NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|778716656|ref|XP_011657577|]
View 

chloride channel protein CLC-d [Cucumis sativus]

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
SCOP:  4003598

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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. ...
43-572 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: 604.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  43 ESLDYEVIENYAYWDEQAQRGKLFVGYSVAVKWLYALFIGIGTGLAAVFINMAVENFAGWKFSLTFALIQKS-YVAGFIV 121
Cdd:cd03685    1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIEKGrLFTAFLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 122 YLAINLALVFSSVYIVTHFAPATAGSGIPEIKGYLNGIDIHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIA 201
Cdd:cd03685   81 YLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 202 SLLGQGGSSKYHLNSRWLQVFKSDRDRRDLVTCGCAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVV 281
Cdd:cd03685  161 AGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVTFTL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 282 RAAMGWCKSGKCGHFGSGGFIIWDISDGQEDYSFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHLHkKGNRVKIIE 361
Cdd:cd03685  241 NFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINH-KGKLLKVLE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 362 ACLISVLTSIISFglpllrqctpcpkpdpelgnecprppgtygnyvnfycskdneyndlatiffntqddairnlfsaktm 441
Cdd:cd03685  320 ALLVSLVTSVVAF------------------------------------------------------------------- 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 442 hefsARSLLTFLVMFYTLAVVTFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMT 521
Cdd:cd03685  333 ----PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSIDPGLYALLGAAAFLGGVMRMT 408
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 778716656 522 VSLCVIMVEISNNLKFLPLIMLVLLMSKAVGDAFNEGLYEEQAQLKGIPLL 572
Cdd:cd03685  409 VSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
593-749 7.51e-30

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: 114.15  E-value: 7.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 593 VVSFPRVAKVADVVSILRSNRHNGFPVIDYSRNGetRVIGLMLRSYLLGLLQSkvdfqhspfssdprgsissrhnfsefv 672
Cdd:cd04591   10 LTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQ--TLVGFILRSQLILLLEA--------------------------- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778716656 673 kpasskgisiddinlssedlemyiDLLPYLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPsNVVGLITRKDLL 749
Cdd:cd04591   61 ------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNG-RLVGIVTRKDLL 112
 
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. ...
43-572 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: 604.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  43 ESLDYEVIENYAYWDEQAQRGKLFVGYSVAVKWLYALFIGIGTGLAAVFINMAVENFAGWKFSLTFALIQKS-YVAGFIV 121
Cdd:cd03685    1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIEKGrLFTAFLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 122 YLAINLALVFSSVYIVTHFAPATAGSGIPEIKGYLNGIDIHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIA 201
Cdd:cd03685   81 YLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 202 SLLGQGGSSKYHLNSRWLQVFKSDRDRRDLVTCGCAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVV 281
Cdd:cd03685  161 AGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVTFTL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 282 RAAMGWCKSGKCGHFGSGGFIIWDISDGQEDYSFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHLHkKGNRVKIIE 361
Cdd:cd03685  241 NFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINH-KGKLLKVLE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 362 ACLISVLTSIISFglpllrqctpcpkpdpelgnecprppgtygnyvnfycskdneyndlatiffntqddairnlfsaktm 441
Cdd:cd03685  320 ALLVSLVTSVVAF------------------------------------------------------------------- 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 442 hefsARSLLTFLVMFYTLAVVTFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMT 521
Cdd:cd03685  333 ----PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSIDPGLYALLGAAAFLGGVMRMT 408
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 778716656 522 VSLCVIMVEISNNLKFLPLIMLVLLMSKAVGDAFNEGLYEEQAQLKGIPLL 572
Cdd:cd03685  409 VSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
129-553 4.13e-64

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: 217.80  E-value: 4.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  129 LVFSSVYIVTHFAPATAGSGIPEIKGYLNGIDihGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGqgg 208
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGGR--GPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLG--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  209 sskyhlnsRWLQvFKSDRDRRDLVTCGCAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVVRAAMGWc 288
Cdd:pfam00654  76 --------RRLF-RLSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGN- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  289 ksGKCGHFGSGGfiiwdisdgqeDYSFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHLHKKgnrvKIIEACLISVL 368
Cdd:pfam00654 146 --SPLFSVGEPG-----------SLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLKIP----PVLRPALGGLL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  369 TSIISFGLPLlrqctpcpkpdpelgnecprppgtygnyvnfycskdneyndlatiFFNTQDDAIRNLFSAKTmhefSARS 448
Cdd:pfam00654 209 VGLLGLLFPE---------------------------------------------VLGGGYELIQLLFNGNT----SLSL 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  449 LLTFLVMFYTLAVVTFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIM 528
Cdd:pfam00654 240 LLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALLFPIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIV 319
                         410       420
                  ....*....|....*....|....*
gi 778716656  529 VEISNNLKFLPLIMLVLLMSKAVGD 553
Cdd:pfam00654 320 FELTGSLQLLLPLMLAVLIAYAVSR 344
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
75-565 1.35e-37

