaaaglaaaFNA-------------PLAGVLFVLEE----LRHSFSPLALLTALVASIAADFVSRLFFGLGPVLSIP--- 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 335 NFGRFdsekmayTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPclQVIEAVLVAAVTATVAFVLiyssrdc 414
Cdd:cd01031  198 PLPAL-------PLKSYWLLLLLGIIAGLLGYLFNRSLLKSQDLYRKLKKLP--RELRVLLPGLLIGPLGLLL------- 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 415 qplqggsmsyPLQLFcaDGEYNsmaaaffntpeksVVSLFHdppGSYNPLTLGLFTLVYFFLACWTYGLTVSAGVFIPSL 494
Cdd:cd01031  262 ----------PEALG--GGHGL-------------ILSLAG---GNFSISLLLLIFVLRFIFTMLSYGSGAPGGIFAPML 313

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466160 495 LIGAAWGRLFGISLSYLTGAAIWAdPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGD 571
Cdd:cd01031  314 ALGALLGLLFGTILVQLGPIPISA-PATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNLLLPLMVVCLVAYLVAD 389
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
96-580 2.64e-26

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 112.15  E-value: 2.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160  96 RTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIkgnidkFTEKGGLSFSLLLWATLNAAFVLVGsVIVAFIEP 175
Cdd:COG0038    1 RRRLLRLLLLAVLVGILAGLAAVLFRLLLELATHLFLGGL------LSAAGSHLPPWLVLLLPPLGGLLVG-LLVRRFAP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 176 VAAGSGIPQIKCFLNGVKipHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQgrstslkrdfkifeYF 255
Cdd:COG0038   74 EARGSGIPQVIEAIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLGR--------------LL 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 256 RRDTEKRD--------------FVSagaaagvsaafgaPVGGVLFSLEE-GASFwnqflTWRIFFASMISTFTLNFVLSI 320
Cdd:COG0038  138 RLSPEDRRillaagaaaglaaaFNA-------------PLAGALFALEVlLRDF-----SYRALIPVLIASVVAYLVSRL 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 321 YHGNMWDLSSPGLINFgrfdsekmayTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQvieAVLVAAVT 400
Cdd:COG0038  200 LFGNGPLFGVPSVPAL----------SLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRLKLPPWLR---PAIGGLLV 266

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 401 ATVAFVLiyssrdcQPLQGGSmsyplqlfcadgeYNSMAAAFFntpeksvvslfhdppGSYNPLTLGLFTLVYFFLACWT 480
Cdd:COG0038  267 GLLGLFL-------PQVLGSG-------------YGLIEALLN---------------GELSLLLLLLLLLLKLLATALT 311

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 481 YGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIwADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIM 560
Cdd:COG0038  312 LGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLG-LSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPLM 390

                        490       500
                 ....*....|....*....|.
gi 167466160 561 LVLMTAKIV-GDVFIEGLYDM 580
Cdd:COG0038  391 IACVIAYLVsRLLFPRSIYTA 411
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
 110-570 6.72e-21

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: 95.71  E-value: 6.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 110 GILTGLVACFIDIVVENLAGLKYrvikGNIDKFTEKGGLSFSLLLWATLNAAFvLVGSVIVAFIEpvAAGSGIPQ-IKCF 188
Cdd:cd00400    1 GVLSGLGAVLFRLLIELLQNLLF----GGLPGELAAGSLSPLYILLVPVIGGL-LVGLLVRLLGP--ARGHGIPEvIEAI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 189 -LNGVKIPhvvrLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRD---------------FKif 252
Cdd:cd00400   74 aLGGGRLP----LRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLGRRLRLSRNDRrilvacgaaagiaaaFN-- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 253 eyfrrdtekrdfvsagaaagvsaafgAPVGGVLFSLEEgASFWNQFltwRIFFASMISTFTLNFVLSIYHGNmwdlssPG 332
Cdd:cd00400  148 --------------------------APLAGALFAIEV-LLGEYSV---ASLIPVLLASVAAALVSRLLFGA------EP 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 333 LINFGRFDSEkmayTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQvieAVLVAAVTATVAFVLiyssr 412
Cdd:cd00400  192 AFGVPLYDPL----SLLELPLYLLLGLLAGLVGVLFVRLLYKIERLFRRLPIPPWLR---PALGGLLLGLLGLFL----- 259

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 413 dcqplqggsmsyPLQLFCAdgeYNSMAAAFfntpeksvvslfhdpPGSYNPLTLGLFTLVYFFLACWTYGLTVSAGVFIP 492
Cdd:cd00400  260 ------------PQVLGSG---YGAILLAL---------------AGELSLLLLLLLLLLKLLATALTLGSGFPGGVFAP 309

