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 494509427   7 MSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLR--------ARFRELGGADSQPDEM------- 71
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRreepgtepRRVWWLDALLESPERLaeeyvka 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494509427  72 ---TAGDVMASPVVAMTADAEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLIAV 125
Cdd:cd04586   81 hgrTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLRA 137

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 494509427    10 PVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRAR 57
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   3 ARHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRARFRElgGADsqPDEMTAGDVMASPVV 82
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAE--GLD--PLDTPVSEVMTRPPI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494509427  83 AMTADAEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLIAVLTTD 129
Cdd:COG2905   77 TVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEE 123

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 494509427   8 SSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRARFRElggadSQPDEMTAGDVMASPVVAMTAD 87
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG-----GLALDTPVAEVMTPDVITVSPD 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494509427  88 AEVSELASAMLRSRLRGIPIVHDHD-ILGIVTRPDLIA 124
Cdd:cd02205   76 TDLEEALELMLEHGIRRLPVVDDDGkLVGIVTRRDILR 113

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   1 MQARHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKhLVGIVSEGDLLRARFRELGgadsqPDEMTAGDVMASP 80
Cdd:COG2524   86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK-LVGIITERDLLKALAEGRD-----LLDAPVSDIMTRD 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494509427  81 VVAMTADAEVSELASAMLRSRLRGIPIVHDHD-ILGIVTRPDLIAVL 126
Cdd:COG2524  160 VVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGkLVGIITRTDILRAL 206

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   7 MSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKhLVGIVSEGDLLRARFRELGGADSQP-----DEMTAGDVMASPV 81
Cdd:cd04584    6 MTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGK-LVGIVTDRDLLRASPSKATSLSIYElnyllSKIPVKDIMTKDV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494509427  82 VAMTADAEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLIAVLT 127
Cdd:cd04584   85 ITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAFI 130

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 494509427   7 MSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRA-----RFRELGGadsqpdemTAGDVMASPV 81
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKAlleasYHCEPGG--------TVADYMSTEV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494509427  82 VAMTADAEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLIAV 125
Cdd:cd04629   73 LTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVLRA 116

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   8 SSPVTTVDRSTSVDECLQL-----VGSsgftvLPVVDERKHLVGIVSEGDLLRArfreLGGADSQPDEMTAGDVMASPVV 82
Cdd:cd04623    1 GRDVVTVSPDATVAEALRLlaeknIGA-----LVVVDDGGRLVGILSERDYVRK----LALRGASSLDTPVSEIMTRDVV 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 494509427  83 AMTADAEVSELASAMLRSRLRGIPIVHDHDILGIV 117
Cdd:cd04623   72 TCTPDDTVEECMALMTERRIRHLPVVEDGKLVGIV 106

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 494509427   7 MSSPVTTVDRSTSVDECLQL-----VGSsgftvLPVVDERKHLVGIVSEGDLLRarfrELGGADSQPDEMTAGDVMASPV 81
Cdd:cd17775    1 CRREVVTASPDTSVLEAARLmrdhhVGS-----VVVVEEDGKPVGIVTDRDIVV----EVVAKGLDPKDVTVGDIMSADL 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494509427  82 VAMTADAEVSELASAMLRSRLRGIPIVHDHDIL-GIVTRPDLIAVL 126
Cdd:cd17775   72 ITAREDDGLFEALERMREKGVRRLPVVDDDGELvGIVTLDDILELL 117

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   8 SSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKhLVGIVSEGDLLRARFRELGGADSQpdemtagDVMASPVVAMTAD 87
Cdd:cd04595    1 SSPVKTVSPDTTIEEARKIMLRYGHTGLPVVEDGK-LVGIISRRDVDKAKHHGLGHAPVK-------GYMSTNVITIDPD 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 494509427  88 AEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLI 123
Cdd:cd04595   73 TSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVL 108

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   6 VMSSPVTTVDRSTSVDECLQLVGSSG-----FTVLPVVDERKHLVGIVSEGDLLRArfrelggadsqPDEMTAGDVMASP 80
Cdd:COG2239  134 LMTTEFVAVREDWTVGEALRYLRRQAedpetIYYIYVVDDDGRLVGVVSLRDLLLA-----------DPDTKVSDIMDTD 202

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494509427  81 VVAMTADAEVSELASAMLRSRLRGIPIVHDHD-ILGIVTRPDLIAVL---TTDDAQ 132
Cdd:COG2239  203 VISVPADDDQEEVARLFERYDLLALPVVDEEGrLVGIITVDDVVDVIeeeATEDIL 258

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   6 VMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKhLVGIVSEGDLlraRFRELggADSQPDEMTAGDVMASPVVAMT 85
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGR-LVGIVTDRDL---RNRVV--AEGLDPDTPVSEIMTPPPVTID 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494509427  86 ADAEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLI 123
Cdd:cd04587   75 ADALVFEALLLMLERNIHHLPVVDDGRVVGVVTATDLM 112

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 494509427    3 ARHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRA 56
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54

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 494509427   3 ARHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKH-LVGIVSEGDLLRARFRElggaDSQPDEMTAGDVMASPV 81
Cdd:cd04630    1 VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVEKRHEHdAYGIVTYTDILKKVIAE----DRDPDLVNVYEIMTKPA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 494509427  82 VAMTADAEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLIA 124
Cdd:cd04630   77 ISVSPDLDIKYAARLMARFNLKRAPVIENNELIGIVSMTDLVL 119