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 145.67  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  75 WLYALFIGIGTGLAAVFINMAVENFAGWKFSLTFALIQKSYvaGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKG 154
Cdd:COG0038    8 LLLAVLVGILAGLAAVLFRLLLELATHLFLGGLLSAAGSHL--PPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 155 YLNGIDihGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGqggsskyhlnsRWLQVfkSDRDRRDLV-- 232
Cdd:COG0038   86 AIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLG-----------RLLRL--SPEDRRILLaa 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 233 -----------TcgcaagvaaafraPVGGVLFALEEVTSWWKSQLLWRVFFTSAVvavvvraamgwckSGKCGHFGSGGF 301
Cdd:COG0038  151 gaaaglaaafnA-------------PLAGALFALEVLLRDFSYRALIPVLIASVV-------------AYLVSRLLFGNG 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 302 IIWDISDGQeDYSFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHlhKKGNRVKIIeacLISVLTSIISFGLPLLrq 381
Cdd:COG0038  205 PLFGVPSVP-ALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRL--KLPPWLRPA---IGGLLVGLLGLFLPQV-- 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 382 ctpcpkpdpeLGNecprppGTygnyvnfycskdneyndlatiffntqdDAIRNLFSaktmHEFSARSLLTFLVMFYTLAV 461
Cdd:COG0038  277 ----------LGS------GY---------------------------GLIEALLN----GELSLLLLLLLLLLKLLATA 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 462 VTFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKFLPLI 541
Cdd:COG0038  310 LTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389
                        490       500
                 ....*....|....*....|....*
gi 778716656 542 MLVLLMSKAV-GDAFNEGLYEEQAQ 565
Cdd:COG0038  390 MIACVIAYLVsRLLFPRSIYTAQLE 414
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
593-749 7.51e-30

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: 114.15  E-value: 7.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 593 VVSFPRVAKVADVVSILRSNRHNGFPVIDYSRNGetRVIGLMLRSYLLGLLQSkvdfqhspfssdprgsissrhnfsefv 672
Cdd:cd04591   10 LTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQ--TLVGFILRSQLILLLEA--------------------------- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778716656 673 kpasskgisiddinlssedlemyiDLLPYLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPsNVVGLITRKDLL 749
Cdd:cd04591   61 ------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNG-RLVGIVTRKDLL 112
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
76-542 3.62e-26

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 112.29  E-value: 3.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  76 LYALFIGIGTGLAAVFINMAVENFAGWKFSLtFALIQKSYVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKGY 155
Cdd:PRK05277   2 FMAAVVGTLTGLVGVAFELAVDWVQNQRLGL-LASVADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 156 LNGidIHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIasllGQGGSSKYHLnsrwlqvfKSDRDRRDLVTCG 235
Cdd:PRK05277  81 LEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNI----GRMVLDIFRL--------RSDEARHTLLAAG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 236 CAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLwrvfftsavvavvvraamgwckSGKCGHFGS-GGFIIWDISDGQ---- 310
Cdd:PRK05277 147 AAAGLAAAFNAPLAGILFVIEEMRPQFRYSLI----------------------SIKAVFIGViMATIVFRLFNGEqavi 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 311 --EDYSFAEL--LPMTVI-GVIGGLLGALFNQLTLYITYWrrnHLHKKGNRVKIIeaclisVLTSII---SFGLPLLRQc 382
Cdd:PRK05277 205 evGKFSAPPLntLWLFLLlGIIFGIFGVLFNKLLLRTQDL---FDRLHGGNKKRW------VLMGGAvggLCGLLGLLA- 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 383 tpcpkpdpelgnecprPPGTYGNYvnfycskdneynDLATIFFNTQddairnlFSAKTMhefsarsLLTFLVMFYTlAVV 462
Cdd:PRK05277 275 ----------------PAAVGGGF------------NLIPIALAGN-------FSIGML-------LFIFVARFIT-TLL 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 463 TFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKF-LPLI 541
Cdd:PRK05277 312 CFGSGAPGGIFAPMLALGTLLGLAFGMVAAALFPQYHIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLiLPLI 391

                 .
gi 778716656 542 M 542
Cdd:PRK05277 392 I 392
CBS COG0517
CBS domain [Signal transduction mechanisms];
583-749 6.40e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 57.57  E-value: 6.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 583 ITAKEACGKRVVSFPRVAKVADVVSILRSNRHNGFPVIDysrnGETRVIGLmlrsyllgllqskvdfqhspfssdprgsI 662
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVD----EDGKLVGI----------------------------V 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 663 SSRhnfsEFVKPASSKGISIDDINLSSedlemyidllpYLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGL 742
Cdd:COG0517   49 TDR----DLRRALAAEGKDLLDTPVSE-----------VMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGI 113

                 ....*..
gi 778716656 743 ITRKDLL 749
Cdd:COG0517  114 ITIKDLL 120
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
701-749 1.24e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 46.05  E-value: 1.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 778716656  701 YLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLL 52
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
706-749 8.46e-06

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 43.27  E-value: 8.46e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 778716656   706 PYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45
 