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167466160 493 SLLIGAAWGRLFGISLSYLTGAAIwADPGKYALMGAAAQLGGIVRMTLSLTVIMMEatsnVTYGFPIMLVLMTAKIVG 570
Cdd:cd00400  310 SLFIGAALGAAFGLLLPALFPGLV-ASPGAYALVGMAALLAAVLRAPLTAILLVLE----LTGDYSLLLPLMLAVVIA 382
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
523-766 8.23e-18

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 82.62  E-value: 8.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 523 YALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYdMHIQLQSVPFLHWEAPVTSHSLT 602
Cdd:COG2524    9 LSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLL-IVLQAAAVRVVAEKELGLVLKMK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 603 AREVMSTPVTCLRRREKVGVIVDVLSDtaSNHNGFPVVEhaDDtqpaRLQGLIlrsqlivllkhkvfversnlglvqrrl 682
Cdd:COG2524   88 VKDIMTKDVITVSPDTTLEEALELMLE--KGISGLPVVD--DG----KLVGII--------------------------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 683 RLKDFRDAYPRFPPIQSIHVSqderectmdlsEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKD 762
Cdd:COG2524  133 TERDLLKALAEGRDLLDAPVS-----------DIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTD 201


                 ....
gi 167466160 763 LARY 766
Cdd:COG2524  202 ILRA 205
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
600-766 4.12e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 72.59  E-value: 4.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 600 SLTAREVMSTPVTCLRRREKVGVIVDVLSDtaSNHNGFPVVEHADdtqpaRLQGLILRSQLIvllkhkvfversnlglvq 679
Cdd:COG3448    1 AMTVRDIMTRDVVTVSPDTTLREALELMRE--HGIRGLPVVDEDG-----RLVGIVTERDLL------------------ 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 680 RRLRLKDFRDAYPRFPPIQsihvsqderectmdLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVT 759
Cdd:COG3448   56 RALLPDRLDELEERLLDLP--------------VEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVT 121


                 ....*..
gi 167466160 760 RKDLARY 766
Cdd:COG3448  122 RTDLLRA 128
CBS COG0517
CBS domain [Signal transduction mechanisms];
601-768 1.38e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 71.05  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 601 LTAREVMSTPVTCLRRREKVGVIVDVLSDTasNHNGFPVVEHADdtqpaRLQGLILRSQLivllkhkvfversnlglvqR 680
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEK--RIGGLPVVDEDG-----KLVGIVTDRDL-------------------R 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 681 RLRLKDFRDAYprfppiqsihvsqderecTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTR 760
Cdd:COG0517   55 RALAAEGKDLL------------------DTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITI 116


                 ....*...
gi 167466160 761 KDLARYRL 768
Cdd:COG0517  117 KDLLKALL 124
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
107-569 2.11e-12

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 69.92  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 107 ALIGILTGLVACFIDIVVENlaglkyrVIKGNIDKFTEKGGLSFSLLLWATL-NAAFVLVGSVIVAFIEPVAAGSGIPQI 185
Cdd:PRK05277   5 AVVGTLTGLVGVAFELAVDW-------VQNQRLGLLASVADNGLLLWIVAFLiSAVLAMIGYFLVRRFAPEAGGSGIPEI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 186 KCFLNGVKIPHVVRLktLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISqgrstslkrdfkifEYFR-RDTEKRD- 263
Cdd:PRK05277  78 EGALEGLRPVRWWRV--LPVKFFGGLGTLGSGMVLGREGPTVQMGGNIGRMVL--------------DIFRlRSDEARHt 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 264 -------------FVSagaaagvsaafgaPVGGVLFSLEEgasFWNQF-LTWRIFFASMISTFTLNFVLSIYHGNmwdls 329
Cdd:PRK05277 142 llaagaaaglaaaFNA-------------PLAGILFVIEE---MRPQFrYSLISIKAVFIGVIMATIVFRLFNGE----- 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 330 sPGLINFGRFDSEkmayTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMFRIRYIHRPCLQVIeaVLVAAVTATVAFVLIY 409
Cdd:PRK05277 201 -QAVIEVGKFSAP----PLNTLWLFLLLGIIFGIFGVLFNKLLLRTQDLFDRLHGGNKKRWV--LMGGAVGGLCGLLGLL 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 410 SSrdcqPLQGGSMSYPLQLFcaDGEYN-SMAAAFFntpeksvvslfhdppgsynpltLGLFTLVyffLACwtYGLTVSAG 488
Cdd:PRK05277 274 AP----AAVGGGFNLIPIAL--AGNFSiGMLLFIF----------------------VARFITT---LLC--FGSGAPGG 320

