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 753930916  21 SVPPEVLLLDALKTMARHALGALVVSTR-DRFIGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd04623    6 TVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVEECMAL 85

                         90       100
                 ....*....|....*....|..
gi 753930916 100 MFERCLSHVPVIDEGRLLDVIS 121
Cdd:cd04623   86 MTERRIRHLPVVEDGKLVGIVS 107

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 753930916  21 SVPPEVLLLDALKTMARHALGALVVSTR-DRFIGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd04623    6 TVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVEECMAL 85

                         90       100
                 ....*....|....*....|..
gi 753930916 100 MFERCLSHVPVIDEGRLLDVIS 121
Cdd:cd04623   86 MTERRIRHLPVVEDGKLVGIVS 107

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 753930916   22 VPPEVLLLDALKTMARHALGALVVSTRDRFIGLVTLNDvlqalsLRGAEVLAGSVDEIMNAEAIISRPDDA-IEDVRRLM 100
Cdd:pfam00478  93 LSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRD------LRFETDLSQPVSEVMTKENLVTAPEGTtLEEAKEIL 166

                          90       100
                  ....*....|....*....|....*.
gi 753930916  101 FERCLSHVPVIDE-GRLLDVISRVDV 125
Cdd:pfam00478 167 HKHKIEKLPVVDDnGRLVGLITIKDI 192

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 753930916    21 SVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQAL 64
Cdd:smart00116   4 TVSPDTTLEEALELLRENGIRRLpVVDEEGRLVGIVTRRDIIKAL 48

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 753930916  21 SVPPEVLLLDALKTMARHALGALVVSTR-DRFIGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd04623    6 TVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVEECMAL 85

                         90       100
                 ....*....|....*....|..
gi 753930916 100 MFERCLSHVPVIDEGRLLDVIS 121
Cdd:cd04623   86 MTERRIRHLPVVEDGKLVGIVS 107

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  21 SVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:COG2905   11 TVSPDATVREAARLMTEKGVGSLvVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAEALEL 90

                         90       100
                 ....*....|....*....|....*....
gi 753930916 100 MFERCLSHVPVIDEGRLLDVISRVDVADA 128
Cdd:COG2905   91 MEEHRIRHLPVVDDGKLVGIVSITDLLRA 119

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916   1 MQLRDILRMRNRERGLPRIRSVPPEVLLLDALKTMARHALGALVVSTRDRFIGLVTLNDVLQALsLRGAEVLAGSVDEIM 80
Cdd:COG2524   78 KELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKAL-AEGRDLLDAPVSDIM 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 753930916  81 NAEAIISRPDDAIEDVRRLMFERCLSHVPVID-EGRLLDVISRVDVADA 128
Cdd:COG2524  157 TRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDdDGKLVGIITRTDILRA 205

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 753930916  21 SVPPEVLLLDALKTMARHALGALVVSTRD-RFIGLVTLNDVLQALSLRGAevLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd09836    7 TVPPETTIREAAKLMAENNIGSVVVVDDDgKPVGIVTERDIVRAVAEGID--LDTPVEEIMTKNLVTVSPDESIYEAAEL 84

                         90       100       110
                 ....*....|....*....|....*....|
gi 753930916 100 MFERCLSHVPVID-EGRLLDVISRVDVADA 128
Cdd:cd09836   85 MREHNIRHLPVVDgGGKLVGVISIRDLARE 114

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  19 IRSVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQALSLRGAEVL--------------AGSVDEIMNAE 83
Cdd:cd04600    5 VVTVTPDTSLEEAWRLLRRHRIKALpVVDRARRLVGIVTLADLLKHADLDPPRGLrgrlrrtlglrrdrPETVGDIMTRP 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 753930916  84 AIISRPDDAIEDVRRLMFERCLSHVPVIDE-GRLLDVISRVDV 125
Cdd:cd04600   85 VVTVRPDTPIAELVPLFSDGGLHHIPVVDAdGRLVGIVTQSDL 127

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 753930916  17 PRIRSVPPEVLLLDALKTMARHA-LGALVVStRDRFIGLVTLNDVLqalSLRGAEVLAGSVDEIMNAEAIISRPDDAIED 95
Cdd:cd04801    5 PEVVTVTPEMTVSELLDRMFEEKhLGYPVVE-NGRLVGIVTLEDIR---KVPEVEREATRVRDVMTKDVITVSPDADAME 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 753930916  96 VRRLMFERCLSHVPVIDEGRLLDVISRVDVADA 128
Cdd:cd04801   81 ALKLMSQNNIGRLPVVEDGELVGIISRTDLMRA 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  21 SVPPEVLLLDALKTMARHALGALVVSTRDRFIGLVTLNDVLQAL-----SLRGAEVLAG----SVDEIMNAEAIISRPDD 91
Cdd:cd04584   12 TVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASpskatSLSIYELNYLlskiPVKDIMTKDVITVSPDD 91

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 753930916  92 AIEDVRRLMFERCLSHVPVIDEGRLLDVISRVDVADAA 129
Cdd:cd04584   92 TVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAF 129