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 494509427   1 MQARHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKhLVGIVSEGDLLRARFREL 61
Cdd:COG2905   65 TPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGK-LVGIVSITDLLRALSEEL 124

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494509427   1 MQARHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDL 53
Cdd:cd04622   60 TTVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427  11 VTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLL--------RARFRELGGADSQPDEMTAGDVMASPVV 82
Cdd:cd04632    4 VITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVdfvvrpgtKTRGGDRGGEKERMLDLPVYDIMSSPVV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 494509427  83 AMTADAEVSELASAMLRSRLRGIPIVHDHDIL-GIVTRPDL 122
Cdd:cd04632   84 TVTRDATVADAVERMLENDISGLVVTPDDNMViGILTKTDV 124

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   6 VMSSPVTTVDRSTSVDECLQLVGSSG-----FTVLPVVDERKHLVGIVSEGDLLRArfrelggadsqPDEMTAGDVMASP 80
Cdd:cd04606    6 LMTTEFVAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLA-----------DPDTKVSDIMDTD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494509427  81 VVAMTADAEVSELASAMLRSRLRGIPIVHDHD-ILGIVTRPDLIAVL 126
Cdd:cd04606   75 VISVSADDDQEEVARLFAKYDLLALPVVDEEGrLVGIITVDDVLDVI 121

Predicted transcriptional regulator containing CBS domains [Transcription];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 494509427   6 VMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRA 56
Cdd:COG4109   81 VMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKA 131

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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 494509427  17 STSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLR---------------------ARFRELGGADSQPDEMTAGD 75
Cdd:cd17789   11 NTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLAldsisgrsqtdnnfppadstwKTFNEVQKLLSKTNGKVVGD 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494509427  76 VMASPVVAMTADAEVSELASAMLRSRLRGIPIV-HDHDILGIVTRPDLI 123
Cdd:cd17789   91 VMTPSPLVVREKTNLEDAARILLETKFRRLPVVdSDGKLVGIITRGNVV 139

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 494509427   6 VMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRArfreLGGADSQPDEMtagdvMASPVVAMT 85
Cdd:cd04605    5 IMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKA----VALKKDSLEEI-----MTRNVITAR 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494509427  86 ADAEVSELASAMLRSRLRGIPIV-HDHDILGIVTRPDL 122
Cdd:cd04605   76 PDEPIELAARKMEKHNISALPVVdDDRRVIGIITSDDI 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
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494509427   2 QARHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLR 55
Cdd:cd02205   60 PVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Thermoplasmatales; 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 494509427  13 TVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRaRFRElggADSQPDEMTAGDVMASPVVAMTADAEVSE 92
Cdd:cd17786    6 TINWNATVFDAVKIMNENHLYGLVVKDDDGNYVGLISERSIIK-RFIP---RNVKPDEVPVKLVMRKPIPKVKSDYDVKD 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 494509427  93 LASAMLRSRLRGIPIVHDHD-ILGIVTRPDL 122
Cdd:cd17786   82 VAAFLSENGLERCAVVDDNGrVVGIVTITDL 112

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
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494509427   4 RHVMSSPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKhLVGIVSEGDLLRA 56
Cdd:cd04629   65 ADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGK-LVGQISRRDVLRA 116

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 494509427   8 SSPVTtVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLlraRFRElggadsqPDEMTAGDVMASPVVAMTAD 87
Cdd:cd04601    2 TDPVT-LSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDI---RFET-------DLSTPVSEVMTPDERLVTAP 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 494509427  88 AEVS-ELASAMLR-SRLRGIPIVHDHDIL-GIVTRPDL 122
Cdd:cd04601   71 EGITlEEAKEILHkHKIEKLPIVDDNGELvGLITRKDI 108

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 494509427    10 PVTTVDRSTSVDECLQLVGSSGFTVLPVVDERKHLVGIVSEGDLLRAR 57
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in 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 494509427   7 MSSPVTTVDRSTSVDECLQL-----VGSSgftvlpVVDERKHLVGIVSEGDLLRARFRelggADSQPDEMTAGDVMASPV 81
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERmlrnrVGSV------VVTDDGTPAGILTETDALHAGYA----TDDPFSEIPVRAVASRPL 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 494509427  82 VAMTADAEVSELASAMLRSRLRGIPIVHDHDILGIVTRPDLIAV 125
Cdd:cd17776   71 VTISPTATLREAAERMVDEGVKKLPVVDGLDLVGILTATDIIRA 114

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494509427   3 ARHVMS--SPVTTVDRSTSVDECLQLVGSSGFTVLPVVDERK-HLVGIVSEGDLLRArfrelggADSQPDEMTAGDVMAs 79
Cdd:cd04590    2 VREVMTprTDVVALDADATLEELLELILESGYSRFPVYEGDLdNIIGVLHVKDLLAA-------LLEGREKLDLRALLR- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494509427  80 PVVAMTADAEVSELASAMLRSRLRgIPIVHD--HDILGIVTRPDLI 123
Cdd:cd04590   74 PPLFVPETTPLDDLLEEFRKERSH-MAIVVDeyGGTAGIVTLEDIL 118

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 494509427   73 AGDVMASPVVAMTADAEVSELASAMLRSRLRGIPIV-HDHDILGIVTRPDLIAVL 126
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVdEDGKLVGIVTLKDLLRAL 55

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).