Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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 1974188977  66 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 145
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1974188977 146 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILK 203
Cdd:cd04618    81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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 1974188977  66 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 145
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1974188977 146 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILK 203
Cdd:cd04618    81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138

CBS domain [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 232 NIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHrsqyfeGVVKCNKL 311
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1974188977 312 ETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQALV 352
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

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 1974188977  236 IHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAA 280
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49

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        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1974188977  157 PLVNISPDASLFDAVYSLIKNKIHRLPVIDPVsGNALYILTHKRILKFLQ 206
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKALA 49

putative manganese-dependent inorganic diphosphatase;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 232 NIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDvinLAaeKTYnnLDITVTQALQHRSQYFEGVVKCNKL 311
Cdd:PRK14869   77 KPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSD---LA--RAY--MDILDPEILSKSPTSLENIIRTLDG 149

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1974188977 312 ETLeTIVDRIVKAEVHRLVVVNETDTIVGIISLSDI 347
Cdd:PRK14869  150 EVL-VGAEEDKVEEGKVVVAAMAPESLLERIEEGDI 184

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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 1974188977  66 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 145
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1974188977 146 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPVSGNALYILTHKRILK 203
Cdd:cd04618    81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138

CBS domain [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 232 NIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHrsqyfeGVVKCNKL 311
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1974188977 312 ETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQALV 352
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

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 1974188977 231 HNIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQALQhrsqyfEGVVKCNK 310
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG-GLALDTPVAEVMT------PDVITVSP 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1974188977 311 LETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQ 349
Cdd:cd02205    75 DTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 231 HNIAFIHPDTPIIKALNIFVDRRISALPVVDEsGKVVDIYSKFDVINLAAEKTYNnLDITVTQALQhrsqyfEGVVKCNK 310
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDL-LDAPVSDIMT------RDVVTVSE 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1974188977 311 LETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQAL 351
Cdd:COG2524   166 DDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 236 IHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKT----YNNLDITVTQALQHRSQYFEG------- 304
Cdd:cd04586     8 VTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGTeprrVWWLDALLESPERLAEEYVKAhgrtvgd 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1974188977 305 -----VVKCNKLETLETIVDRIVKAEVHRLVVVNEtDTIVGIISLSDILQA 350
Cdd:cd04586    88 vmtrpVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLLRA 137

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 156 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpvSGNALYILTHKRILKFLQLFVSEMPKPA--FMKKNLdelgigtyhni 233
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDLLDAPVsdIMTRDV----------- 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1974188977 234 AFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVIN 277
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204

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 1974188977 231 HNIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLD-ITVtqalqhrSQYFEGVVKCN 309
Cdd:cd04629     3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPgGTV-------ADYMSTEVLTV 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1974188977 310 KLETleTIVD---RIVKAEVHRLVVVnETDTIVGIISLSDILQA 350
Cdd:cd04629    76 SPDT--SIVDlaqLFLKNKPRRYPVV-EDGKLVGQISRRDVLRA 116

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 1974188977  74 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETwrelylqe 153
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK-LVGIVTERDILRALVEGGLALDTPVAEVMTPDVIT-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1974188977 154 tfkplvnISPDASLFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILK 203
Cdd:cd02205    72 -------VSPDTDLEEALELMLEHGIRRLPVVDD-DGKLVGIVTRRDILR 113

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 1974188977 232 NIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKTynNLDITVTQALqhrsqyFEGVVKCNKL 311
Cdd:cd09836     4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGI--DLDTPVEEIM------TKNLVTVSPD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1974188977 312 ETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQAL 351
Cdd:cd09836    76 ESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 231 HNIAFIHPDTPIIKALNIFVDRRISALPVVDEsGKVV------DIyskfdVIN-LAAEKTYNnlDITVTQALQHrsqyfe 303
Cdd:cd04622     3 RDVVTVSPDTTLREAARLMRDLDIGALPVCEG-DRLVgmvtdrDI-----VVRaVAEGKDPN--TTTVREVMTG------ 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1974188977 304 GVVKCNKLETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDI 347
Cdd:cd04622    69 DVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 156 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpvSGNALYILTHKRILKFLqlfVSEMPK---PAFMKKNldelgigtyhn 232
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVD--DGKLVGIVTLTDIAKAL---AEGKENakvKDIMTKD----------- 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1974188977 233 IAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINL 278
Cdd:cd04588    66 VITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111

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 1974188977 236 IHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGV-------VKC 308
Cdd:cd04600     8 VTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRDRPETVgdimtrpVVT 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1974188977 309 NKLET-LETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQAL 351
Cdd:cd04600    88 VRPDTpIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLIAAL 131

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977  74 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKqsFVGMLTITDFINILHRYYKSPMVQIYELEEhkietwrelylqe 153
Cdd:COG2524    93 TKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDAPVSDIMT------------- 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1974188977 154 tfKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFL 205
Cdd:COG2524   158 --RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDD-DGKLVGIITRTDILRAL 206