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 489 VFIPSLLIGAAWGRLFGISLSYLTGAAIwADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKI 568
Cdd:PRK05277 321 IFAPMLALGTLLGLAFGMVAAALFPQYH-IEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLILPLIITCLGATL 399


                 .
gi 167466160 569 V 569
Cdd:PRK05277 400 L 400
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
710-777 1.60e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 62.58  E-value: 1.60e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167466160 710 TMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARyRLGKRGLEELS 777
Cdd:COG3448    1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLR-ALLPDRLDELE 67
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 713-769 1.96e-11

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 59.53  E-value: 1.96e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 167466160  713 LSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLG 769
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 714-768 4.85e-10

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 57.92  E-value: 4.85e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDLARYRL 768
Cdd:COG2905   68 SEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALS 121
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 714-765 1.56e-09

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: 56.66  E-value: 1.56e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDLAR 765
Cdd:cd04584    3 KDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDD-GKLVGIVTDRDLLR 53
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
 148-579 2.06e-09

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: 60.32  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 148 LSFSLLLWATLNAAfvlvgsvivafiePVAAGSGIPQIKCFL---NGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEG 224
Cdd:cd01034   35 AGFALIAWLTRRFF-------------PGAAGSGIPQVIAALelpSAAARRRLLSLRTAVGKILLTLLGLLGGASVGREG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 225 PMIHSGSVIAAGISQ--GRSTSLKRdfkifeyfrrdtekRDFVSAGAAAGVSAAFGAPVGGVLFSLEE-GASF---WNQF 298
Cdd:cd01034  102 PSVQIGAAVMLAIGRrlPKWGGLSE--------------RGLILAGGAAGLAAAFNTPLAGIVFAIEElSRDFelrFSGL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 299 LTWRIFFASMIStftlnfvLSIYHGNMWdlsspglinFGRFDSEkmAYTIHEIPVFIAMGVVGGVLGAVFNALNYWLTMF 378
Cdd:cd01034  168 VLLAVIAAGLVS-------LAVLGNYPY---------FGVAAVA--LPLGEAWLLVLVCGVVGGLAGGLFARLLVALSSG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 379 RIRYIHRPCLQviEAVLVAAVTATVAFVLIYSSrdcqplqgGSMSYplqlfcaDGEYNSMAAAFFNtpeksvvslfhdpp 458
Cdd:cd01034  230 LPGWVRRFRRR--RPVLFAALCGLALALIGLVS--------GGLTF-------GTGYLQARAALEG-------------- 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 459 GSYNPLTLGLFTLVYFFLACWTyglTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIwadpgkyALMGAAAQLGGIVRM 538
Cdd:cd01034  279 GGGLPLWFGLLKFLATLLSYWS---GIPGGLFAPSLAVGAGLGSLLAALLGSVSQGAL-------VLLGMAAFLAGVTQA 348

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 167466160 539 TLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFI-EGLYD 579
Cdd:cd01034  349 PLTAFVIVMEMTGDQQMLLPLLAAALLASGVSRLVCpEPLYH 390
CBS COG0517
CBS domain [Signal transduction mechanisms];
711-778 2.36e-09

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 56.03  E-value: 2.36e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167466160 711 MDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARyRLGKRGLEELSL 778
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRR-ALAAEGKDLLDT 67
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 721-768 4.04e-09

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: 52.90  E-value: 4.04e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 167466160   721 PYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRL 768
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 713-765 5.85e-09

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: 54.56  E-value: 5.85e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 167466160 713 LSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd02205   61 VAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
600-766 7.99e-09

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 54.53  E-value: 7.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 600 SLTAREVMSTP-VTCLRRREKVGVIVDVLSDTasNHNGFPVVehaDDTQpaRLQGLIlrsqlivllkhkvfversnlglv 678
Cdd:COG4109   15 ILLVEDIMTLEdVATLSEDDTVEDALELLEKT--GHSRFPVV---DENG--RLVGIV----------------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 679 qrrlRLKDFRDAYPRFPpiqsihvsqderectmdLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLV 758
Cdd:COG4109   65 ----TSKDILGKDDDTP-----------------IEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGII 123


                 ....*...
gi 167466160 759 TRKDLARY 766
Cdd:COG4109  124 SRQDVLKA 131
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 714-763 1.32e-08

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


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 53.22  E-value: 1.32e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDL 763
Cdd:cd04607   61 EEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDL 110
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
711-780 2.05e-08

