NCBI Conserved Domain Search

HPP family; These proteins are integral membrane proteins with four transmembrane spanning helices. The most conserved region of the alignment is a motif HPP. The function of these proteins is uncertain but they may be transporters.

Pssm-ID: 461506 Cd Length: 122 Bit Score: 157.29 E-value: 2.14e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819  64 IVAPIGASAVLLFAVPVSPLAQPWSIIGGNTISALIGVSVTYIVADQM--LAIGLAVALAILAMSLTRSLHPPGGAAALT 141
Cdd:pfam04982   1 LIASFGASAVLLFGAPESPLAQPRNVVGGHLISALIGVAIAKLFGLSLlwLAAALAVALAIALMQLTRTLHPPAGATALL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1553175819 142 AVIGGaAVARSGFWFPFIPVAINSLILVGLGMVFHRLARRQYP 184
Cdd:pfam04982  81 AVLGG-PIHALGWWFVLVPVLLGSLLLVLVALLVNNLTGRRYP 122

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 113.42 E-value: 1.56e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 250 LTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGKEPGSKLP---------------IS 314
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlldlpvedvmTR 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1553175819 315 AAATARPSDPAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLLATLAKSLSHN 369
Cdd:COG3448    82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136

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: 86.46 E-value: 1.39e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGL-----------------RELAGKEPGSKLPISAAA- 317
Cdd:cd04600     1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLadllkhadldpprglrgRLRRTLGLRRDRPETVGDi 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1553175819 318 ------TARPSDPAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLLATLAK 364
Cdd:cd04600    81 mtrpvvTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLIAALYR 133

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 74.90 E-value: 1.94e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL-----AGKEPGSKLPISAAA-----TARPS 322
Cdd:COG0517     4 KDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLrralaAEGKDLLDTPVSEVMtrppvTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1553175819 323 DPAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLLATLAKSLS 367
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128

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: 71.89 E-value: 1.56e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 257 SRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVG----LRELAGKEPGSKLPISAAA-----TARPSDPAIG 327
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTerdiLRALVEGGLALDTPVAEVMtpdviTVSPDTDLEE 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1553175819 328 LLPRLTDGATHAVVILDDDGKVVGIISQTDLLA 360
Cdd:cd02205    81 ALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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: 71.30 E-value: 4.64e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENeKLQGTVGLRELAGKEPG--------------SKLPISAA-- 316
Cdd:cd04584     3 KDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDG-KLVGIVTDRDLLRASPSkatslsiyelnyllSKIPVKDImt 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 317 ---ATARPSDPA-----------IGLLPrltdgathaVVildDDGKVVGIISQTDLLATL 362
Cdd:cd04584    82 kdvITVSPDDTVeeaallmlenkIGCLP---------VV---DGGKLVGIITETDILRAF 129

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 71.48 E-value: 4.90e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIM-SRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGKEPG-------SKLPIsaaaTARPSDPA 325
Cdd:COG4109    20 DIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDtpiedvmTKNPI----TVTPDTSL 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1553175819 326 IGLLPRLT-DGATHAVVIlDDDGKVVGIISQTDLLATLAK 364
Cdd:COG4109    96 ASAAHKMIwEGIELLPVV-DDDGRLLGIISRQDVLKALQK 134

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 70.68 E-value: 3.38e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 233 ALLREVELQALIRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDeNEKLQGTVG----LRELAGKEPG 308
Cdd:COG2524    69 AAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITerdlLKALAEGRDL 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1553175819 309 SKLPISAAA-----TARPSDPAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLLATL 362
Cdd:COG2524   148 LDAPVSDIMtrdvvTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 67.16 E-value: 1.27e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL-----AGKEPGSKLPISAAA-----TARPS 322
Cdd:COG2905     2 KDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLrrrvlAEGLDPLDTPVSEVMtrppiTVSPD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1553175819 323 DPAIGLLPRLTD-GATHAVVIldDDGKVVGIISQTDLLATLAKSL 366
Cdd:COG2905    82 DSLAEALELMEEhRIRHLPVV--DDGKLVGIVSITDLLRALSEEL 124

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 60.26 E-value: 3.43e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1553175819 226 VSREDIdalLREVELQAliRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELA 303
Cdd:COG0517    48 VTDRDL---RRALAAEG--KDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLL 120