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 156 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDP-------VS-GNALY---ILTHKRILKFLQLFVSEMPKPAFMKKNLDE 224
Cdd:cd04586     3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDDdgklvgiVSeGDLLRreePGTEPRRVWWLDALLESPERLAEEYVKAHG 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1974188977 225 LGIG---TyHNIAFIHPDTPIIKALNIFVDRRISALPVVDEsGKVVDIYSKFDVI 276
Cdd:cd04586    83 RTVGdvmT-RPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLL 135

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 159 VNISPDASLFDAVYSLIKNKIHRLPVidpVSGNALY-ILTHKRILKFL---QLF----------VSEMPKPAFMKKNlde 224
Cdd:cd04631    11 ITATPGTPIEDVAKIMVRNGFRRLPV---VSDGKLVgIVTSTDIMRYLgsgEAFeklktgniheVLNVPISSIMKRD--- 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1974188977 225 lgigtyhnIAFIHPDTPIIKALNIFVDRRISALPVVDEsGKVVDIYSKFDVIN 277
Cdd:cd04631    85 --------IITTTPDTDLGEAAELMLEKNIGALPVVDD-GKLVGIITERDILR 128

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 1974188977 156 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFL-QLFVSEMPKPAFMKKNLdelgIGTYhnia 234
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVaEGIDLDTPVEEIMTKNL----VTVS---- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1974188977 235 fihPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVIN 277
Cdd:cd09836    74 ---PDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113

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 1974188977 156 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpvSGNALYILTHKRILKFL-----QLFVSEMPKPAFMKKNLDELgigTY 230
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFgsheaKKRLTTGDIDEAYSTPVEEI---MS 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1974188977 231 HNIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVI 276
Cdd:cd17778    83 KEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 232 NIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQalqhrsqyfeGVVKCNKL 311
Cdd:cd04605     9 DVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALK-KDSLEEIMTR----------NVITARPD 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1974188977 312 ETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDI 347
Cdd:cd04605    78 EPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113

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
                  ....*....|....*....|....*....|....*....|....*...
gi 1974188977 305 VVKCNKLETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQALV 352
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56

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 1974188977 156 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPvSGNALYILTHKRILKFLqlfvsempkpAFMKKNLDElgIGTyHNIAF 235
Cdd:cd04605     8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSE-DGKLIGIVTSWDISKAV----------ALKKDSLEE--IMT-RNVIT 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1974188977 236 IHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYS 271
Cdd:cd04605    74 ARPDEPIELAARKMEKHNISALPVVDDDRRVIGIIT 109

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 1974188977 232 NIAFIHPDTPIIKALNIFVDRRISALPVVDeSGKVVDIYSKFDVI-NLAAEKTYNNLDIT-VTQALQHRSQYF--EGVVK 307
Cdd:cd17778     9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVkYFGSHEAKKRLTTGdIDEAYSTPVEEImsKEVVT 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1974188977 308 CNKLETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDILQAL 351
Cdd:cd17778    88 IEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131

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 1974188977 236 IHPDTPIIKALNIFVDRRISALPVVDEsGKVVDIYSKFDVinlaaektynnlDITVTQALQH---RSQYFEGVVKCNKLE 312
Cdd:cd04595     7 VSPDTTIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDV------------DKAKHHGLGHapvKGYMSTNVITIDPDT 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1974188977 313 TLETIVDRIVKAEVHRLVVVNEtDTIVGIISLSDILQA 350
Cdd:cd04595    74 SLEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVLRY 110

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974188977 230 YHNIAFIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSkfdVINLAAEKTYnnldITVTqalqhrsqyfEGVVKCN 309
Cdd:cd04597     4 YDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLS---ISDIARTVDY----IMTK----------DNLIVFK 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1974188977 310 KLETLETIVDRIVKAEVHRLVVVNETDTIVGIISLSDIL 348
Cdd:cd04597    67 EDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLI 105

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 1974188977 235 FIHPDTPIIKALNIFVDRRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDiTVTQALqhrsqyFEGVVKCNKLETL 314
Cdd:cd04608    14 TVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSD-PVSKAM------YKQFKQVDLDTPL 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1974188977 315 ETiVDRIVKaEVHRLVVVNETDTIVGIISLSDIL 348
Cdd:cd04608    87 GA-LSRILE-RDHFALVVDGQGKVLGIVTRIDLL 118

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 1974188977 161 ISPDASLFDAVYSLIKNKIHRLPVIDPvSGNALYILT-----HKRILK---FLQLFVSEMpkpafMKKNLdelgigtyhn 232
Cdd:cd04623     7 VSPDATVAEALRLLAEKNIGALVVVDD-GGRLVGILSerdyvRKLALRgasSLDTPVSEI-----MTRDV---------- 70