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. ...
43-572 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: 604.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  43 ESLDYEVIENYAYWDEQAQRGKLFVGYSVAVKWLYALFIGIGTGLAAVFINMAVENFAGWKFSLTFALIQKS-YVAGFIV 121
Cdd:cd03685    1 ESLDYEVIENDLFREEWRKRKKKQVLQYEFLKWIICLLIGIFTGLVAYFIDLAVENLAGLKFLVVKNYIEKGrLFTAFLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 122 YLAINLALVFSSVYIVTHFAPATAGSGIPEIKGYLNGIDIHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIA 201
Cdd:cd03685   81 YLGLNLVLVLVAALLVAYIAPTAAGSGIPEVKGYLNGVKIPHILRLKTLLVKIVGVILSVSGGLALGKEGPMIHIGACIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 202 SLLGQGGSSKYHLNSRWLQVFKSDRDRRDLVTCGCAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVV 281
Cdd:cd03685  161 AGLSQGGSTSLRLDFRWFRYFRNDRDKRDFVTCGAAAGVAAAFGAPVGGVLFSLEEVASFWNQALTWRTFFSSMIVTFTL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 282 RAAMGWCKSGKCGHFGSGGFIIWDISDGQEDYSFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHLHkKGNRVKIIE 361
Cdd:cd03685  241 NFFLSGCNSGKCGLFGPGGLIMFDGSSTKYLYTYFELIPFMLIGVIGGLLGALFNHLNHKVTRFRKRINH-KGKLLKVLE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 362 ACLISVLTSIISFglpllrqctpcpkpdpelgnecprppgtygnyvnfycskdneyndlatiffntqddairnlfsaktm 441
Cdd:cd03685  320 ALLVSLVTSVVAF------------------------------------------------------------------- 332
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 442 hefsARSLLTFLVMFYTLAVVTFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMT 521
Cdd:cd03685  333 ----PQTLLIFFVLYYFLACWTFGIAVPSGLFIPMILIGAAYGRLVGILLGSYFGFTSIDPGLYALLGAAAFLGGVMRMT 408
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 778716656 522 VSLCVIMVEISNNLKFLPLIMLVLLMSKAVGDAFNEGLYEEQAQLKGIPLL 572
Cdd:cd03685  409 VSLTVILLELTNNLTYLPPIMLVLMIAKWVGDYFNEGIYDIIIQLKGVPFL 459
ClC_euk cd01036
Chloride channel, ClC. These domains are found in the eukaryotic halogen ion (Cl-, Br- and I-) ...
82-561 1.61e-146

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: 436.39  E-value: 1.61e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  82 GIGTGLAAVFINMAVENFAGWKFSLTFAlIQKSYVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKGYLNGIDI 161
Cdd:cd01036    1 GLLMGLVAVVLDYAVESSLDAGQWLLRR-IPGSYLLGYLMWVLWSVVLVLISSGICLYFAPQAAGSGIPEVMAYLNGVHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 162 HGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGQGGSSKYHLNSRWLQVFKSDRDRRDLVTCGCAAGVA 241
Cdd:cd01036   80 PMYLSIRTLIAKTISCICAVASGLPLGKEGPLVHLGAMIGAGLLQGRSRTLGCHVHLFQLFRNPRDRRDFLVAGAAAGVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 242 AAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVVRAAMGWCKSGKCGHFGSGGFIIWDISDGQEDYSFAELLPM 321
Cdd:cd01036  160 SAFGAPIGGLLFVLEEVSTFFPVRLAWRVFFAALVSAFVIQIYNSFNSGFELLDRSSAMFLSLTVFELHVPLNLYEFIPT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 322 TVIGVIGGLLGALFNQLTLYITYWRRNHLHKKGNRVKIIEACLISVLTSIISFglpllrqctpcpkpdpelgnecprppg 401
Cdd:cd01036  240 VVIGVICGLLAALFVRLSIIFLRWRRRLLFRKTARYRVLEPVLFTLIYSTIHY--------------------------- 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 402 tygnyvnfycskdneyndlatiffntqddairnlfsaktmhefsARSLLTFLVMFYTLAVVTFGTAVPAGQFVPGIMIGS 481
Cdd:cd01036  293 --------------------------------------------APTLLLFLLIYFWMSALAFGIAVPGGTFIPSLVIGA 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 482 TYGRLVGKFVVSFYK--------KPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKFLPLIMLVLLMSKAVGD 553
Cdd:cd01036  329 AIGRLVGLLVHRIAVagigaesaTLWADPGVYALIGAAAFLGGTTRLTFSICVIMMELTGDLHHLLPLMVAILIAKAVAD 408

                 ....*...
gi 778716656 554 AFNEGLYE 561
Cdd:cd01036  409 AFCESLYH 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 ...
82-572 7.92e-80