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 59.88 E-value: 5.14e-11

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1553175819 226 VSREDIDALLREVELQALIRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:COG3448    49 VTERDLLRALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDL 125

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

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 57.93 E-value: 1.76e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 250 LTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVG----LRELAGKEPGSKLPISAAATAR----- 320
Cdd:cd04608     2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTegnlLSSLLAGRAQPSDPVSKAMYKQfkqvd 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1553175819 321 PSDPAIGLLPRLTDGatHAVVILDDDGKVVGIISQTDLLA 360
Cdd:cd04608    82 LDTPLGALSRILERD--HFALVVDGQGKVLGIVTRIDLLN 119

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 59.51 E-value: 2.74e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 106 IVADQMLAIGLAVALAILAMSLTRSLHPPGGAAALTAVIGGAAVARSGFWFPFIPVAINSLILVGLGMVFHRLARRQYPH 185
Cdd:COG2524     1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 186 RPGVAPVNTHATADPPPALRVgfnSEDIDSAIARLNET-------LD-------VSREDIDALLREVelqaliRQRGELT 251
Cdd:COG2524    81 GLVLKMKVKDIMTKDVITVSP---DTTLEEALELMLEKgisglpvVDdgklvgiITERDLLKALAEG------RDLLDAP 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1553175819 252 CADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:COG2524   152 VSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202

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: 53.76 E-value: 1.24e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:pfam00571   2 KDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 54.17 E-value: 3.58e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELA-----GKEPGSKLPISAAATARPSDPAIGL 328
Cdd:cd04605     4 DIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISkavalKKDSLEEIMTRNVITARPDEPIELA 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1553175819 329 LPRLTDGATHAVVILDDDGKVVGIISQTDL 358
Cdd:cd04605    84 ARKMEKHNISALPVVDDDRRVIGIITSDDI 113

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: 53.02 E-value: 7.54e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1553175819 249 ELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:cd02205    58 DTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111

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

Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 51.95 E-value: 2.36e-08

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1553175819 234 LLREVELQALIRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTV 297
Cdd:cd04606    49 LLGVVSLRDLLLADPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGII 112

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

Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 51.57 E-value: 3.38e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 255 IMSRDVVTVPGDTTPDHA-RYL----LLKHDIRTLPVLDENEKLQGTVGLRELagkepgsklpISAAATARPSDpaigll 329
Cdd:cd04606     6 LMTTEFVAVRPDWTVEEAlEYLrrlaPDPETIYYIYVVDEDRRLLGVVSLRDL----------LLADPDTKVSD------ 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1553175819 330 prLTDGATHAVVILDDDGKVVGIISQTDLLA 360
Cdd:cd04606    70 --IMDTDVISVSADDDQEEVARLFAKYDLLA 98

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: 51.27 E-value: 3.66e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENeKLQGTVG-----LRELAGKEPGSKLPISAAATA-----RPSDP- 324
Cdd:cd04622     1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGD-RLVGMVTdrdivVRAVAEGKDPNTTTVREVMTGdvvtcSPDDDv 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1553175819 325 --AIGLLprltdgATHAV---VILDDDGKVVGIISQTDL 358
Cdd:cd04622    80 eeAARLM------AEHQVrrlPVVDDDGRLVGIVSLGDL 112

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

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 50.49 E-value: 5.93e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 257 SRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVG----LRELAGKEPGSK-LPISAA-----ATARPSDPAI 326
Cdd:cd04623     1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSerdyVRKLALRGASSLdTPVSEImtrdvVTCTPDDTVE 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1553175819 327 GLLPRLTDGAT-HAVVIldDDGKVVGIISQTDL 358
Cdd:cd04623    81 ECMALMTERRIrHLPVV--EDGKLVGIVSIGDV 111

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: 50.21 E-value: 7.36e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVG----LRELAGKEPGSkLPISAAA-----TARPSDPAI 326
Cdd:cd09836     1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTerdiVRAVAEGIDLD-TPVEEIMtknlvTVSPDESIY 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1553175819 327 GLLPRLTDGATHAVVILDDDGKVVGIISQTDLLATLA 363
Cdd:cd09836    80 EAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116

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: 50.02 E-value: 1.16e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 257 SRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGK--EPGSK---------------LPI-----S 314
Cdd:cd04632     1 TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFvvRPGTKtrggdrggekermldLPVydimsS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1553175819 315 AAATARPSDPAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLL 359
Cdd:cd04632    81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVL 125

