CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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 1958770488 188 TYHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 267
Cdd:cd04641     1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                          90
                  ....*....|....*....
gi 1958770488 268 SKLETLETIVDRIVRAEVR 286
Cdd:cd04641    81 TLNDTLETIIDRIVKAEVH 99

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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 1958770488 188 TYHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 267
Cdd:cd04641     1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                          90
                  ....*....|....*....
gi 1958770488 268 SKLETLETIVDRIVRAEVR 286
Cdd:cd04641    81 TLNDTLETIIDRIVKAEVH 99

CBS domain [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 191 NIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHrsqyfeGVVKCSKL 270
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90
                  ....*....|....*.
gi 1958770488 271 ETLETIVDRIVRAEVR 286
Cdd:COG0517    84 TSLEEAAELMEEHKIR 99

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 1958770488 190 HNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 240
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

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 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 164
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRAL 55

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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 1958770488 188 TYHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 267
Cdd:cd04641     1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                          90
                  ....*....|....*....
gi 1958770488 268 SKLETLETIVDRIVRAEVR 286
Cdd:cd04641    81 TLNDTLETIIDRIVKAEVH 99

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 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpisGNALY-ILTHKRILKFLqlfMSDMPKPAFMKQNLDELGIgTYHNI- 192
Cdd:cd04584     8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVD---DGKLVgIVTDRDLLRAS---PSKATSLSIYELNYLLSKI-PVKDIm 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958770488 193 ----AFIHPNTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLA 238
Cdd:cd04584    81 tkdvITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPA--FMKQNLdelgigtyhni 192
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDLLDAPVsdIMTRDV----------- 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958770488 193 AFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 236
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488  33 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETwrelylqe 112
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK-LVGIVTERDILRALVEGGLALDTPVAEVMTPDVIT-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958770488 113 tfkplvnISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILK 162
Cdd:cd02205    72 -------VSPDTDLEEALELMLEHGIRRLPVVDD-DGKLVGIVTRRDILR 113

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 190 HNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQALQhrsqyfEGVVKCSK 269
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG-GLALDTPVAEVMT------PDVITVSP 74

                          90
                  ....*....|....*..
gi 1958770488 270 LETLETIVDRIVRAEVR 286
Cdd:cd02205    75 DTDLEEALELMLEHGIR 91

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFL-----QLFMSDMPKPAFMKQNLDELGIGTY 189
Cdd:cd17779     8 KDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskYNLVEKKHNGNLLAAINEPVREIMT 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958770488 190 HNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 235
Cdd:cd17779    88 RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133

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 1958770488 190 HNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLD-ITVtqalqhrSQYFEGVVKCS 268
Cdd:cd04629     3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPgGTV-------ADYMSTEVLTV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958770488 269 KLETleTIVDrivRAEVRDRSPPHIFPrvcwahtqqVV--GRLLG 311
Cdd:cd04629    76 SPDT--SIVD---LAQLFLKNKPRRYP---------VVedGKLVG 106

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488  33 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKqsFVGMLTITDFINILHRYYKSPMVQIYELEEhkietwrelylqe 112
Cdd:COG2524    93 TKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDAPVSDIMT------------- 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958770488 113 tfKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 164
Cdd:COG2524   158 --RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDD-DGKLVGIITRTDILRAL 206

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
                  ....*....|....*....|....*....|....*....|.
gi 1958770488 195 IHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 235
Cdd:cd04586     8 VTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLL 48

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 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLFMS-DMPKPAFMKQNLdelgIGTYhnia 193
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVAEGIDlDTPVEEIMTKNL----VTVS---- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958770488 194 fihPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 236
Cdd:cd09836    74 ---PDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 118 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFL---QLFMS----------DMPKPAFMKQNldel 184
Cdd:cd04631    11 ITATPGTPIEDVAKIMVRNGFRRLPVVS--DGKLVGIVTSTDIMRYLgsgEAFEKlktgnihevlNVPISSIMKRD---- 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958770488 185 gigtyhnIAFIHPNTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 236
Cdd:cd04631    85 -------IITTTPDTDLGEAAELMLEKNIGALPVVDD-GKLVGIITERDILR 128

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 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNAL-------------YILTHKRILKFLQLFMSDMPKPAfmKQNL 181
Cdd:cd04586     3 TDVVTVTPDTSVREAARLLLEHRISGLPVVD--DDGKLvgivsegdllrreEPGTEPRRVWWLDALLESPERLA--EEYV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958770488 182 DELG-----IGTyHNIAFIHPNTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVI 235
Cdd:cd04586    79 KAHGrtvgdVMT-RPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLL 135