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: 263.70  E-value: 7.92e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  82 GIGTGLAAVFINMAVENFAGWKFSltfaliqksyVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKGYLNGIDI 161
Cdd:cd03684    1 GIAIGLIAGLIDIIASWLSDLKEG----------YCNYIIYVLLALLFAFIAVLLVKVVAPYAAGSGIPEIKTILSGFII 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 162 HGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGQgGSSKYHLNsrwlqvfksDRDRRDLVTCGCAAGVA 241
Cdd:cd03684   71 RGFLGKWTLLIKSVGLVLAVASGLSLGKEGPLVHIATCVGNIISR-LFPKYRRN---------EAKRREILSAAAAAGVA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 242 AAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVVRAAmgwcksgkcGHFGSGGFIIWDISDGQeDYSFAELLPM 321
Cdd:cd03684  141 VAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFCALVAAFTLKSL---------NPFGTGRLVLFEVEYDR-DWHYFELIPF 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 322 TVIGVIGGLLGALFNQLTLYITYWRRNHLHKKGNrvkIIEACLISVLTSIISFGLPLLRQctpcpkPDPELGNECPRPpg 401
Cdd:cd03684  211 ILLGIFGGLYGAFFIKANIKWARFRKKSLLKRYP---VLEVLLVALITALISFPNPYTRL------DMTELLELLFNE-- 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 402 tygnyvnfyCSKDNEYNDLATIFFNTQDDAIRNLFsaktmhefsarSLLTFLVMFYTLAVVTFGTAVPAGQFVPGIMIGS 481
Cdd:cd03684  280 ---------CEPGDDNSLCCYRDPPAGDGVYKALW-----------SLLLALIIKLLLTIFTFGIKVPAGIFVPSMAVGA 339
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 482 TYGRLVGKFVVSFYKK--------------PNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKFLPLIMLVLLM 547
Cdd:cd03684  340 LFGRIVGILVEQLAYSypdsiffacctagpSCITPGLYAMVGAAAFLGGVTRMTVSLVVIMFELTGALNYILPLMIAVMV 419
                        490       500
                 ....*....|....*....|....*.
gi 778716656 548 SKAVGDAFN-EGLYEEQAQLKGIPLL 572
Cdd:cd03684  420 SKWVADAIGkEGIYDAHIHLNGYPFL 445
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
129-553 4.13e-64

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: 217.80  E-value: 4.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  129 LVFSSVYIVTHFAPATAGSGIPEIKGYLNGIDihGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGqgg 208
Cdd:pfam00654   1 GGLLAGWLVKRFAPEAAGSGIPEVKAALHGGR--GPLPLRVLPVKFLGTVLTLGSGLSLGREGPSVQIGAAIGSGLG--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  209 sskyhlnsRWLQvFKSDRDRRDLVTCGCAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVVRAAMGWc 288
Cdd:pfam00654  76 --------RRLF-RLSPRDRRILLAAGAAAGLAAAFNAPLAGVLFALEELSRSFSLRALIPVLLASVVAALVSRLIFGN- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  289 ksGKCGHFGSGGfiiwdisdgqeDYSFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHLHKKgnrvKIIEACLISVL 368
Cdd:pfam00654 146 --SPLFSVGEPG-----------SLSLLELPLFILLGILCGLLGALFNRLLLKVQRLFRKLLKIP----PVLRPALGGLL 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  369 TSIISFGLPLlrqctpcpkpdpelgnecprppgtygnyvnfycskdneyndlatiFFNTQDDAIRNLFSAKTmhefSARS 448
Cdd:pfam00654 209 VGLLGLLFPE---------------------------------------------VLGGGYELIQLLFNGNT----SLSL 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  449 LLTFLVMFYTLAVVTFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIM 528
Cdd:pfam00654 240 LLLLLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGLLLALLFPIGGLPPGAFALVGMAAFLAAVTRAPLTAIVIV 319
                         410       420
                  ....*....|....*....|....*
gi 778716656  529 VEISNNLKFLPLIMLVLLMSKAVGD 553
Cdd:pfam00654 320 FELTGSLQLLLPLMLAVLIAYAVSR 344
ClC_1_like cd03683
ClC-1-like chloride channel proteins. This CD includes isoforms ClC-0, ClC-1, ClC-2 and ClC_K. ...
75-572 1.39e-50

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: 183.22  E-value: 1.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  75 WLYALFIGIGTGLAAVFINMAVENFaGWKFSLTFALIQKSYVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKG 154
Cdd:cd03683    2 WLFLALLGILMALISIAMDFAVEKL-LNARRWLYSLLTGNSLLQYLVWVAYPVALVLFSALFCKYISPQAVGSGIPEMKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 155 YLNGIDIHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGQGGSSKyhlnsrwlQVFKSDRDRR-DLVT 233
Cdd:cd03683   81 ILRGVVLPEYLTFKTLVAKVIGLTCALGSGLPLGKEGPFVHISSIVAALLSKLTTFF--------SGIYENESRRmEMLA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 234 CGCAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVVRAAMGWCKSgkcGHFGSGGFiiWDISDGQEDY 313
Cdd:cd03683  153 AACAVGVACTFGAPIGGVLFSIEVTSTYFAVRNYWRGFFAATCGAFTFRLLAVFFSD---QETITALF--KTTFFVDFPF 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 314 SFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNH--LHKKGNRVKIIEACLISVLTSIISFglPLLrqctpcpkpdpe 391
Cdd:cd03683  228 DVQELPIFALLGIICGLLGALFVFLHRKIVRFRRKNrlFSKFLKRSPLLYPAIVALLTAVLTF--PFL------------ 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 392 lgnecprppgtygnyvnfycskdneyndlatiffntqddairnlfsaktmhefsarSLLTFLVMFYTLAVVTFGTAVPAG 471
Cdd:cd03683  294 --------------------------------------------------------TLFLFIVVKFVLTALAITLPVPAG 317
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 472 QFVPGIMIGSTYGRLVGKFVVSFY-------KKPNIEEGTYALLGAASFLGGSMRmTVSLCVIMVEISNNLKFLPLIMLV 544
Cdd:cd03683  318 IFMPVFVIGAALGRLVGEIMAVLFpegirggISNPIGPGGYAVVGAAAFSGAVTH-TVSVAVIIFELTGQISHLLPVLIA 396
                        490       500
                 ....*....|....*....|....*...
gi 778716656 545 LLMSKAVGDAFNEGLYEEQAQLKGIPLL 572
Cdd:cd03683  397 VLISNAVAQFLQPSIYDSIIKIKKLPYL 424
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
82-548 1.20e-44