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: 50.12 E-value: 1.27e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1553175819 239 ELQALIRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENeKLQGTVGLREL 302
Cdd:cd04586    72 RLAEEYVKAHGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDG-KLVGIVSRADL 134

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: 50.12 E-value: 1.54e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVG----LRELAGKEPGSKLPI------------------ 313
Cdd:cd04586     1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSegdlLRREEPGTEPRRVWWldallesperlaeeyvka 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1553175819 314 ----------SAAATARPSDP---AIGLLprltdgATHAV----VIldDDGKVVGIISQTDLL 359
Cdd:cd04586    81 hgrtvgdvmtRPVVTVSPDTPleeAARLM------ERHRIkrlpVV--DDGKLVGIVSRADLL 135

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];

Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 52.81 E-value: 1.92e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819  88 SIIGGNTISALIGVSVTYIVADQMLAIGLAVALAILAMSLtrslhppggaaaLTAVIGGaavarsgfwfpFIP--VAIN- 164
Cdd:COG1253    75 GALGEAALAALLAPLLGSLGLPAALAHTLALVLAVVLITF------------LSLVFGE-----------LVPkrLALQn 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 165 ----SLILVGLGMVFHRLARrqyphrPGVAPVNTHATAdpppALR-VGFNSEDIDSAiarlnetldVSREDIDALLREVE 239
Cdd:COG1253   132 pervALLVAPPLRLFSRLFR------PLVWLLNGSTNL----LLRlLGIEPAEEEPA---------VTEEELRALVEESE 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 240 LQALIRQR-----------GELTCADIMS--RDVVTVPGDTTPDHARYLLLKHDIRTLPVLDEN-EKLQGTVGLRELAgK 305
Cdd:COG1253   193 ESGVIEEEeremienvfefGDRTVREVMTprTDVVALDLDDTLEEALELILESGHSRIPVYEGDlDDIVGVVHVKDLL-R 271

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 306 EPGSKLPISAAATARP------SDPAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLL 359
Cdd:COG1253   272 ALLEGEPFDLRDLLRPplfvpeTKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDIL 331

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

Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 49.03 E-value: 2.07e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1553175819 226 VSREDIDALLREVELQALIRQrgeltcadIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENE 291
Cdd:cd04595    40 ISRRDVDKAKHHGLGHAPVKG--------YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGK 97

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: 49.34 E-value: 2.35e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1553175819 226 VSREDI-DAL------LREVELQALIRQrgeLTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENeKLQGTV 297
Cdd:cd04584    46 VTDRDLlRASpskatsLSIYELNYLLSK---IPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGG-KLVGII 120

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 52.53 E-value: 2.46e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1553175819 249 ELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELA 303
Cdd:PRK14869   67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLA 121

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

Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 48.19 E-value: 4.50e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 258 RDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGK------EPGSKLP---ISAAATARPSDPAIGL 328
Cdd:cd17784     2 KNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNlildkyELGTTVEevmVKDVATVHPDETLLEA 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1553175819 329 LPRLTDGATHAVVI----LDDDGKVVGIISQTDLLATLA 363
Cdd:cd17784    82 IKKMDSNAPDEEIInqlpVVDDGKLVGIISDGDIIRAIK 120

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: 47.41 E-value: 7.50e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1553175819 251 TCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELA 303
Cdd:cd04622    61 TVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDLA 113

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: 47.18 E-value: 1.01e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLdENEKLQGTVGLRELAGKEPG-----------SKLPIsaaaTARPS 322
Cdd:cd04801     1 DIMTPEVVTVTPEMTVSELLDRMFEEKHLGYPVV-ENGRLVGIVTLEDIRKVPEVereatrvrdvmTKDVI----TVSPD 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1553175819 323 DPAIGLLPRLTDGATHAVVILDDdGKVVGIISQTDLL 359
Cdd:cd04801    76 ADAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111

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: 46.72 E-value: 1.15e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 260 VVTVPGDTTPDHARYLLLKHDIRTLPVLdENEKLQGTVGLREL--AGKEPGSKLPISA-----AATARPSDPA------- 325
Cdd:cd04595     4 VKTVSPDTTIEEARKIMLRYGHTGLPVV-EDGKLVGIISRRDVdkAKHHGLGHAPVKGymstnVITIDPDTSLeeaqelm 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1553175819 326 ----IGLLPrltdgathaVVildDDGKVVGIISQTDLL 359
Cdd:cd04595    83 vehdIGRLP---------VV---EEGKLVGIVTRSDVL 108

