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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  79 EIMSPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASL-NTNIDGTPVAVCMTRVPHVKTCTPEF 157
Cdd:cd04617    1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLgGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488295193 158 TILEAADTLQKYEVDSLPVVEKEN-PKKVIGKITKTKILTYITQ 200
Cdd:cd04617   81 SVLEAARKLIEHEIDSLPVVEKEDgKLKVVGRITKTNITRLFVE 124

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  79 EIMSPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASL-NTNIDGTPVAVCMTRVPHVKTCTPEF 157
Cdd:cd04617    1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLgGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488295193 158 TILEAADTLQKYEVDSLPVVEKEN-PKKVIGKITKTKILTYITQ 200
Cdd:cd04617   81 SVLEAARKLIEHEIDSLPVVEKEDgKLKVVGRITKTNITRLFVE 124

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488295193   77 VQEIMS-PPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASLN 132
Cdd:pfam00571   1 VKDIMTkDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488295193   1 MKLSKRQEQIIAVVKEHQPVSGERISDILAVSRATLRSDLSFLTLSGILK-----ASPKVGYTYESD 62
Cdd:COG1349    1 MLAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRrvhggAVLVSSAAAEPP 67

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 488295193    83 PPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRA 129
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47

Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer. [Transport and binding proteins, Cations and iron carrying compounds]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  104 DVGSLYVMDEAKELLGVLSRKDLLRASLNTNIDgtpvAVCMTRVPHVKTCTPEftiLEAADTLQKYEVDSLPVVEKENpk 183
Cdd:TIGR00400 166 DIYTLYVTNESKHLKGVLSIRDLILAKPEEILS----SIMRSSVFSIVGVNDQ---EEVARLIQKYDFLAVPVVDNEG-- 236

                          90       100
                  ....*....|....*....|....
gi 488295193  184 KVIGKITKTKILTYITQQAKEAAQ 207
Cdd:TIGR00400 237 RLVGIVTVDDIIDVIQSEATEDFY 260

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  79 EIMSPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASL-NTNIDGTPVAVCMTRVPHVKTCTPEF 157
Cdd:cd04617    1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLgGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488295193 158 TILEAADTLQKYEVDSLPVVEKEN-PKKVIGKITKTKILTYITQ 200
Cdd:cd04617   81 SVLEAARKLIEHEIDSLPVVEKEDgKLKVVGRITKTNITRLFVE 124

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  77 VQEIMS-PPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASL--NTNIDGTPVAVCMTRvpHVKTC 153
Cdd:COG2905    1 VKDIMSrDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLaeGLDPLDTPVSEVMTR--PPITV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488295193 154 TPEFTILEAADTLQKYEVDSLPVVEKEnpkKVIGKITKTKILTYITQQ 201
Cdd:COG2905   79 SPDDSLAEALELMEEHRIRHLPVVDDG---KLVGIVSITDLLRALSEE 123

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  72 VFQTKVQEIMS-PPLMVAQETSIRDAITNLFMYDVGSLYVMDEaKELLGVLSRKDLLRASL-NTNIDGTPVAVCMTRvpH 149
Cdd:COG2524   83 VLKMKVKDIMTkDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAeGRDLLDAPVSDIMTR--D 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488295193 150 VKTCTPEFTILEAADTLQKYEVDSLPVVEKENpkKVIGKITKTKILTYI 198
Cdd:COG2524  160 VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDG--KLVGIITRTDILRAL 206

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  76 KVQEIMSPPLM-VAQETSIRDAItNLFM-YDVGSLYVMDEAKeLLGVLSRKDLLRAS-----------LNTNIDGTPVAV 142
Cdd:cd04584    1 LVKDIMTKNVVtVTPDTSLAEAR-ELMKeHKIRHLPVVDDGK-LVGIVTDRDLLRASpskatslsiyeLNYLLSKIPVKD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488295193 143 CMTRvpHVKTCTPEFTILEAADTLQKYEVDSLPVVEKEnpkKVIGKITKTKIL 195
Cdd:cd04584   79 IMTK--DVITVSPDDTVEEAALLMLENKIGCLPVVDGG---KLVGIITETDIL 126

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  81 MSP-PLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASLNT---NIDGTPVAVCMTRvpHVKTCTPE 156
Cdd:cd04629    1 MTRnPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEAsyhCEPGGTVADYMST--EVLTVSPD 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488295193 157 FTILEAADTLQKYEVDSLPVVEKenpKKVIGKITKTKIL 195
Cdd:cd04629   79 TSIVDLAQLFLKNKPRRYPVVED---GKLVGQISRRDVL 114

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  87 VAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLR--ASLNTNIDGTPVAVCMTRvpHVKTCTPEFTILEAAD 164
Cdd:cd04623    7 VSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRklALRGASSLDTPVSEIMTR--DVVTCTPDDTVEECMA 84

                         90       100
                 ....*....|....*....|...
gi 488295193 165 TLQKYEVDSLPVVEKEnpkKVIG 187
Cdd:cd04623   85 LMTERRIRHLPVVEDG---KLVG 104

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  82 SPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKeLLGVLSRKDLLRAsLNTNIDGTPVAVCMTRvpHVKTCTPEFTILE 161
Cdd:cd04595    2 SPVKTVSPDTTIEEARKIMLRYGHTGLPVVEDGK-LVGIISRRDVDKA-KHHGLGHAPVKGYMST--NVITIDPDTSLEE 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488295193 162 AADTLQKYEVDSLPVVEKEnpkKVIGKITKTKILTY 197
Cdd:cd04595   78 AQELMVEHDIGRLPVVEEG---KLVGIVTRSDVLRY 110

CBS domain [Signal transduction mechanisms];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  71 DVFQTKVQEIMS-PPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRA 129
Cdd:COG0517   63 DLLDTPVSEVMTrPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKA 122

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193 108 LYVMDEAKELLGVLSRKDLLRASLNTNIDgtpvAVCMTRVPHVKTCTP-EftilEAADTLQKYEVDSLPVVEKENpkKVI 186
Cdd:cd04606   40 IYVVDEDRRLLGVVSLRDLLLADPDTKVS----DIMDTDVISVSADDDqE----EVARLFAKYDLLALPVVDEEG--RLV 109

                 ....
gi 488295193 187 GKIT 190
Cdd:cd04606  110 GIIT 113

voltage-gated chloride channel ClcB;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  75 TKVQEIMSPPLMVAQETSIRDAITNLFM-YDVGSLYVMDEAKELLGVLSRKDLLRASLNTNiDGTPVAVCMTRVPHVKTC 153
Cdd:PRK01862 447 TQMRELIQPAQTVVPPTASVADMTRVFLeYPVKYLYVVDDDGRFRGAVALKDITSDLLDKR-DTTDKTAADYAHTPFPLL 525

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488295193 154 TPEFTILEAADTLQKYEVDSLPVVEKENPKKVIGKITKTKIL 195
Cdd:PRK01862 526 TPDMPLGDALEHFMAFQGERLPVVESEASPTLAGVVYKTSLL 567

Predicted transcriptional regulator containing CBS domains [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  76 KVQEIM--SPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASlntniDGTPVAVCMTRVPHvkTC 153
Cdd:COG4109   17 LVEDIMtlEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKD-----DDTPIEDVMTKNPI--TV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488295193 154 TPEFTILEAADTLQKYEVDSLPVVEKENpkKVIGKITKTKIL 195
Cdd:COG4109   90 TPDTSLASAAHKMIWEGIELLPVVDDDG--RLLGIISRQDVL 129

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  81 MSPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASLNTNID--GTPVAVCMTrvPHVKTCTPEFT 158
Cdd:cd17782    1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVLRVLAAGLDpaTTSVVRVMT--PNPETAPPSTT 78

                         90       100
                 ....*....|....*....|....*....
gi 488295193 159 ILEAADTLQKYEVDSLPVVEKENpkKVIG 187
Cdd:cd17782   79 ILDALHKMHEGKFLNLPVVDDEG--EIVG 105

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  80 IMSPPLMVAQETSIRDAITnlFMYD--VGSLYVMDEaKELLGVLSRKDL----LRASLNTNidgTPVAVCMTRVPHvkTC 153
Cdd:cd04587    2 MSRPPVTVPPDATIQEAAQ--LMSEerVSSLLVVDD-GRLVGIVTDRDLrnrvVAEGLDPD---TPVSEIMTPPPV--TI 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488295193 154 TPEFTILEAADTLQKYEVDSLPVVEKEnpkKVIGKITKTKILTY 197
Cdd:cd04587   74 DADALVFEALLLMLERNIHHLPVVDDG---RVVGVVTATDLMRL 114

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  43 LTLSGILKASPKVGYTYESDNMEAFfffdVFQTKVQEIMS-PPLMVAQETSIRDAItnLFMYD--VGSLYVMDEAKeLLG 119
Cdd:cd04584   46 VTDRDLLRASPSKATSLSIYELNYL----LSKIPVKDIMTkDVITVSPDDTVEEAA--LLMLEnkIGCLPVVDGGK-LVG 118

                         90
                 ....*....|
gi 488295193 120 VLSRKDLLRA 129
Cdd:cd04584  119 IITETDILRA 128

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488295193    8 EQIIAVVKEHQ-PVSGERISDILAVSRATLRSDLSFLTLSGI-LKASPKVGY 57
Cdd:pfam08279   1 LQILQLLLEARgPISGQELAEKLGVSRRTIRRDIKILEELGVpIEAEPGRGY 52

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  82 SPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKE-LLGVLSRKDLLRAsLNTNIDGTPVAVCMTRvpHVKTCTPEFTIL 160
Cdd:cd17772    2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGrLVGIITRQVAEKA-IYHGLGDLPVSEYMTT--EFATVTPDAPLS 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488295193 161 EAADTL----QKYevdsLPVVEKEnpkKVIGKITKTKILTY 197
Cdd:cd17772   79 EIQEIIveqrQRL----VPVVEDG---RLVGVITRTDLLNL 112

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  80 IMSPPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRASLNTNID-GTPVAVCMTRVPHvkTCTPEFT 158
Cdd:cd17771    2 IRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDlDAPISEVMTPDPV--RLPPSAS 79

                         90       100
                 ....*....|....*....|....*....
gi 488295193 159 ILEAADTLQKYEVDSLPVVEKENPKKVIG 187
Cdd:cd17771   80 AFEAALLMAEHGFRHVCVVDNGRLVGVVS 108

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  84 PLMVAQETSIRDAIT--------------NLFMYDVGSLY--VMDEAKeLLGVLSRKDLLR-ASLNTNIDGTPVAVCMTR 146
Cdd:cd04620    9 PLTVSPDTPVIEAIAlmsqtrssccllseDSIITEARSSCvlVVENQQ-LVGIFTERDVVRlTASGIDLSGVTIAEVMTQ 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488295193 147 VphVKTCT-PEFT-ILEAADTLQKYEVDSLPVVEKENpkKVIGKITKTKIL 195
Cdd:cd04620   88 P--VITLKeSEFQdIFTVLSLLRQHQIRHLPIVDDQG--QLVGLITPESLR 134

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488295193  144 MTRvpHVKTCTPEFTILEAADTLQKYEVDSLPVVEKENpkKVIGKITKTKILTYI 198
Cdd:pfam00571   5 MTK--DVVTVSPDTTLEEALELMREHGISRLPVVDEDG--KLVGIVTLKDLLRAL 55

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).

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488295193  75 TKVQEIMSPPLM-VAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLR 128
Cdd:cd02205   59 TPVAEVMTPDVItVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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).

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488295193  77 VQEIMSPPLM-VAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRA 129
Cdd:cd04632   74 VYDIMSSPVVtVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127

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.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 488295193    83 PPLMVAQETSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRA 129
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47

helix_turn_helix, Deoxyribose operon repressor;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 488295193     6 RQEQIIAVVKEHQPVSGERISDILAVSRATLRSDLSFLTLSGILK 50
Cdd:smart00420   1 RQQQILELLAQQGKVSVEELAELLGVSEMTIRRDLNKLEEQGLLT 45

DeoR-like helix-turn-helix domain;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 488295193    6 RQEQIIAVVKEHQPVSGERISDILAVSRATLRSDLSFLTLSGILK 50
Cdd:pfam08220   1 RIQQILELLKQQGTLSVEELAELLGVSEMTIRRDLNELEEQGLLT 45

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.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488295193  71 DVFQTKVQEIMSPPLMVAQE-TSIRDAITNLFMYDVGSLYVMDEAKELLGVLSRKDLLRA 129
Cdd:cd17778   71 EAYSTPVEEIMSKEVVTIEPdADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIA 130