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: 165.43  E-value: 1.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  82 GIGTGLAAVFINMAVENFAGWKFSLTFALI-QKSYVAGFIVYLAINLALVfssVYIVTHFAPATAGSGIPE-IKGYLNGi 159
Cdd:cd00400    1 GVLSGLGAVLFRLLIELLQNLLFGGLPGELaAGSLSPLYILLVPVIGGLL---VGLLVRLLGPARGHGIPEvIEAIALG- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 160 diHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGqggsskyhlnsRWLQVfkSDRDRRDLVTCGCAAG 239
Cdd:cd00400   77 --GGRLPLRVALVKFLASALTLGSGGSVGREGPIVQIGAAIGSWLG-----------RRLRL--SRNDRRILVACGAAAG 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 240 VAAAFRAPVGGVLFALEEVTSWWKSQ----LLWRVFFTSAvvavvvraamgwcksgkCGHFGSGGFIIWDISDGQeDYSF 315
Cdd:cd00400  142 IAAAFNAPLAGALFAIEVLLGEYSVAslipVLLASVAAAL-----------------VSRLLFGAEPAFGVPLYD-PLSL 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 316 AELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHlhkkgNRVKIIEACLISVLTSIISFGLPLLrqctpcpkpdpeLGNe 395
Cdd:cd00400  204 LELPLYLLLGLLAGLVGVLFVRLLYKIERLFRRL-----PIPPWLRPALGGLLLGLLGLFLPQV------------LGS- 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 396 cprppgTYGNyvnfycskdneyndlatiffntqddairnlFSAKTMHEFSARSLLTFLVMFYTLAVVTFGTAVPAGQFVP 475
Cdd:cd00400  266 ------GYGA------------------------------ILLALAGELSLLLLLLLLLLKLLATALTLGSGFPGGVFAP 309
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778716656 476 GIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKFLPLIMLVLLMS 548
Cdd:cd00400  310 SLFIGAALGAAFGLLLPALFPGLVASPGAYALVGMAALLAAVLRAPLTAILLVLELTGDYSLLLPLMLAVVIA 382
ClcA COG0038
H+/Cl- antiporter ClcA [Inorganic ion transport and metabolism];
75-565 1.35e-37

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


Pssm-ID: 439808 [Multi-domain]  Cd Length: 415  Bit Score: 145.67  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  75 WLYALFIGIGTGLAAVFINMAVENFAGWKFSLTFALIQKSYvaGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKG 154
Cdd:COG0038    8 LLLAVLVGILAGLAAVLFRLLLELATHLFLGGLLSAAGSHL--PPWLVLLLPPLGGLLVGLLVRRFAPEARGSGIPQVIE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 155 YLNGIDihGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGqggsskyhlnsRWLQVfkSDRDRRDLV-- 232
Cdd:COG0038   86 AIHLKG--GRIPLRVAPVKFLASLLTIGSGGSLGREGPSVQIGAAIGSLLG-----------RLLRL--SPEDRRILLaa 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 233 -----------TcgcaagvaaafraPVGGVLFALEEVTSWWKSQLLWRVFFTSAVvavvvraamgwckSGKCGHFGSGGF 301
Cdd:COG0038  151 gaaaglaaafnA-------------PLAGALFALEVLLRDFSYRALIPVLIASVV-------------AYLVSRLLFGNG 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 302 IIWDISDGQeDYSFAELLPMTVIGVIGGLLGALFNQLTLYITYWRRNHlhKKGNRVKIIeacLISVLTSIISFGLPLLrq 381
Cdd:COG0038  205 PLFGVPSVP-ALSLLELPLYLLLGILAGLVGVLFNRLLLKVERLFKRL--KLPPWLRPA---IGGLLVGLLGLFLPQV-- 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 382 ctpcpkpdpeLGNecprppGTygnyvnfycskdneyndlatiffntqdDAIRNLFSaktmHEFSARSLLTFLVMFYTLAV 461
Cdd:COG0038  277 ----------LGS------GY---------------------------GLIEALLN----GELSLLLLLLLLLLKLLATA 309
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 462 VTFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKFLPLI 541
Cdd:COG0038  310 LTLGSGGPGGIFAPSLFIGALLGAAFGLLLNLLFPGLGLSPGLFALVGMAAVFAAVTRAPLTAILLVLEMTGSYSLLLPL 389
                        490       500
                 ....*....|....*....|....*
gi 778716656 542 MLVLLMSKAV-GDAFNEGLYEEQAQ 565
Cdd:COG0038  390 MIACVIAYLVsRLLFPRSIYTAQLE 414
EriC cd01031
ClC chloride channel EriC. This domain is found in the EriC chloride transporters that ...
81-561 1.21e-36