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: 47.33 E-value: 1.33e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1553175819 245 RQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRE-LAGKE 306
Cdd:cd04611    62 RHPGNTPVGELASRPLLTVGAEDSLIHARDLLIDHRIRHLAVVDEDGQVTGLLGFADlLAGVE 124

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: 46.77 E-value: 1.47e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELA------GKEPgSKLPISA-----AATARPSDP 324
Cdd:cd17775     1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVvevvakGLDP-KDVTVGDimsadLITAREDDG 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1553175819 325 AIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLLATL 362
Cdd:cd17775    80 LFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 49.68 E-value: 1.52e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 218 ARLNETLD----VSREDIdaLLREVELQALIRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKL 293
Cdd:COG2239   159 AEDPETIYyiyvVDDDGR--LVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRL 236


                  ..
gi 1553175819 294 QG 295
Cdd:COG2239   237 VG 238

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: 46.36 E-value: 1.66e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 251 TCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENE--KLQGTVGLRELA---GKEPGSKLPISaAATARPSDPa 325
Cdd:cd04591     1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTEsqTLVGFILRSQLIlllEADLRPIMDPS-PFTVTEETS- 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1553175819 326 iglLPRLTD-----GATHAVVIldDDGKVVGIISQTDLL 359
Cdd:cd04591    79 ---LEKVHDlfrllGLRHLLVT--NNGRLVGIVTRKDLL 112

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: 45.99 E-value: 1.96e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 257 SRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDeNEKLQGTVGLRELA-----GKEPG------SKLPISAAATARPSDpA 325
Cdd:cd04588     1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVD-DGKLVGIVTLTDIAkalaeGKENAkvkdimTKDVITIDKDEKIYD-A 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1553175819 326 IGLLP-----RLtdgathavVILDDDGKVVGIISQTDLL 359
Cdd:cd04588    79 IRLMNkhnigRL--------IVVDDNGKPVGIITRTDIL 109

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 46.36 E-value: 2.14e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1553175819 249 ELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENeKLQGTVGLRELA 303
Cdd:COG2905    64 DTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDG-KLVGIVSITDLL 117

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: 45.25 E-value: 4.83e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 257 SRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKlqGTVGL--RELA--------GKEPGSKLPISAAATARPSDPai 326
Cdd:cd17772     1 SSPVISVEPDTTIAEAAELMTRYNINALPVVDGGTG--RLVGIitRQVAekaiyhglGDLPVSEYMTTEFATVTPDAP-- 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1553175819 327 glLPRLTD---GATHAVVILDDDGKVVGIISQTDLL 359
Cdd:cd17772    77 --LSEIQEiivEQRQRLVPVVEDGRLVGVITRTDLL 110

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: 45.01 E-value: 8.50e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENE-------------------KLQGTVGLRELAGKEPGSKLPIS 314
Cdd:cd17778     4 EFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKlvgivtamdivkyfgsheaKKRLTTGDIDEAYSTPVEEIMSK 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1553175819 315 AAATARPsDPAIGLLPRLTDGA-THAVVILDDDGKVVGIISQTDLLATL 362
Cdd:cd17778    84 EVVTIEP-DADIAEAARLMIKKnVGSLLVVDDEGELKGIITERDVLIAL 131

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

Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 44.23 E-value: 9.02e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENeKLQGTVGLRELAGKEPGSKL-------PISAAATARPSDPA--- 325
Cdd:cd04610     1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDG-KVVGYVTAKDLLGKDDDEKVseimsrdTVVADPDMDITDAArvi 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1553175819 326 ----IGLLPrltdgathaVVilDDDGKVVGIISQTD 357
Cdd:cd04610    80 frsgISKLP---------VV--DDEGNLVGIITNMD 104

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: 44.07 E-value: 1.04e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1553175819 248 GELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:cd17775    59 KDVTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 46.60 E-value: 1.50e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 255 IMSRDVVTVPGDTTPDHA-RYL----LLKHDIRTLPVLDENEKLQGTVGLRELAGKEPGSKL-------PISAAATARPS 322
Cdd:COG2239   134 LMTTEFVAVREDWTVGEAlRYLrrqaEDPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVsdimdtdVISVPADDDQE 213

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1553175819 323 DPA-----IGLLprltdgathAVVILDDDGKVVGII 353
Cdd:COG2239   214 EVArlferYDLL---------ALPVVDEEGRLVGII 240

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];

Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 42.70 E-value: 2.09e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMSRDVVTV-PGDTTPDHARYLLLKHDIRTLPVLdeneKLQGtVGLRELAGKEPGsklpisaaatarPSDPAIGLLPR 331
Cdd:COG3620     2 RDLMSRDVVTVsPDDTLGEALRLMRKELGLSQLPVA----ELVG-VSQSDILRIESG------------KRDPTVSTLEK 64

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1553175819 332 LTD--GATHAVVILDDDGKVVGIISQTDLLA 360
Cdd:COG3620    65 IAEalGKELSAVLVVDDGKLVGIITRRDLLK 95

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: 43.28 E-value: 2.12e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELA 303
Cdd:cd09836    63 EIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLA 112

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; 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: 341402 [Multi-domain] Cd Length: 116 Bit Score: 43.32 E-value: 2.35e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRDVVTV---PGDTtPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGKEPGSKLPISAA-----ATARPSDPA 325
Cdd:cd09831     1 DIARKTQVTViekTGDG-PRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENAQSLEDAfltdvETVPADTSL 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1553175819 326 IGLLPRLTDgATHAVVILDDDGKVVGIISQTDLLATLA 363
Cdd:cd09831    80 SDILGLVAS-APCPLPVVDEDGRYLGVISKASLLETLD 116

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

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 42.79 E-value: 3.08e-05

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENE 291
Cdd:cd04623    63 SEIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVEDGK 101

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: 40.57 E-value: 3.74e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1553175819  259 DVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44

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

Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 44.69 E-value: 6.00e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1553175819 253 ADIMSRD-VVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQG 295
Cdd:pfam00478 142 SEVMTKEnLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVG 185

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

Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 41.93 E-value: 7.67e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1553175819 226 VSREDI-DALLREVELQALIRQRGE------LTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTV 297
Cdd:cd04632    41 VTTYDIvDFVVRPGTKTRGGDRGGEkermldLPVYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGIL 119

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

Pssm-ID: 341396 [Multi-domain] Cd Length: 109 Bit Score: 41.56 E-value: 7.99e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1553175819 243 LIRQRGELTCADIMSRDVVTV-PGDTTPDHARyLLLKHDIRTLPVLDENeKLQGTV 297
Cdd:cd04638    48 LLRNPDEEQIALLMSRDPITIsPDDTLSEAAE-LMLEHNIRRVPVVDDD-KLVGIV 101

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: 41.75 E-value: 1.14e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1553175819 249 ELTCADIMSRDVVTVPGDTTPD--HARYLLLKHDIRTLPVLDENEKLQGTV 297
Cdd:cd04620    78 GVTIAEVMTQPVITLKESEFQDifTVLSLLRQHQIRHLPIVDDQGQLVGLI 128

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: 341359 [Multi-domain] Cd Length: 111 Bit Score: 41.22 E-value: 1.15e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGKEP--GSKL-PISAAATARpsDPAIGLLP 330
Cdd:cd04582     1 EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDARGASGtcGDFAhPFKATVPVD--ENLRVVLS 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1553175819 331 RLTDGATHAVVILDDDGKVVGIISQTDLLATLA 363
Cdd:cd04582    79 RMYEHNTSWLPVVDEDGRYAGEVTQDSIADYLS 111

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

Pssm-ID: 341396 [Multi-domain] Cd Length: 109 Bit Score: 40.79 E-value: 1.39e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVL-DENEKLQGTVGLRELAGKEPGSKLPI---SAAATARPSDPAIGLLPR 331
Cdd:cd04638     1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVkKETGKLVGIVTRKDLLRNPDEEQIALlmsRDPITISPDDTLSEAAEL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1553175819 332 LTDGATHAVVILDDDgKVVGIISQTDLLAT 361
Cdd:cd04638    81 MLEHNIRRVPVVDDD-KLVGIVTVADLVRA 109

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: 40.47 E-value: 1.65e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1553175819 254 DIMSRD--VVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQG 295
Cdd:cd04601    58 EVMTPDerLVTAPEGITLEEAKEILHKHKIEKLPIVDDNGELVG 101

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: 40.51 E-value: 1.96e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1553175819 225 DVSRedidALLREVELQALIRQrgeltcadIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:cd04607    45 DIRR----GLLKGLSLDAPVEE--------VMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDL 110

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: 40.50 E-value: 2.24e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQG----------------------TVGlrELAGKEPGSKLP- 312
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGflseqdclkalleasyhcepggTVA--DYMSTEVLTVSPd 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1553175819 313 ---ISAAATARPSDPAIglLPrltdgathaVVildDDGKVVGIISQTDLLA 360
Cdd:cd04629    79 tsiVDLAQLFLKNKPRR--YP---------VV---EDGKLVGQISRRDVLR 115

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

Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 40.02 E-value: 2.32e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 261 VTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGKEPGS--KLPISAAATARPSDPAIGLLPRLTDGATH 338
Cdd:cd04594     5 IKVSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDIENKSPGKvgKYVVRGSPYVTPTSSLEEAWEIMMRNKSR 84

                          90       100
                  ....*....|....*....|....*
gi 1553175819 339 --AVVildDDGKVVGIISQTDLLAT 361
Cdd:cd04594    85 wvAVV---EKGKFLGIITLDDLLEA 106

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: 40.17 E-value: 2.53e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMS--RDVVTVPGDTTPDHARYLLLKHDIRTLPVLDEN-EKLQGTVGLRELAGKEPGSKLPISAAATARP------SD 323
Cdd:cd04590     3 REVMTprTDVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVLHVKDLLAALLEGREKLDLRALLRPplfvpeTT 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1553175819 324 PAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLL 359
Cdd:cd04590    83 PLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118

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: 341421 [Multi-domain] Cd Length: 136 Bit Score: 40.33 E-value: 3.63e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 220 LNETLDVS-REDIDALLREVELQALIRQRGELTCADIMsRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVG 298
Cdd:cd17785    52 LMELLKYIgYRFGVTIYKGVSFGLLLRISLKEKAKDIM-LSPIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIGDLN 130


                  ....
gi 1553175819 299 LREL 302
Cdd:cd17785   131 SLEL 134

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: 39.15 E-value: 5.46e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1553175819 317 ATARPSDPAIGLLPRLTDGATHAVVILDDDGKVVGIISQTDLLATLAKSLSHNG--LSEIMQGN 378
Cdd:cd02205     5 VTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDtpVAEVMTPD 68

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: 6.73e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 255 IMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDEnEKLQGTVGLREL-----AGKEPGSkLPISAAATARP-----SDP 324
Cdd:cd04587     1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDD-GRLVGIVTDRDLrnrvvAEGLDPD-TPVSEIMTPPPvtidaDAL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1553175819 325 AIGLLPRLTDGATHAVVILDDdGKVVGIISQTDLL 359
Cdd:cd04587    79 VFEALLLMLERNIHHLPVVDD-GRVVGVVTATDLM 112

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: 39.05 E-value: 6.76e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1553175819 241 QALIRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTV 297
Cdd:cd04588    47 KALAEGKENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGII 103

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

Pssm-ID: 341371 [Multi-domain] Cd Length: 108 Bit Score: 38.60 E-value: 8.40e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 270 DHARYlllkhdirtlPVLDENEKLQGTVGLRELAGKEPG-------SKLPIsaaaTARPSDP-----------AIGLLPr 331
Cdd:cd04596    24 GHSRF----------PVVDEENRVVGIVTAKDVIGKEDDtpiekvmTKNPI----TVKPKTSvasaahmmiweGIELLP- 88

                          90       100
                  ....*....|....*....|....*...
gi 1553175819 332 ltdgathaVVilDDDGKVVGIISQTDLL 359
Cdd:cd04596    89 --------VV--DENRKLLGVISRQDVL 106

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). 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: 341386 [Multi-domain] Cd Length: 150 Bit Score: 39.18 E-value: 1.00e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:cd04614    98 KDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDL 147

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

Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 38.07 E-value: 1.19e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1553175819 243 LIRQRGELTCADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQG 295
Cdd:cd04610    46 LLGKDDDEKVSEIMSRDTVVADPDMDITDAARVIFRSGISKLPVVDDEGNLVG 98

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

Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 37.11 E-value: 2.45e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1553175819 254 DIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTV 297
Cdd:cd04583    58 EIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLV 101

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

Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 37.98 E-value: 2.46e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1553175819 255 IMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:cd17779    85 IMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDF 132

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

Pssm-ID: 341398 [Multi-domain] Cd Length: 133 Bit Score: 37.54 E-value: 3.12e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1553175819 254 DIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGKEP 307
Cdd:cd04640     1 DFRRVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKP 54

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 39.43 E-value: 3.61e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1553175819 243 LIRQrgELTCADIM-SRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLRELAGKEP 307
Cdd:PRK14869  241 LINQ--SIPVSYIMtTEDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHLLSPVR 304

CBS pair domains found in archeal proteins, repeat 1; 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: 341413 [Multi-domain] Cd Length: 137 Bit Score: 37.32 E-value: 3.72e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVGLREL 302
Cdd:cd17777    84 ETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDL 133

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

Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 36.73 E-value: 3.80e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1553175819 339 AVVILDDDGKVVGIISQTDLLATLAKSLSHN-GLSEIMQGN 378
Cdd:cd09836    28 SVVVVDDDGKPVGIVTERDIVRAVAEGIDLDtPVEEIMTKN 68

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: 36.78 E-value: 3.98e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRDVVTVPGDTTPDHA--RYLLLKHDIRTLPVLDENEKLQGTVGLREL--AGKEPGSKLPISAAATARPSDPAIGLL 329
Cdd:cd04639     1 DAMVTEFPIVDADLTLREFadDYLIGKKSWREFLVTDEAGRLVGLITVDDLraIPTSQWPDTPVRELMKPLEEIPTVAAD 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1553175819 330 PRLTDGAT-------HAVVILDDDGKVVGIISQTD 357
Cdd:cd04639    81 QSLLEVVKlleeqqlPALAVVSENGTLVGLIEKED 115

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

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 36.63 E-value: 4.19e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1553175819 318 TARPSDP---AIGLLprltdgATH---AVVILDDDGKVVGIISQTDL---LATLAKSLSHNGLSEIM 375
Cdd:cd04623     6 TVSPDATvaeALRLL------AEKnigALVVVDDGGRLVGILSERDYvrkLALRGASSLDTPVSEIM 66

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

Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 36.55 E-value: 4.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 256 MSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLdENEKLQGTVGLRELAGKEPG-------SKLPISAAATARPSDpAIGL 328
Cdd:cd04599     1 MTRNPITISPLDSVARAAALMERQRIGGLPVV-ENGKLVGIITSRDVRRAHPNrlvadamSRNVVTISPEASLWE-AKEL 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1553175819 329 LPRltDGATHAVVIldDDGKVVGIISQTDLLAT 361
Cdd:cd04599    79 MEE--HGIERLVVV--EEGRLVGIITKSTLYLE 107

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

Pssm-ID: 341387 [Multi-domain] Cd Length: 125 Bit Score: 36.31 E-value: 6.93e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 254 DIMSRdVVTVPGDTTPDHARYLLLKHDIRTLPVLDENEKLQGTVG----LRELAGKEPGSKLPISAAAT-------ARPS 322
Cdd:cd04617     1 DIMSV-PVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSrkdlLKATLGGQDLEKTPVSMIMTrmpnivtVTPD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1553175819 323 DPAIGLLPRLTDgatHAV----VILDDDG--KVVGIISQTDLL 359
Cdd:cd04617    80 DSVLEAARKLIE---HEIdslpVVEKEDGklKVVGRITKTNIT 119

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: 35.86 E-value: 9.00e-03

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1553175819 253 ADIMSRDVVTVPGDTTPDHARYLLLKHDIRTLPVLDENE 291
Cdd:cd04587    63 SEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDDGR 101

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: 35.62 E-value: 9.46e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553175819 210 SEDIDSAIARLNETLdvSREDIDALL--------------REVELQALIRQRGELTCADIMSRDVVTVPGDTTPDHARYL 275
Cdd:cd17772     6 SVEPDTTIAEAAELM--TRYNINALPvvdggtgrlvgiitRQVAEKAIYHGLGDLPVSEYMTTEFATVTPDAPLSEIQEI 83

                          90       100
                  ....*....|....*....|..
gi 1553175819 276 LLKHDIRTLPVLdENEKLQGTV 297
Cdd:cd17772    84 IVEQRQRLVPVV-EDGRLVGVI 104