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 1958770488 117 LVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLqlfmsdmpkpafmkqnLDelgiGTYHN----- 191
Cdd:cd04629     5 PVTLTPDTSILEAVELLLEHKISGAPVVDE-QGRLVGFLSEQDCLKAL----------------LE----ASYHCepggt 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958770488 192 --------IAFIHPNTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 236
Cdd:cd04629    64 vadymsteVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDVLR 115

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958770488 190 HNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITV 250
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPV 67

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        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFL--QLFMSDMPKP---AFMKQNLDELgigTY 189
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFgsHEAKKRLTTGdidEAYSTPVEEI---MS 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958770488 190 HNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 235
Cdd:cd17778    83 KEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 115 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLqlfmsdmpkpAFMKQNLDElgIGTyHNIAF 194
Cdd:cd04605     8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSE-DGKLIGIVTSWDISKAV----------ALKKDSLEE--IMT-RNVIT 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958770488 195 IHPNTPIIKALNIFVERRISALPVVDESGKVVDIYS 230
Cdd:cd04605    74 ARPDEPIELAARKMEKHNISALPVVDDDRRVIGIIT 109

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 1958770488 116 PLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPAFMKQNldelgigtyhnIAFI 195
Cdd:cd04595     3 PVKTVSPDTTIEEARKIMLRYGHTGLPVVE--DGKLVGIISRRDVDKAKHHGLGHAPVKGYMSTN-----------VITI 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958770488 196 HPNTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 236
Cdd:cd04595    70 DPDTSLEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVLR 109

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958770488 120 ISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLFMS-DMPKPAFMKQNLDElgigtyhniafihpn 198
Cdd:cd04597    10 LSPETSIKDAWNLMDENNLKTLPVTDD-NGKLIGLLSISDIARTVDYIMTkDNLIVFKEDDYLDE--------------- 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958770488 199 tpiIKalNIFVERRISALPVVDESGKVVDIYSKFDVIN 236
Cdd:cd04597    74 ---VK--EIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106

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 1958770488   36 LVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILH 84
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGR-LVGIVTRRDIIKALA 49

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 1958770488 118 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILThKRILKFLqlfmSDMPKP--AFMkqnldelgigTYHNIAFI 195
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVD--DGKLVGIVT-NRDLRFE----TDLSQPvsEVM----------TKENLVTA 153

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958770488 196 HPNTPIIKALNIFVERRISALPVVDESGKVV 226
Cdd:pfam00478 154 PEGTTLEEAKEILHKHKIEKLPVVDDNGRLV 184

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
                  ....*....|....*....|....*....|..
gi 1958770488 195 IHPNTPIIKALNIFVERRISALPVVDESGKVV 226
Cdd:cd04604    83 ISPDALAAEALELMEEHKITVLPVVDEDGKPV 114

Predicted transcriptional regulator containing CBS domains [Transcription];

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958770488 188 TYHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 236
Cdd:COG4109    23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG 71

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 1958770488 118 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILThKRILKFLQlfMSDMPKPAFMKQNLDelgigtyhnIAFIH 196
Cdd:cd04601     5 VTLSPDATVADVLELKAEYGISGVPVTE--DGGKLVgIVT-SRDIRFET--DLSTPVSEVMTPDER---------LVTAP 70

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958770488 197 PNTPIIKALNIFVERRISALPVVDESGKVVDI 228
Cdd:cd04601    71 EGITLEEAKEILHKHKIEKLPIVDDNGELVGL 102

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
                  ....*....|....*....|....*....|....*....|....
gi 1958770488 118 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRIL 161
Cdd:cd04599    64 VTISPEASLWEAKELMEEHGIERLVVVE--EGRLVGIITKSTLY 105

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958770488 189 YHNIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDV 234
Cdd:cd04597     4 YDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDI 49

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958770488 191 NIAFIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLD 247
Cdd:cd04605     9 DVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALK-KDSLE 64

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
                  ....*....|....*....|....*....|....*....|.
gi 1958770488 194 FIHPNTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDV 234
Cdd:cd04601     6 TLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDI 46

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 1958770488 118 VNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFlqlfmsdmpkpAFMKQNLDELGIGT----YHNIA 193
Cdd:cd04617     7 VVVDETTSVYDAIVTLFLEDVGSLFVVDE-EGYLVGVVSRKDLLKA-----------TLGGQDLEKTPVSMimtrMPNIV 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958770488 194 FIHPNTPIIKALNIFVERRISALPVVDESG---KVVDIYSKFDVINLAAE 240
Cdd:cd04617    75 TVTPDDSVLEAARKLIEHEIDSLPVVEKEDgklKVVGRITKTNITRLFVE 124