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: 142.68  E-value: 1.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  81 IGIGTGLAAVFINMAVENFAGWKFSLtfALIQKSYVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKGYLNGId 160
Cdd:cd01031    1 IGLLAGLVAVLFRLGIDKLGNLRLSL--YDFAANNPPLLLVLPLISAVLGLLAGWLVKKFAPEAKGSGIPQVEGVLAGL- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 161 iHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLgqggsskyhlnSRWLQVfkSDRDRRDLVTCGCAAGV 240
Cdd:cd01031   78 -LPPNWWRVLPVKFVGGVLALGSGLSLGREGPSVQIGAAIGQGV-----------SKWFKT--SPEERRQLIAAGAAAGL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 241 AAAFRAPVGGVLFALEEVTSWWKSQLLWRVFFTSAvvavvvraamgwcksgkcghfgSGGFIIW-------DISDGQEDY 313
Cdd:cd01031  144 AAAFNAPLAGVLFVLEELRHSFSPLALLTALVASI----------------------AADFVSRlffglgpVLSIPPLPA 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 314 SFAELLPMTVI-GVIGGLLGALFNQLTLYITYWRRNhLHKKGNRVKIIeacLISVLTSIISFGLPLLrqctpcpkpdpeL 392
Cdd:cd01031  202 LPLKSYWLLLLlGIIAGLLGYLFNRSLLKSQDLYRK-LKKLPRELRVL---LPGLLIGPLGLLLPEA------------L 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 393 GNecprppgtyGNYVNFYcskdneyndlatifFNTQDDAIRNLFSAktmheFSARSLLTFLvmfytlavvTFGTAVPAGQ 472
Cdd:cd01031  266 GG---------GHGLILS--------------LAGGNFSISLLLLI-----FVLRFIFTML---------SYGSGAPGGI 308
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 473 FVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLK-FLPLiMLVLLMSKAV 551
Cdd:cd01031  309 FAPMLALGALLGLLFGTILVQLGPIPISAPATFAIAGMAAFFAAVVRAPITAIILVTEMTGNFNlLLPL-MVVCLVAYLV 387
                        490
                 ....*....|.
gi 778716656 552 GDAFNEG-LYE 561
Cdd:cd01031  388 ADLLGGKpIYE 398
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
593-749 7.51e-30

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: 114.15  E-value: 7.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 593 VVSFPRVAKVADVVSILRSNRHNGFPVIDYSRNGetRVIGLMLRSYLLGLLQSkvdfqhspfssdprgsissrhnfsefv 672
Cdd:cd04591   10 LTVLARDETVGDIVSVLKTTDHNGFPVVDSTESQ--TLVGFILRSQLILLLEA--------------------------- 60
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778716656 673 kpasskgisiddinlssedlemyiDLLPYLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPsNVVGLITRKDLL 749
Cdd:cd04591   61 ------------------------DLRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNG-RLVGIVTRKDLL 112
PRK05277 PRK05277
H(+)/Cl(-) exchange transporter ClcA;
76-542 3.62e-26

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


Pssm-ID: 235385 [Multi-domain]  Cd Length: 438  Bit Score: 112.29  E-value: 3.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  76 LYALFIGIGTGLAAVFINMAVENFAGWKFSLtFALIQKSYVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKGY 155
Cdd:PRK05277   2 FMAAVVGTLTGLVGVAFELAVDWVQNQRLGL-LASVADNGLLLWIVAFLISAVLAMIGYFLVRRFAPEAGGSGIPEIEGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 156 LNGidIHGVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIasllGQGGSSKYHLnsrwlqvfKSDRDRRDLVTCG 235
Cdd:PRK05277  81 LEG--LRPVRWWRVLPVKFFGGLGTLGSGMVLGREGPTVQMGGNI----GRMVLDIFRL--------RSDEARHTLLAAG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 236 CAAGVAAAFRAPVGGVLFALEEVTSWWKSQLLwrvfftsavvavvvraamgwckSGKCGHFGS-GGFIIWDISDGQ---- 310
Cdd:PRK05277 147 AAAGLAAAFNAPLAGILFVIEEMRPQFRYSLI----------------------SIKAVFIGViMATIVFRLFNGEqavi 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 311 --EDYSFAEL--LPMTVI-GVIGGLLGALFNQLTLYITYWrrnHLHKKGNRVKIIeaclisVLTSII---SFGLPLLRQc 382
Cdd:PRK05277 205 evGKFSAPPLntLWLFLLlGIIFGIFGVLFNKLLLRTQDL---FDRLHGGNKKRW------VLMGGAvggLCGLLGLLA- 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 383 tpcpkpdpelgnecprPPGTYGNYvnfycskdneynDLATIFFNTQddairnlFSAKTMhefsarsLLTFLVMFYTlAVV 462
Cdd:PRK05277 275 ----------------PAAVGGGF------------NLIPIALAGN-------FSIGML-------LFIFVARFIT-TLL 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 463 TFGTAVPAGQFVPGIMIGSTYGRLVGKFVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKF-LPLI 541
Cdd:PRK05277 312 CFGSGAPGGIFAPMLALGTLLGLAFGMVAAALFPQYHIEPGTFAIAGMGALFAATVRAPLTGIVLVLEMTDNYQLiLPLI 391

                 .
gi 778716656 542 M 542
Cdd:PRK05277 392 I 392
EriC_like cd01034
ClC chloride channel family. These protein sequences, closely related to the ClC Eric family, ...
86-560 8.53e-19