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 55.27  E-value: 2.05e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 711 MDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDLARYRLGKRGLEELSLAQ 780
Cdd:COG2524   86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAPVSD 154
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 713-766 3.88e-08

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 52.14  E-value: 3.88e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466160 713 LSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARY 766
Cdd:cd09836   61 VEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARE 114
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 713-778 5.86e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 51.75  E-value: 5.86e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167466160 713 LSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARyRLGKRGLEELSL 778
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRR-RVLAEGLDPLDT 65
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 713-765 5.38e-07

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


Pssm-ID: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 48.76  E-value: 5.38e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466160 713 LSEFMNpSP-YTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd09833   63 ISEVMS-SPvLTIPQDTTLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDVVL 115
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 721-779 9.02e-07

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: 48.01  E-value: 9.02e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167466160 721 PYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLGKRGLEELSLA 779
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVA 62
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 702-765 3.55e-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: 3.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466160 702 VSQDEREcTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDLAR 765
Cdd:cd04801   51 VPEVERE-ATRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLMR 112
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 713-764 4.21e-05

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


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 43.28  E-value: 4.21e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466160 713 LSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLA 764
Cdd:cd04583   56 VGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTRASLV 107
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
488-553 7.55e-05

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 46.28  E-value: 7.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466160 488 GVFIPSLLIGAAWGRLFGISLSYLTGAAIwADPGKYALMGAAAQLGG-----------IVRMTLSLTVIMMEATSNV 553
Cdd:PRK01862 338 GVFTPTLFVGAVVGSLFGLAMHALWPGHT-SAPFAYAMVGMGAFLAGatqaplmailmIFEMTLSYQVVLPLMVSCV 413
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
700-766 9.11e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 42.98  E-value: 9.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167466160 700 IHVSQDERECTMDLSEFM-NPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARY 766
Cdd:COG4109    5 ISTSYDTFKEILLVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK 72
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 723-763 9.90e-05

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


Pssm-ID: 341384 [Multi-domain]  Cd Length: 131  Bit Score: 42.71  E-value: 9.90e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 167466160 723 TVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDL 763
Cdd:cd04611   79 TVGAEDSLIHARDLLIDHRIRHLAVVDEDGQVTGLLGFADL 119
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 714-765 1.02e-04

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


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 42.41  E-value: 1.02e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd04622   63 REVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDLAV 114
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 677-765 1.82e-04

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


Pssm-ID: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 41.79  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 677 LVQRRLRLKDFRDAY-------PRFPPIQS-------IHVSQ-----DERECTMDLSEFMNPSPY--TVPQEASLPRVFK 735
Cdd:cd04639    9 IVDADLTLREFADDYligkkswREFLVTDEagrlvglITVDDlraipTSQWPDTPVRELMKPLEEipTVAADQSLLEVVK 88

                         90       100       110
                 ....*....|....*....|....*....|
gi 167466160 736 LFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd04639   89 LLEEQQLPALAVVSENGTLVGLIEKEDIIE 118
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 717-765 2.02e-04

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 41.78  E-value: 2.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 167466160 717 MNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLK 49
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 676-766 2.34e-04

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 41.64  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 676 GLVQRRlrlkDFRDAYPrfppiqSIHVSQDERECTMDLS-----EFMNPSPYTVPQEASLPRVFKLFralgLRH----LV 746
Cdd:cd04584   44 GIVTDR----DLLRASP------SKATSLSIYELNYLLSkipvkDIMTKDVITVSPDDTVEEAALLM----LENkigcLP 109

                         90       100
                 ....*....|....*....|
gi 167466160 747 VVDNrNQVVGLVTRKDLARY 766
Cdd:cd04584  110 VVDG-GKLVGIITETDILRA 128
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 638-767 2.36e-04

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 41.78  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 638 PVVEHAddtqpARLQGLILRSQLIvllkhkvfversnlglvqRRLRLKDFRDAYPRFPPIQSIHVSQDERectmdLSEFM 717
Cdd:cd04600   30 PVVDRA-----RRLVGIVTLADLL------------------KHADLDPPRGLRGRLRRTLGLRRDRPET-----VGDIM 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466160 718 NPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDL--ARYR 767
Cdd:cd04600   82 TRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLiaALYR 133
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 710-763 2.37e-04

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 41.36  E-value: 2.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466160 710 TMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDL 763
Cdd:cd04588   55 NAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDI 108
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 608-766 2.50e-04

