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 489822021  82 DIMTQPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKGALADADTKATPIATIMTRMPNLVTVTKND 160
Cdd:cd04617    1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEgYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489822021 161 TVLHAAEQLVFHQIDSLPVLENT----KVVGKISKTRITALFVD 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 489822021  82 DIMTQPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKGALADADTKATPIATIMTRMPNLVTVTKND 160
Cdd:cd04617    1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEgYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489822021 161 TVLHAAEQLVFHQIDSLPVLENT----KVVGKISKTRITALFVD 200
Cdd:cd04617   81 SVLEAARKLIEHEIDSLPVVEKEdgklKVVGRITKTNITRLFVE 124

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021   74 EIRQLKVAD--IMTQPFFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLLKgaladADTKATPIATIMTRMp 151
Cdd:pfam00478  75 EVRKVKRSEsgMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDLRF-----ETDLSQPVSEVMTKE- 148

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 489822021  152 NLVTVTKNDTVLHAAEQLVFHQIDSLPVL-ENTKVVGKI 189
Cdd:pfam00478 149 NLVTAPEGTTLEEAKEILHKHKIEKLPVVdDNGRLVGLI 187

DNA-binding transcriptional repressor;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489822021   1 MIPIElspRQHQIVAYVRANEPATGDSIAAHLKLTRATIRADLSiltmtgILDARPKVGYFYSGLETNPIHFD 73
Cdd:PRK10434   1 MKPRQ---RQAAILEYLQKQGKTSVEELAQYFDTTGTTIRKDLV------ILEHAGTVIRTYGGVVLNKEESD 64

PafC helix-turn-helix domain; This entry is an N-terminal HTH domain found in the PafC protein. Transcriptional activator PafBC is responsible for upregulating the majority of genes induced by DNA damage.

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 489822021   13 IVAYVRANEPATGDSIAAHLKLTRATIRADLSILTMTGI 51
Cdd:pfam19187   9 LVPYLRQHPGVSVAEAAARFGVTPAQLRADLDVLFVCGL 47

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 489822021  82 DIMTQPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKGALADADTKATPIATIMTRMPNLVTVTKND 160
Cdd:cd04617    1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEgYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489822021 161 TVLHAAEQLVFHQIDSLPVLENT----KVVGKISKTRITALFVD 200
Cdd:cd04617   81 SVLEAARKLIEHEIDSLPVVEKEdgklKVVGRITKTNITRLFVE 124

CBS domain [Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  78 LKVADIMT-QPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKGALAD-ADTKATPIATIMTRmpNLV 154
Cdd:COG0517    1 MKVKDIMTtDVVTVSPDATVREALELMSEKRIGGLPVVDEDgKLVGIVTDRDLRRALAAEgKDLLDTPVSEVMTR--PPV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489822021 155 TVTKNDTVLHAAEQLVFHQIDSLPVLENT-KVVGKISKTRITALFVD 200
Cdd:COG0517   79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDgRLVGIITIKDLLKALLE 125

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 489822021  79 KVADIMTQ-PFFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLLKGALADADTKA----------TPIATIM 147
Cdd:cd04584    1 LVKDIMTKnVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKATSLSiyelnyllskIPVKDIM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489822021 148 TRmpNLVTVTKNDTVLHAAEQLVFHQIDSLPVLENTKVVGKISKTRITALFV 199
Cdd:cd04584   81 TK--DVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAFI 130

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 489822021  93 ETSVYDAIVMLFMEDIGSLYVVDE-DLLVGLVSRKDLL-KGALADADTKATPIATIMTRmpNLVTVTKNDTVLHAAEQLV 170
Cdd:cd04623   10 DATVAEALRLLAEKNIGALVVVDDgGRLVGILSERDYVrKLALRGASSLDTPVSEIMTR--DVVTCTPDDTVEECMALMT 87

                         90       100
                 ....*....|....*....|
gi 489822021 171 FHQIDSLPVLENTKVVGKIS 190
Cdd:cd04623   88 ERRIRHLPVVEDGKLVGIVS 107

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  83 IMTQPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKgALADADTKATPIATIMTRmpNLVTVTKNDT 161
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDgKPVGIVTERDIVR-AVAEGIDLDTPVEEIMTK--NLVTVSPDES 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489822021 162 VLHAAEQLVFHQIDSLPVLEN-TKVVGKISKTRITA 196
Cdd:cd09836   78 IYEAAELMREHNIRHLPVVDGgGKLVGVISIRDLAR 113

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  84 MTQ-PFFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDL-LKGALADADTKATPIATIMTRmpNLVTVTKNDT 161
Cdd:cd04622    1 MTRdVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIvVRAVAEGKDPNTTTVREVMTG--DVVTCSPDDD 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 489822021 162 VLHAAEQLVFHQIDSLPVLENTK-VVGKIS 190
Cdd:cd04622   79 VEEAARLMAEHQVRRLPVVDDDGrLVGIVS 108

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 489822021  85 TQPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKGALADA--DTKATPIATIMTRmpNLVTVTKNDT 161
Cdd:cd04629    3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQgRLVGFLSEQDCLKALLEASyhCEPGGTVADYMST--EVLTVSPDTS 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489822021 162 VLHAAEQLVFHQIDSLPVLENTKVVGKISKTRI 194
Cdd:cd04629   81 IVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDV 113

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  84 MT-QPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLL-----------------------KGALADADT 138
Cdd:cd04586    1 MTtDVVTVTPDTSVREAARLLLEHRISGLPVVDDDgKLVGIVSEGDLLrreepgteprrvwwldallespeRLAEEYVKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489822021 139 KATPIATIMTRmpNLVTVTKNDTVLHAAEQLVFHQIDSLPVLENTKVVGKISKT 192
Cdd:cd04586   81 HGRTVGDVMTR--PVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRA 132

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  95 SVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLlkgaladadTKATP---IATIMTRmpNLVTVTKNDTVLHAAEQLVF 171
Cdd:cd04599   13 SVARAAALMERQRIGGLPVVENGKLVGIITSRDV---------RRAHPnrlVADAMSR--NVVTISPEASLWEAKELMEE 81

                         90       100
                 ....*....|....*....|...
gi 489822021 172 HQIDSLPVLENTKVVGKISKTRI 194
Cdd:cd04599   82 HGIERLVVVEEGRLVGIITKSTL 104

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021   74 EIRQLKVAD--IMTQPFFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLLKgaladADTKATPIATIMTRMp 151
Cdd:pfam00478  75 EVRKVKRSEsgMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDLRF-----ETDLSQPVSEVMTKE- 148

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 489822021  152 NLVTVTKNDTVLHAAEQLVFHQIDSLPVL-ENTKVVGKI 189
Cdd:pfam00478 149 NLVTAPEGTTLEEAKEILHKHKIEKLPVVdDNGRLVGLI 187

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  85 TQPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKGALADADTKATPIATIMTRmpNLVTVTKNDTVL 163
Cdd:cd17784    2 KNVITAKPNEGVVEAFEKMLKHKISALPVVDDEgKLIGIVTATDLGHNLILDKYELGTTVEEVMVK--DVATVHPDETLL 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489822021 164 HAAEQLVFHQ-----IDSLPVLENTKVVGKIS 190
Cdd:cd17784   80 EAIKKMDSNApdeeiINQLPVVDDGKLVGIIS 111

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489822021  74 EIRQLKVADIMTQ-PFFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLLK 130
Cdd:COG2905   61 DPLDTPVSEVMTRpPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLR 118

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  98 DAIVMLFMEDIGSLYVV--DEDLLVGLVSRKDLLKgaladaDTKATPIATIMTRmpNLVTVTKNDTVLHAAEQLVFHQID 175
Cdd:cd04638   16 DVLEILKKKAISGVPVVkkETGKLVGIVTRKDLLR------NPDEEQIALLMSR--DPITISPDDTLSEAAELMLEHNIR 87

                         90       100
                 ....*....|....*....|.
gi 489822021 176 SLPVLENTKVVGKISKTRITA 196
Cdd:cd04638   88 RVPVVDDDKLVGIVTVADLVR 108

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021 113 VVDEDLLVGLVSRKDLlkGALADADTKATPIATIMTRmpNLVTVTKNDTVLHAAEQLVFHQIDSLPVLENTKVVGKISKT 192
Cdd:cd04801   33 VVENGRLVGIVTLEDI--RKVPEVEREATRVRDVMTK--DVITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRT 108

                 ...
gi 489822021 193 RIT 195
Cdd:cd04801  109 DLM 111

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  45 ILTMTGILDArpkvgyFYSGLETnpihfdeirqLKVADIMTQ-PFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGL 122
Cdd:cd04588   39 IVTLTDIAKA------LAEGKEN----------AKVKDIMTKdVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNgKPVGI 102

                 ....*...
gi 489822021 123 VSRKDLLK 130
Cdd:cd04588  103 ITRTDILK 110

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  85 TQPFFAKKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKgaladADTKATPIATIMTRMPNLVTVTKNDTVL 163
Cdd:cd04601    2 TDPVTLSPDATVADVLELKAEYGISGVPVTEDGgKLVGIVTSRDIRF-----ETDLSTPVSEVMTPDERLVTAPEGITLE 76

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489822021 164 HAAEQLVFHQIDSLPVL-ENTKVVGKISKTRI 194
Cdd:cd04601   77 EAKEILHKHKIEKLPIVdDNGELVGLITRKDI 108

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  92 KETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLL----------------KGALADADTKAtPIATIMTRMPnlVT 155
Cdd:cd17777   17 PSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARDLVsylgggclfkivesrhQGDLYSALNRE-VVETIMTPNP--VY 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489822021 156 VTKNDTVLHAAEQLVFHQIDSLPVL-ENTKVVGKIS 190
Cdd:cd17777   94 VYEDSDLIEALTIMVTRGIGSLPVVdRDGRPVGIVT 129

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).

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  73 DEIRQLKVADIMTQ-PFFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLLKG 131
Cdd:cd04801   54 VEREATRVRDVMTKdVITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRTDLMRA 113

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).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489822021  61 FYSGLETNPIHFDEIRQLKVADIMTQP-FFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLLK 130
Cdd:cd04586   66 LLESPERLAEEYVKAHGRTVGDVMTRPvVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; 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 489822021  91 KKETSVYDAIVMLFMEDIGSLYVVDED-LLVGLVSRKDLLKGALA-DADTKATPIATIMTRMPnlVTVTKNDTVLHAAEQ 168
Cdd:cd17781    8 PETTTVAEAAQLMAAKRTDAVLVVDDDgGLSGIFTDKDLARRVVAsGLDPRSTLVSSVMTPNP--LCVTMDTSATDALDL 85

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489822021 169 LVFHQIDSLPVLE-NTKVVGKISktrITALFVDTIK 203
Cdd:cd17781   86 MVEGKFRHLPVVDdDGDVVGVLD---ITKCLYDAIE 118

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 489822021  83 IMTQPFFA-KKETSVYDAIVML-----FMEDIGSLYVVDED-LLVGLVSRKDLLkgaLADADTKatpIATIMTRmpNLVT 155
Cdd:cd04606    6 LMTTEFVAvRPDWTVEEALEYLrrlapDPETIYYIYVVDEDrRLLGVVSLRDLL---LADPDTK---VSDIMDT--DVIS 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489822021 156 VTKNDTVLHAAEQLVFHQIDSLPVL-ENTKVVG 187
Cdd:cd04606   78 VSADDDQEEVARLFAKYDLLALPVVdEEGRLVG 110

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        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489822021  73 DEIRQLKVADIMT-QPFFAKKETSVYDAIVMLFMEDIGSLYVVDEDL-LVGLVSRKDLLK 130
Cdd:cd02205   54 GLALDTPVAEVMTpDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGkLVGIVTRRDILR 113

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 489822021  83 IMTQPFFAKKETSVYDAIVMLFMEDIGSLYVVDEDLLVGLVSRKDLLKGALAD---ADTKATPIATImtrmpNLVTVTKN 159
Cdd:cd04589    1 YLHPPLFVDAETSIREATRLMKENGADSLLVRDGDGRVGIVTRTDLRDAVVLDgqpVDTPVGEIATF-----PLISVEPD 75

                         90       100
                 ....*....|....*....|....*...
gi 489822021 160 DTVLHAAEQLVFHQIDSLPVLENTKVVG 187
Cdd:cd04589   76 DFLFNALLLMTRHRVKRVVVREGEEIVG 103

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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 489822021  78 LKVADIMTQ----PFfAKKETSVYDAIVMLFMEDIGSLYVVDEDL-LVGLVSRKDLLKGALADADTKATPIATIMTRMPn 152
Cdd:cd04604    3 LRVSDLMHTgdelPL-VSPDTSLKEALLEMTRKGLGCTAVVDEDGrLVGIITDGDLRRALEKGLDILNLPAKDVMTRNP- 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489822021 153 lVTVTKNDTVLHAAEQLVFHQIDSLPVL-ENTKVVG 187
Cdd:cd04604   81 -KTISPDALAAEALELMEEHKITVLPVVdEDGKPVG 115

DNA-binding transcriptional repressor;

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489822021   1 MIPIElspRQHQIVAYVRANEPATGDSIAAHLKLTRATIRADLSiltmtgILDARPKVGYFYSGLETNPIHFD 73
Cdd:PRK10434   1 MKPRQ---RQAAILEYLQKQGKTSVEELAQYFDTTGTTIRKDLV------ILEHAGTVIRTYGGVVLNKEESD 64

Predicted transcriptional regulator, ArsR family [Transcription];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489822021   5 ELSPRQHQIVAYVRANEPATGDSIAAHLKLTRATIRADLSILTMTGILDAR 55
Cdd:COG2345   10 LADPTRRRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVERE 60