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: 89.21  E-value: 8.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656  86 GLAAVFINMAVEnfagwkfsLTFALIQKSYVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKGYL---NGIDIH 162
Cdd:cd01034    1 GLVALLFAKLAD--------LALALFQRLTATHPWLPLLLTPAGFALIAWLTRRFFPGAAGSGIPQVIAALelpSAAARR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 163 GVLFFRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIAsllgqggsskYHLNSRWLQvfKSDRDRRDLVTCGCAAGVAA 242
Cdd:cd01034   73 RLLSLRTAVGKILLTLLGLLGGASVGREGPSVQIGAAVM----------LAIGRRLPK--WGGLSERGLILAGGAAGLAA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 243 AFRAPVGGVLFALEEVTSW----WKSQLLWRVFFTSAVVAVVVraamgwcksGKCGHFG--SGGFIIWDIsdgqedysfa 316
Cdd:cd01034  141 AFNTPLAGIVFAIEELSRDfelrFSGLVLLAVIAAGLVSLAVL---------GNYPYFGvaAVALPLGEA---------- 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 317 eLLPMTVIGVIGGLLGALFNQLTLYITYWRRNHLHKKGNRVKIIEACLISVLTSIIsfglpllrqctpcpkpdpelgnec 396
Cdd:cd01034  202 -WLLVLVCGVVGGLAGGLFARLLVALSSGLPGWVRRFRRRRPVLFAALCGLALALI------------------------ 256
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 397 prppGTYgnyvnfycSKDNEYNDlatiffntqddairNLFSAKTMHEFSARSLLTFLVMFYTLAVVTFGTAVPAGQFVPG 476
Cdd:cd01034  257 ----GLV--------SGGLTFGT--------------GYLQARAALEGGGGLPLWFGLLKFLATLLSYWSGIPGGLFAPS 310
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 477 IMIGSTYGRLVGKFVvsfykkPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISNNLKFLPLIMLVLLMSKAVGDAF- 555
Cdd:cd01034  311 LAVGAGLGSLLAALL------GSVSQGALVLLGMAAFLAGVTQAPLTAFVIVMEMTGDQQMLLPLLAAALLASGVSRLVc 384

                 ....*
gi 778716656 556 NEGLY 560
Cdd:cd01034  385 PEPLY 389
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
506-749 2.20e-11

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 64.13  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 506 ALLGAASFLGGSMRMTVSLCVIMVEISNNLKFLPLIMLVLLMSKAVGDAFNEGLYEEQAQLKGIPLLESRPkyQMRKITA 585
Cdd:COG2524   11 LLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELG--LVLKMKV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 586 KEACGKRVVSFPRVAKVADVVSILRSNRHNGFPVIDysrNGetRVIGLmlrsyllgllqskvdfqhspfssdprgsISSR 665
Cdd:COG2524   89 KDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD---DG--KLVGI----------------------------ITER 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 666 HnfsefVKPASSKGISIDDINLSSedlemyidllpYLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITR 745
Cdd:COG2524  136 D-----LLKALAEGRDLLDAPVSD-----------IMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITR 199

                 ....
gi 778716656 746 KDLL 749
Cdd:COG2524  200 TDIL 203
CBS COG0517
CBS domain [Signal transduction mechanisms];
583-749 6.40e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 57.57  E-value: 6.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 583 ITAKEACGKRVVSFPRVAKVADVVSILRSNRHNGFPVIDysrnGETRVIGLmlrsyllgllqskvdfqhspfssdprgsI 662
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVD----EDGKLVGI----------------------------V 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 663 SSRhnfsEFVKPASSKGISIDDINLSSedlemyidllpYLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGL 742
Cdd:COG0517   49 TDR----DLRRALAAEGKDLLDTPVSE-----------VMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGI 113

                 ....*..
gi 778716656 743 ITRKDLL 749
Cdd:COG0517  114 ITIKDLL 120
ClC_like cd01033
Putative ClC chloride channel. Clc proteins are putative halogen ion (Cl-, Br- and I-) ...
167-547 4.77e-08

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


Pssm-ID: 238505 [Multi-domain]  Cd Length: 388  Bit Score: 56.15  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 167 FRTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLgqggsskyhlnSRWLQVfkSDRDRRDLVTCGCAAGVAAAFRA 246
Cdd:cd01033   82 FWETIIHAVLQIVTVGLGAPLGREVAPREVGALLAQRF-----------SDWLGL--TVADRRLLVACAAGAGLAAVYNV 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 247 PVGGVLFALEEVTSWWKSQLLWRVFFTSAVVAVVvraamgwcksgkcGHFGSGGFIIWDISdgQEDYSFAELLPMTVIGV 326
Cdd:cd01033  149 PLAGALFALEILLRTISLRSVVAALATSAIAAAV-------------ASLLKGDHPIYDIP--PMQLSTPLLIWALLAGP 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 327 IGGLLGALFNQLTLYITywrrnhlHKKGNRVKIIEACLI-SVLTSIISFGLPLLrqctpcpkpdpeLGNecPRPPGTYGn 405
Cdd:cd01033  214 VLGVVAAGFRRLSQAAR-------AKRPKGKRILWQMPLaFLVIGLLSIFFPQI------------LGN--GRALAQLA- 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 406 yvnfycskdneyndlatiffntqddairnlfsaktMHEFSARSLLTFLVMFYTLAV-VTFGTAVPAGQFVPGIMIGSTYG 484
Cdd:cd01033  272 -----------------------------------FSTTLTLSLLLILLVLKIVATlLALRAGAYGGLLTPSLALGALLG 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 778716656 485 RLVGkfVVSFYKKPNIEEGTYALLGAASFLGGSMRMTVSLCVIMVEISnnlkFLPLIMLVLLM 547
Cdd:cd01033  317 ALLG--IVWNALLPPLSIAAFALIGAAAFLAATQKAPLTALILVLEFT----RQNPLFLIPLM 373
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
701-749 1.24e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 46.05  E-value: 1.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 778716656  701 YLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLL 52
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
591-749 1.35e-06