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 40.94  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 608 STPVTCLRRREKVGVIVDVLSDTasNHNGFPVVEhaDDtqpaRLQGLILRSQLIVLLKHKvfversnlglvqrrlrlkdF 687
Cdd:cd04595    1 SSPVKTVSPDTTIEEARKIMLRY--GHTGLPVVE--DG----KLVGIISRRDVDKAKHHG-------------------L 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167466160 688 RDAyprfpPIQSihvsqderectmdlseFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDLARY 766
Cdd:cd04595   54 GHA-----PVKG----------------YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVLRY 110
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
717-781 2.52e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 44.44  E-value: 2.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167466160 717 MNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYRLGKRGLEELSLAQT 781
Cdd:PRK14869  74 EIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYMDILDPEILSKSPT 138
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 710-766 2.74e-04

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


Pssm-ID: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 41.01  E-value: 2.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167466160 710 TMDLSEFMNPSPYTVPQEASLPRVFKLFraLGLRH-LV-VVDNrNQVVGLVTRKDLARY 766
Cdd:cd17772   57 DLPVSEYMTTEFATVTPDAPLSEIQEII--VEQRQrLVpVVED-GRLVGVITRTDLLNL 112
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 714-765 3.31e-04

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 40.99  E-value: 3.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd17775   64 GDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILE 115
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 718-774 4.91e-04

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 40.78  E-value: 4.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167466160 718 NPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLA--------RYRLGKRGLE 774
Cdd:cd04632    1 TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVdfvvrpgtKTRGGDRGGE 65
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 714-765 6.60e-04

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 40.11  E-value: 6.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDLAR 765
Cdd:cd04629   65 ADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDVLR 115
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 713-759 9.33e-04

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: 40.21  E-value: 9.33e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 167466160 713 LSEFMNPSPYTVpQEASLPRVFK---LFRALGLRHLVVVDNRNQVVGLVT 759
Cdd:cd04620   81 IAEVMTQPVITL-KESEFQDIFTvlsLLRQHQIRHLPIVDDQGQLVGLIT 129
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 714-766 1.20e-03

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 39.62  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDLARY 766
Cdd:cd17778    3 KEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSG-GKLVGIVTAMDIVKY 54
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 713-763 1.23e-03

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 38.93  E-value: 1.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 167466160 713 LSEFMNPSPY--TVPQEASLPRVFKLFRalglRH----LVVVDNRNQVVGLVTRKDL 763
Cdd:cd04601   56 VSEVMTPDERlvTAPEGITLEEAKEILH----KHkiekLPIVDDNGELVGLITRKDI 108
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 717-765 1.37e-03

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 39.04  E-value: 1.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 167466160 717 MNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVR 49
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 714-766 1.56e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 38.95  E-value: 1.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167466160 714 SEFMNPSPYTVPQEASlprvfkLFRAL------GLRHLVVVDNrNQVVGLVTRKDLARY 766
Cdd:cd04587   63 SEIMTPPPVTIDADAL------VFEALllmlerNIHHLPVVDD-GRVVGVVTATDLMRL 114
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 710-767 1.76e-03

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 41.58  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466160 710 TMDLSEFMNPSP--YTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARYR 767
Cdd:PLN02274 162 ETKLSEVMTSDDdlVTAPAGIDLEEAEAVLKDSKKGKLPLVNEDGELVDLVTRTDVKRVK 221
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 713-763 1.99e-03

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 39.24  E-value: 1.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 167466160 713 LSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDL 763
Cdd:cd17778   77 VEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDV 127
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 710-763 2.55e-03

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 38.25  E-value: 2.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167466160 710 TMDLSEFMNPsPYTVPQEASLPRVFKLFRALGLrHL-VVVDNRNQVVGLVTRKDL 763
Cdd:cd04590   65 KLDLRALLRP-PLFVPETTPLDDLLEEFRKERS-HMaIVVDEYGGTAGIVTLEDI 117
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 714-763 3.98e-03

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: 38.18  E-value: 3.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 167466160 714 SEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDL 763
Cdd:cd04586   86 GDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADL 134
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 702-763 4.43e-03

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 37.68  E-value: 4.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466160 702 VSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNrNQVVGLVTRKDL 763
Cdd:cd17771   52 VALPQIDLDAPISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVDN-GRLVGVVSERDL 112
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 717-766 6.41e-03

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: 37.79  E-value: 6.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 167466160 717 MNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLARY 766
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRR 50
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 712-765 9.47e-03

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: 36.56  E-value: 9.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466160 712 DLsEFMNPSPYTvpQEASLPRVFKLFRALGLRHLVVVDNRNQVVGLVTRKDLAR 765
Cdd:cd04597    1 DL-EYDKVEPLS--PETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIAR 51
 
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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