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 753930916  21 SVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVL--------------QALSLRGAEVLAG--------SVD 77
Cdd:cd04586    7 TVTPDTSVREAARLLLEHRISGLpVVDDDGKLVGIVSEGDLLrreepgteprrvwwLDALLESPERLAEeyvkahgrTVG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 753930916  78 EIMNAEAIISRPDDAIEDVRRLMFERCLSHVPVIDEGRLLDVISRVDV 125
Cdd:cd04586   87 DVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADL 134

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 753930916  30 DALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQALSLRgaevlAGSVDEIMNAEAIISRPDDAIEDVRRLMFERCLSHV 108
Cdd:cd04605   21 EAAKIMIDKNVTHLpVVSEDGKLIGIVTSWDISKAVALK-----KDSLEEIMTRNVITARPDEPIELAARKMEKHNISAL 95

                         90
                 ....*....|....
gi 753930916 109 PVIDE-GRLLDVIS 121
Cdd:cd04605   96 PVVDDdRRVIGIIT 109

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  21 SVPPEVLLLDALKTMARHALGALVVSTRDRFIGLVTLNDVLQALSLRGaevlagsVDEIMNAEAIISRPDDAIEDVRRLM 100
Cdd:cd04610    7 TVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLGKDDDEK-------VSEIMSRDTVVADPDMDITDAARVI 79

                         90       100
                 ....*....|....*....|....*.
gi 753930916 101 FERCLSHVPVID-EGRLLDVISRVDV 125
Cdd:cd04610   80 FRSGISKLPVVDdEGNLVGIITNMDV 105

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  21 SVPPEVLLLDALKTMARHALGALVVS-TRDRFIGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd17775    7 TASPDTSVLEAARLMRDHHVGSVVVVeEDGKPVGIVTDRDIVVEVVAKGLDPKDVTVGDIMSADLITAREDDGLFEALER 86

                         90       100
                 ....*....|....*....|....*..
gi 753930916 100 MFERCLSHVPVIDE-GRLLDVISRVDV 125
Cdd:cd17775   87 MREKGVRRLPVVDDdGELVGIVTLDDI 113

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 753930916  30 DALKTMARHALGALVVSTRDRF--IGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRLMFERCLSH 107
Cdd:cd04630   20 EALQLMKEHNVKSLIVEKRHEHdaYGIVTYTDILKKVIAEDRDPDLVNVYEIMTKPAISVSPDLDIKYAARLMARFNLKR 99

                         90
                 ....*....|....*...
gi 753930916 108 VPVIDEGRLLDVISRVDV 125
Cdd:cd04630  100 APVIENNELIGIVSMTDL 117

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 753930916  21 SVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQALSLRGAEvLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd17784    6 TAKPNEGVVEAFEKMLKHKISALpVVDDEGKLIGIVTATDLGHNLILDKYE-LGTTVEEVMVKDVATVHPDETLLEAIKK 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 753930916 100 M-----FERCLSHVPVIDEGRLLDVISRVDV 125
Cdd:cd17784   85 MdsnapDEEIINQLPVVDDGKLVGIISDGDI 115

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
                 ....*....|....*....|....*....|....*....|....*....|....
gi 753930916  76 VDEIMNAEAIISRPDDAIEDVRRLMFERCLSHVPVIDEGRLLDVISRVDVADAA 129
Cdd:cd04584    2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRAS 55

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  21 SVPPEVLLLDALKTMARHALGALVVSTRDRF-IGLVTLNDVLQALSLRGAEvLAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd17771    8 TCSPDTPLRAALETMHERRVGSMVVVDANRRpVGIFTLRDLLSRVALPQID-LDAPISEVMTPDPVRLPPSASAFEAALL 86

                         90       100
                 ....*....|....*....|....*.
gi 753930916 100 MFERCLSHVPVIDEGRLLDVISRVDV 125
Cdd:cd17771   87 MAEHGFRHVCVVDNGRLVGVVSERDL 112

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 753930916   22 VPPEVLLLDALKTMARHALGALVVSTRDRFIGLVTLNDvlqalsLRGAEVLAGSVDEIMNAEAIISRPDDA-IEDVRRLM 100
Cdd:pfam00478  93 LSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRD------LRFETDLSQPVSEVMTKENLVTAPEGTtLEEAKEIL 166

                          90       100
                  ....*....|....*....|....*.
gi 753930916  101 FERCLSHVPVIDE-GRLLDVISRVDV 125
Cdd:pfam00478 167 HKHKIEKLPVVDDnGRLVGLITIKDI 192

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916   9 MRNRERGLPRIRSVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQALsLRGAEVLAGSVDEIMNAEAIIS 87
Cdd:cd04608    2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLpVVDEDGRVVGMVTEGNLLSSL-LAGRAQPSDPVSKAMYKQFKQV 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 753930916  88 RPDDAIEDVRRLmFERCLSHVPVIDEGRLLDVISRVDV 125
Cdd:cd04608   81 DLDTPLGALSRI-LERDHFALVVDGQGKVLGIVTRIDL 117

Fusion of CP12 with N-terminal CBS domain pair [Energy production and conversion, Signal transduction mechanisms];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  30 DALKTMARHALGALVVSTR---DRFiGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRLMFERCLS 106
Cdd:COG5792   22 EAVKLMKEKGLRALIVERRheqDAY-GIVTETDIVYKVTAYGKDPKKVRVYEIMTKPCIVVNPDLGVEYVARLFANTGIR 100

                         90
                 ....*....|....*....
gi 753930916 107 HVPVIdEGRLLDVISRVDV 125
Cdd:COG5792  101 RAPVI-QGKLLGIISVSDI 118

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  21 SVPPEVLLLDALKTM-ARHALGALVVSTRDRFIGLVTLNDVLQALSLrgaevlAGSVDEIMNAEAIISRPDDAIEDVRRL 99
Cdd:cd04583    6 TITPERTLAQAIEIMrEKRVDSLLVVDKDNVLLGIVDIEDINRNYRK------AKKVGEIMERDVFTVKEDSLLRDTVDR 79

                         90       100
                 ....*....|....*....|....*....
gi 753930916 100 MFERCLSHVPVID-EGRLLDVISRVDVAD 127
Cdd:cd04583   80 ILKRGLKYVPVVDeQGRLVGLVTRASLVD 108

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916  44 VVSTRDRFIGLVTLNDVLQALSLRGAEVLAgSVDEIMNAEAIISRPDDAIEDVRRLMFERCLSHVPVIDE---GRLLDVI 120
Cdd:cd04613   31 VVDEQGRLTGILSIQDVRGVLFEEELWDLV-VVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDDddpGKVLGML 109

                         90
                 ....*....|.
gi 753930916 121 SRVDVAdAAYA 131
Cdd:cd04613  110 SRRDVI-AAYN 119

CBS domain [Signal transduction mechanisms];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 753930916  76 VDEIMNAEAIISRPDDAIEDVRRLMFERCLSHVPVIDE-GRLLDVISRVDVADAAYAE 132
Cdd:COG0517    3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEdGKLVGIVTDRDLRRALAAE 60

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 753930916  22 VPPEVLLLDALKTMAR-HALGALVVSTRDRFIGLVTLNDVLQALSLRGAEVLAGSVDEIMNAEAIISRPDDAIEDVRRLM 100
Cdd:cd17781    7 VPETTTVAEAAQLMAAkRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSATDALDLM 86

                         90
                 ....*....|....
gi 753930916 101 FERCLSHVPVIDEG 114
Cdd:cd17781   87 VEGKFRHLPVVDDD 100

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

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 753930916  17 PRIRSVPPEVLLLDALKTMARHALGALVVSTRDRFIGLVTLNDVLQALS 65
Cdd:COG2905   73 RPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALS 121

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 753930916  18 RIRSVPPEVLLLDALKTMARHALGALVVSTRDRFIGLVTLNDVLQALSLRGA----------EVLAGSVDEIMNAEAIIS 87
Cdd:cd17778    9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYFGSHEAkkrlttgdidEAYSTPVEEIMSKEVVTI 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 753930916  88 RPDDAIEDVRRLMFERCLSHVPVID-EGRLLDVISRVDV 125
Cdd:cd17778   89 EPDADIAEAARLMIKKNVGSLLVVDdEGELKGIITERDV 127

putative manganese-dependent inorganic diphosphatase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753930916   2 QLRDILrmrnrergLPRIRSVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQAL-------SLRGAEVLA 73
Cdd:PRK14869  69 QVRDLE--------IDKPVTVSPDTSLKEAWNLMDENNVKTLpVVDEEGKLLGLVSLSDLARAYmdildpeILSKSPTSL 140

                         90       100
                 ....*....|....*....|..
gi 753930916  74 GSVDEIMNAEAIISRPDDAIED 95
Cdd:PRK14869 141 ENIIRTLDGEVLVGAEEDKVEE 162

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 753930916  30 DALKTMARHALGALVVSTRDRFIGLVTLNDVLQALSLRgaevlagSVDEIMNAEAIISRPDDAIEDVRRLMFERCLSHVP 109
Cdd:cd04599   16 RAAALMERQRIGGLPVVENGKLVGIITSRDVRRAHPNR-------LVADAMSRNVVTISPEASLWEAKELMEEHGIERLV 88

                         90
                 ....*....|....*.
gi 753930916 110 VIDEGRLLDVISRVDV 125
Cdd:cd04599   89 VVEEGRLVGIITKSTL 104

CBS domain [Signal transduction mechanisms];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 753930916   4 RDILRMRNRERGLPR-----------IRSVPPEVLLLDALKTMARHALGAL-VVSTRDRFIGLVTLNDVLQAL 64
Cdd:COG0517   51 RDLRRALAAEGKDLLdtpvsevmtrpPVTVSPDTSLEEAAELMEEHKIRRLpVVDDDGRLVGIITIKDLLKAL 123