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 47.62  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 591 KRVVSFPRVAKVADVVSILRSNRHNGFPVIDysRNGEtrviglmlrsyLLGLLqSKVDFQHSPFSSDprgsissrhnfse 670
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVD--DDGK-----------LVGIV-TERDILRALVEGG------------- 54
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 778716656 671 fvkpaSSKGISIDDInlssedlemyidllpyLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:cd02205   55 -----LALDTPVAEV----------------MTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
583-749 3.43e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 47.17  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 583 ITAKEACGKRVVSFPRVAKVADVVSILRSNRHNGFPVIDysrnGETRVIGLMlrsyllgllqskvdfqhspfssdprgsi 662
Cdd:COG3448    2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVD----EDGRLVGIV---------------------------- 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 663 sSRHNFSEFVKPASSKGISIDDINLSSEDLeMyidllpylNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGL 742
Cdd:COG3448   50 -TERDLLRALLPDRLDELEERLLDLPVEDV-M--------TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGI 119

                 ....*..
gi 778716656 743 ITRKDLL 749
Cdd:COG3448  120 VTRTDLL 126
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
706-749 8.46e-06

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 43.27  E-value: 8.46e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 778716656   706 PYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
591-749 1.14e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 45.67  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 591 KRVVSFPRVAKVADVVSILRSNRHNGFPVIDysrnGETRVIGLmlrsyllgllqskvdfqhspfssdprgsissrhnfse 670
Cdd:COG4109   25 EDVATLSEDDTVEDALELLEKTGHSRFPVVD----ENGRLVGI------------------------------------- 63
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 778716656 671 fvkpasskgISIDDInLSSEDLEMYIDLLpylNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:COG4109   64 ---------VTSKDI-LGKDDDTPIEDVM---TKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
701-767 8.49e-05

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 43.32  E-value: 8.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 701 YLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL---IEDSEDSDAMELQSTSVR 767
Cdd:COG3448    7 IMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLralLPDRLDELEERLLDLPVE 76
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
696-749 2.94e-04

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


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 41.33  E-value: 2.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 778716656 696 IDLLPYLNPsPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:cd04590   66 LDLRALLRP-PLFVPETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
75-206 3.75e-04

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: 43.31  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656   75 WLYALFIGIGTGLAAVFinmavenfagwkFSLTFALIQKSYVAGFIVYLAINLALVFSSVYIVTHFAPATAGSGIPEIKG 154
Cdd:pfam00654 162 LPLFILLGILCGLLGAL------------FNRLLLKVQRLFRKLLKIPPVLRPALGGLLVGLLGLLFPEVLGGGYELIQL 229
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 778716656  155 YLNGIDIHGVLFFrTLIGKIFGSIGSVGGGLALGKEGPLVHTGACIASLLGQ 206
Cdd:pfam00654 230 LFNGNTSLSLLLL-LLLLKFLATALSLGSGAPGGIFAPSLAIGAALGRAFGL 280
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
706-771 4.66e-04

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: 40.31  E-value: 4.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 778716656 706 PYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLLIEDSEDSDAMELQSTSVRARRP 771
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDV 69
CBS COG0517
CBS domain [Signal transduction mechanisms];
701-767 6.79e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 40.23  E-value: 6.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 778716656 701 YLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLLIEdsEDSDAMELQSTSVR 767
Cdd:COG0517    6 IMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRA--LAAEGKDLLDTPVS 70
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
701-762 9.22e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 41.41  E-value: 9.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 778716656 701 YLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVpRPSNVVGLITRKDLLIEDSEDSDAMELQ 762
Cdd:COG2524   91 IMTKDVITVSPDTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDLLKALAEGRDLLDAP 151
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
600-749 2.90e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 38.27  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 600 AKVADVVSILRSNRHNGFPVIDysrnGETRVIGLmlrsyllgllqskvdfqhspfssdprgsISSRhnfsEFVKPASSKG 679
Cdd:COG2905   16 ATVREAARLMTEKGVGSLVVVD----DDGRLVGI----------------------------ITDR----DLRRRVLAEG 59
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 778716656 680 ISIDDINLSSedlemyidllpYLNPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVpRPSNVVGLITRKDLL 749
Cdd:COG2905   60 LDPLDTPVSE-----------VMTRPPITVSPDDSLAEALELMEEHRIRHLPVV-DDGKLVGIVSITDLL 117
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
592-644 4.55e-03

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 35.95  E-value: 4.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 778716656   592 RVVSFPRVAKVADVVSILRSNRHNGFPVIDysrnGETRVIGLMLRSYLLGLLQ 644
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVD----EEGRLVGIVTRRDIIKALA 49
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
703-749 4.96e-03

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


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 37.42  E-value: 4.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 778716656 703 NPSPYIVPEDMSLTKVYNLFRQLGLRHAFVVPRPSNVVGLITRKDLL 749
Cdd:cd04607   65 NKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLL 111
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH