NCBI Conserved Domain Search

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341399 [Multi-domain] Cd Length: 124 Bit Score: 190.03 E-value: 1.55e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 137 TFRDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNHLDMSVGEALRQRTLCLEGVLSC 216
Cdd:cd04641     1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958801841 217 QPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALV 260
Cdd:cd04641    81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124

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).

Pssm-ID: 341388 [Multi-domain] Cd Length: 138 Bit Score: 188.53 E-value: 1.10e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841   1 MVANGVRAAPLWDSKKQSFVGMLTITDFILVLHRYYRSPLVQIYEIEEHKIETWREIYLQGCFKPLVSISPNDSLFEAVY 80
Cdd:cd04618    28 LVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIETWREIERQIGVPPLVSVHPEDSLYDAAL 107

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958801841  81 ALIKNRIHRLPVLDPVSGTVLYILTHKRLLK 111
Cdd:cd04618   108 LLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 89.92 E-value: 1.64e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNHLDMSVGEALRQrtlcleGVLSCQP 218
Cdd:COG0517     9 TDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALV 260
Cdd:COG0517    83 DTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

CBS-domain-containing membrane protein [Signal transduction mechanisms];

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 85.69 E-value: 6.15e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAA-----QQTYNHLDMSVGEALRQRtlclegV 213
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLpdrldELEERLLDLPVEDVMTRP------V 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841 214 LSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALV 260
Cdd:COG3448    84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130

CBS-domain-containing membrane protein [Signal transduction mechanisms];

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 84.92 E-value: 1.55e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLHIFGALLPRPSFLCRTIQDLgigTFRDLAV 143
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDRLDELEERLLDLPVEDV---MTRPVVT 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841 144 VLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQ 190
Cdd:COG3448    86 VTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARL 132

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).

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 79.21 E-value: 1.10e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNhLDMSVGEALRqrtlclEGVLSCQP 218
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLA-LDTPVAEVMT------PDVITVSP 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQ 257
Cdd:cd02205    75 DTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 77.18 E-value: 7.93e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNHLDMSVGEALRQRtlclegVLSCQP 218
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRP------PITVSP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDEtQHLLGVVSLSDILQAL 259
Cdd:COG2905    81 DDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRAL 120

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 76.46 E-value: 1.17e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNEsGQVVGLYSRFDVIHLAAQQTYnHLDMSVGEalrqrtLCLEGVLSCQP 218
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRD-LLDAPVSD------IMTRDVVTVSE 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:COG2524   166 DDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206

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).

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 69.58 E-value: 4.69e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLHIFGALLPRPSFLCRTiqdlgigtfRDLAV 143
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDD-DGKLVGIVTERDILRALVEGGLALDTPVAEVMT---------PDVIT 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 144 VLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI 184
Cdd:cd02205    72 VSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112

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).

Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 69.00 E-value: 1.06e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQT---YNHLDMSVGEALRQ---------- 205
Cdd:cd04586     3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGTeprRVWWLDALLESPERlaeeyvkahg 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801841 206 ---RTLCLEGVLSCQPHESLGEVIDRIAREQVHRLVLVDEtQHLLGVVSLSDILQA 258
Cdd:cd04586    83 rtvGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLLRA 137

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 70.30 E-value: 1.91e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  19 FVGMLTITDFILVLHRYYRSPLVQIYEIEEHKIETWREIylqgCFKPLVSISPNDSLFEAVYALIKNRIHRLPVLDpvSG 98
Cdd:COG2524    53 AGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDI----MTKDVITVSPDTTLEEALELMLEKGISGLPVVD--DG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  99 TVLYILTHKRLLKFLHIFGALLPRPsflcrtIQDLgigTFRDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLY 178
Cdd:COG2524   127 KLVGIITERDLLKALAEGRDLLDAP------VSDI---MTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGII 197


                  ....*.
gi 1958801841 179 SRFDVI 184
Cdd:COG2524   198 TRTDIL 203

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 67.97 E-value: 2.33e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDpVSGTVLYILTHKRLLKFLHIFGAllprpSFLCRTIQDlgIGTfRDLAV 143
Cdd:COG0517     9 TDVVTVSPDATVREALELMSEKRIGGLPVVD-EDGKLVGIVTDRDLRRALAAEGK-----DLLDTPVSE--VMT-RPPVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841 144 VLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQ 190
Cdd:COG0517    80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEP 126

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).

Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 66.68 E-value: 7.02e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDpvSGTVLYILTHKRLLKFLHIFGALLPRPS----FLCRTIQDlgIGTfR 139
Cdd:cd04584     8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVD--DGKLVGIVTDRDLLRASPSKATSLSIYElnylLSKIPVKD--IMT-K 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801841 140 DLAVVLETAPILTALDIFVDRRVSALPVVNEsGQVVGLYSRFDVIHLA 187
Cdd:cd04584    83 DVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129

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).

Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 65.54 E-value: 1.41e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTY-NHLDMSVGEALRqrtlclEGVLSCQ 217
Cdd:cd04629     3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYhCEPGGTVADYMS------TEVLTVS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 218 PHESLGEVIDRIAREQVHRLVLVDETQhLLGVVSLSDILQA 258
Cdd:cd04629    77 PDTSIVDLAQLFLKNKPRRYPVVEDGK-LVGQISRRDVLRA 116

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 64.16 E-value: 6.82e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 137 TFRDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVihlaaqqtynhldMSVGEALRQRTLCLEGVLSC 216
Cdd:COG4109    23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDI-------------LGKDDDTPIEDVMTKNPITV 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958801841 217 QPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:COG4109    90 TPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132

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).

Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 60.51 E-value: 1.03e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVnESGQVVGLYSRFD-VIHLAAQQTyNHLDMSVGEAlrqrtlCLEGVLSCQ 217
Cdd:cd04622     3 RDVVTVSPDTTLREAARLMRDLDIGALPVC-EGDRLVGMVTDRDiVVRAVAEGK-DPNTTTVREV------MTGDVVTCS 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958801841 218 PHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDI 255
Cdd:cd04622    75 PDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

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).

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 59.18 E-value: 2.53e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841   1 MVANGVRAAPLWDSKKQsFVGMLTITDFILVLHRYYRSPLVQIYEIEEhkietwreiylqgcfKPLVSISPNDSLFEAVY 80
Cdd:cd02205    20 MAENGIGALPVVDDDGK-LVGIVTERDILRALVEGGLALDTPVAEVMT---------------PDVITVSPDTDLEEALE 83

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958801841  81 ALIKNRIHRLPVLDPvSGTVLYILTHKRLLK 111
Cdd:cd02205    84 LMLEHGIRRLPVVDD-DGKLVGIVTRRDILR 113

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 57.15 E-value: 1.76e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLhifgaLLPRPSFLCRTIQDlgIGTfRDLAV 143
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDD-DGRLVGIITDRDLRRRV-----LAEGLDPLDTPVSE--VMT-RPPIT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841 144 VLETAPILTALDIFVDRRVSALPVVNEsGQVVGLYSRFDVIHLAAQQ 190
Cdd:COG2905    78 VSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSEE 123

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).

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 57.57 E-value: 1.82e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLHifgaLLPRPSFLCRTIQDLGIGTFRDLAV 143
Cdd:cd04600     3 RDVVTVTPDTSLEEAWRLLRRHRIKALPVVDR-ARRLVGIVTLADLLKHAD----LDPPRGLRGRLRRTLGLRRDRPETV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801841 144 ----------VLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI 184
Cdd:cd04600    78 gdimtrpvvtVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128

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

Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 57.44 E-value: 1.85e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLL---------KFLHIFGALLPRPSFLCRTIQDLG 134
Cdd:cd04586     3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDD-DGKLVGIVSEGDLLrreepgtepRRVWWLDALLESPERLAEEYVKAH 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801841 135 IGTFRDL-----AVVLETAPILTALDIFVDRRVSALPVVNEsGQVVGLYSRFDVIH 185
Cdd:cd04586    82 GRTVGDVmtrpvVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLLR 136

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).

Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 53.68 E-value: 3.00e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTynHLDMSVGEALRqrtlclEGVLSCQP 218
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGI--DLDTPVEEIMT------KNLVTVSP 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:cd09836    75 DESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115

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).

Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 53.10 E-value: 5.67e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYnhlDMSVGEAL--RQRTLCL------ 210
Cdd:cd04632     2 EEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGT---KTRGGDRGgeKERMLDLpvydim 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801841 211 -EGVLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQA 258
Cdd:cd04632    79 sSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127

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.

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 50.20 E-value: 1.09e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958801841  140 DLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAA 188
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49

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).

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 51.26 E-value: 2.12e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNHLDMSVGEALRQRtlclegVLSCQP 218
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRD------VVTCTP 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958801841 219 HESLGEVIDRIAREQV-HRLVLVDEtqHLLGVVSLSDI 255
Cdd:cd04623    76 DDTVEECMALMTERRIrHLPVVEDG--KLVGIVSIGDV 111

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.

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 49.05 E-value: 2.41e-08

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958801841  213 VLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48

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

Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 51.08 E-value: 3.73e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPVSGTVLYILTHKRLLKFL-----------HIFGALLPRPSFLCRTIQD 132
Cdd:cd17779     8 KDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskynlvekKHNGNLLAAINEPVREIMT 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958801841 133 lgigtfRDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI 184
Cdd:cd17779    88 ------RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 50.68 E-value: 5.36e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  67 VSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLHIFgallprpsflcrTIQDLGIgtfRDLAVVLE 146
Cdd:COG4109    28 ATLSEDDTVEDALELLEKTGHSRFPVVDE-NGRLVGIVTSKDILGKDDDT------------PIEDVMT---KNPITVTP 91

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958801841 147 TAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI 184
Cdd:COG4109    92 DTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.

Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 50.42 E-value: 7.57e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDpvSGTVLYILTHKRLLKFLhifGALLPRPSFLCRTIQDL-------GIG 136
Cdd:cd17777    10 PPVLSISPSAPILSAFEKMNRRGIRRLVVVD--ENKLEGILSARDLVSYL---GGGCLFKIVESRHQGDLysalnreVVE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801841 137 TF--RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI 184
Cdd:cd17777    85 TImtPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 49.83 E-value: 7.87e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841   1 MVANGVRAAPLWDSKKQsFVGMLTITDFILVLHRYYRSPL-VQIYEIeehkietwreiylqgCFKPLVSISPNDSLFEAV 79
Cdd:COG2905    25 MTEKGVGSLVVVDDDGR-LVGIITDRDLRRRVLAEGLDPLdTPVSEV---------------MTRPPITVSPDDSLAEAL 88

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958801841  80 YALIKNRIHRLPVLDpvSGTVLYILTHKRLLKFL 113
Cdd:COG2905    89 ELMEEHRIRHLPVVD--DGKLVGIVSITDLLRAL 120

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).

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 49.87 E-value: 9.03e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNHLDMSVGEAL---RQRTLCLEGVLS 215
Cdd:cd04600     3 RDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLglrRDRPETVGDIMT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801841 216 C-----QPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:cd04600    83 RpvvtvRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLIAAL 131

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.

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 47.21 E-value: 1.37e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHL 186
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54

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.

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 47.21 E-value: 1.38e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801841 213 VLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALV 260
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56

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).

Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 48.67 E-value: 1.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLHIfGALLPRPsflcrtiqdLGIGTFRDLAV 143
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVAE-GIDLDTP---------VEEIMTKNLVT 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 144 VLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI 184
Cdd:cd09836    72 VSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLA 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).

Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 48.20 E-value: 2.38e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  66 LVSISPNDSLFEAVYALIKNRIHRLPVLDpVSGTVLYILTHKRLLKflhifgALLpRPSFLC---RTIQDLgigTFRDLA 142
Cdd:cd04629     5 PVTLTPDTSILEAVELLLEHKISGAPVVD-EQGRLVGFLSEQDCLK------ALL-EASYHCepgGTVADY---MSTEVL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958801841 143 VVLETAPILTALDIFVDRRVSALPVVnESGQVVGLYSRFDVI 184
Cdd:cd04629    74 TVSPDTSIVDLAQLFLKNKPRRYPVV-EDGKLVGQISRRDVL 114

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341397 [Multi-domain] Cd Length: 120 Bit Score: 48.34 E-value: 2.42e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 143 VVLETAPILTA---LDIFVDRRVSA------LPVVNESGQVVGLYSRFDVIhlaAQQTYNHLDMSVGEALRQrtlcLEGV 213
Cdd:cd04639     2 AMVTEFPIVDAdltLREFADDYLIGkkswreFLVTDEAGRLVGLITVDDLR---AIPTSQWPDTPVRELMKP----LEEI 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958801841 214 LSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:cd04639    75 PTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIELL 120

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.

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 46.35 E-value: 2.81e-07

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801841   65 PLVSISPNDSLFEAVYALIKNRIHRLPVLDPVsGTVLYILTHKRLLKFLH 114
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKALA 49

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.

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 46.94 E-value: 8.59e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDpvSGTVLYILTHKRLLKFL--HIFGALLPRPS---FLCRTIQDLgigTF 138
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFgsHEAKKRLTTGDideAYSTPVEEI---MS 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI 184
Cdd:cd17778    83 KEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128

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

Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 46.65 E-value: 9.59e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 150 ILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNhLDMSVGEALrqrtlcLEGVLSCQPHESLGEVIDRI 229
Cdd:cd17784    13 VVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKYE-LGTTVEEVM------VKDVATVHPDETLLEAIKKM 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958801841 230 -----AREQVHRLVLVDETQhLLGVVSLSDILQAL 259
Cdd:cd17784    86 dsnapDEEIINQLPVVDDGK-LVGIISDGDIIRAI 119

CBS-domain-containing membrane protein [Signal transduction mechanisms];

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 47.17 E-value: 1.01e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801841 213 VLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALVLS 262
Cdd:COG3448    12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPD 61

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).

Pssm-ID: 341408 [Multi-domain] Cd Length: 112 Bit Score: 46.41 E-value: 1.17e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPVSGTVLYILTHKRLLKFLHifgallprpsflcrtiqdLGIGTF----- 138
Cdd:cd17772     2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIY------------------HGLGDLpvsey 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 --RDLAVVLETAPILTALDIFVDRRVSALPVVnESGQVVGLYSRFDVIHL 186
Cdd:cd17772    64 mtTEFATVTPDAPLSEIQEIIVEQRQRLVPVV-EDGRLVGVITRTDLLNL 112

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.

Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 48.92 E-value: 1.36e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  67 VSISPNDSLFEAVYALIKNRIHRLPVLDpvSGTVLYILThKRLLKFlhifgallprPSFLCRTIQDlgIGTFRDLAVVLE 146
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVD--DGKLVGIVT-NRDLRF----------ETDLSQPVSE--VMTKENLVTAPE 155

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958801841 147 TAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDV 183
Cdd:pfam00478 156 GTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192

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).

Pssm-ID: 341425 [Multi-domain] Cd Length: 141 Bit Score: 46.70 E-value: 1.47e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958801841 140 DLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAA 188
Cdd:cd17789     4 KLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDS 52

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

Pssm-ID: 341403 [Multi-domain] Cd Length: 116 Bit Score: 46.06 E-value: 1.64e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 149 PILTALDIFVDRRVSALpVVNESGQVVGLYSRFDVihLAaqqtynhLDMSVGEALRQ--RTLCLEGVLSCQPHESLGEVI 226
Cdd:cd09833    15 PLADAAARMAERRCSSI-LIVENGEIVGIWTERDA--LK-------LDFSDPDAFRRpiSEVMSSPVLTIPQDTTLGEAA 84

                          90       100
                  ....*....|....*....|....*....
gi 1958801841 227 DRIAREQVHRLVLVDETQHLLGVVSLSDI 255
Cdd:cd09833    85 VRFRQEGVRHLLVVDDDGRPVGIVSQTDV 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.

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 44.13 E-value: 1.75e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLH 114
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRALL 56

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).

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 45.87 E-value: 1.82e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  66 LVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFLHIFGAllprpSFLCRTIQDlgIGTfRDLAVVL 145
Cdd:cd04623     4 VVTVSPDATVAEALRLLAEKNIGALVVVDD-GGRLVGILSERDYVRKLALRGA-----SSLDTPVSE--IMT-RDVVTCT 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958801841 146 ETAPILTALDIFVDRRVSALPVVnESGQVVGLYSRFDVI 184
Cdd:cd04623    75 PDDTVEECMALMTERRIRHLPVV-EDGKLVGIVSIGDVV 112

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).

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 44.93 E-value: 3.72e-06

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801841 213 VLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALV 260
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51

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).

Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 44.83 E-value: 3.86e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDpvSGTVLYILThkrllkfLHIFGALLPRpSFLCRTIQDlgIGTfRDLAV 143
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVD--DGKLVGIVT-------LTDIAKALAE-GKENAKVKD--IMT-KDVIT 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958801841 144 VLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHL 186
Cdd:cd04588    69 IDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111

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).

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 44.45 E-value: 5.93e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801841 203 LRQRTLCLEGVLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALV 260
Cdd:cd04608     2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLL 59

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 44.09 E-value: 1.06e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801841 197 MSVGEALRQRtlclegVLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALVLSPAGIDALSA 271
Cdd:COG0517     1 MKVKDIMTTD------VVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPV 69

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).

Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 43.29 E-value: 1.20e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNEsGQVVGLYSRFDVIHLAAQqtyNHLDMSVGEALRQRtlclegVLSCQP 218
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD-GKLVGIVTLTDIAKALAE---GKENAKVKDIMTKD------VITIDK 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQ 257
Cdd:cd04588    72 DEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 43.68 E-value: 1.52e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841 213 VLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:cd17774    79 LFSLRPDDSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSLLQAL 125

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 42.51 E-value: 2.69e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801841 206 RTLCLEGVLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALVLspAGIDALSA 271
Cdd:COG2905     2 KDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLA--EGLDPLDT 65

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).

Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 42.80 E-value: 3.44e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841   1 MVANGVRAAPLWDSKKQsFVGMLTITDFI----LVLHRYYRSPL------VQIYEIEEHKIETWR--EIylqgCFKPLVS 68
Cdd:cd04586    21 LLEHRISGLPVVDDDGK-LVGIVSEGDLLrreePGTEPRRVWWLdallesPERLAEEYVKAHGRTvgDV----MTRPVVT 95

                          90       100
                  ....*....|....*....|....*.
gi 1958801841  69 ISPNDSLFEAVYALIKNRIHRLPVLD 94
Cdd:cd04586    96 VSPDTPLEEAARLMERHRIKRLPVVD 121

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

Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 42.60 E-value: 3.75e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841   1 MVANGVRAAPLWDSKKQSFVGMLTITDFI----------LVLHRYYRSPLV----QIYEIEEHKIetwreiylqgcfkpl 66
Cdd:cd17779    26 MTEKGFRRLPVADAGTKRLEGIVTSMDIVdflgggskynLVEKKHNGNLLAainePVREIMTRDV--------------- 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841  67 VSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKFL 113
Cdd:cd17779    91 ISVKENASIDDAIELMLEKNVGGLPIVDK-DGKVIGIVTERDFLKFL 136

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 43.33 E-value: 4.19e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 132 DLGIGTFRDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNHLDMSVGEALRQRTLCLE 211
Cdd:COG2524    15 LLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTK 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958801841 212 GVLSCQPHESLGEVIDRIAREQVHRLVLVDEtQHLLGVVSLSDILQAL 259
Cdd:COG2524    95 DVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKAL 141

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.

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 41.93 E-value: 5.12e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVnESGQVVGLYSRFDVIH-LAAQQTYNHLDM-SVGEAL--RQRTLCLEGVL 214
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVV-SGGKLVGIVTAMDIVKyFGSHEAKKRLTTgDIDEAYstPVEEIMSKEVV 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958801841 215 SCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:cd17778    87 TIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131

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

Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 41.35 E-value: 5.55e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 150 ILTALDIFVDRRVSALPVVNESGQVVGlysrfdVIHLAAQQTYNHLDMSVGEALRQRtlclegVLSCQPHESLGEVIDRI 229
Cdd:cd04583    13 LAQAIEIMREKRVDSLLVVDKDNVLLG------IVDIEDINRNYRKAKKVGEIMERD------VFTVKEDSLLRDTVDRI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958801841 230 AREQVHRLVLVDETQHLLGVV---SLSDIL 256
Cdd:cd04583    81 LKRGLKYVPVVDEQGRLVGLVtraSLVDIV 110

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).

Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 41.55 E-value: 6.25e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801841 213 VLSCQPHESLGEVIDRIAR-----EQVHRLVLVDETQHLLGVVSLSDILQA 258
Cdd:cd04606    11 FVAVRPDWTVEEALEYLRRlapdpETIYYIYVVDEDRRLLGVVSLRDLLLA 61

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

Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 41.17 E-value: 6.56e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 138 FRDLAVVLETaPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVihlaAQQTYNHldmsVGEALRQrtlcleGVLSCQ 217
Cdd:cd04594     2 IRDIKVSAYD-TVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDI----ENKSPGK----VGKYVVR------GSPYVT 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 218 PHESLGEVIDRIAREQVhRLVLVDETQHLLGVVSLSDILQA 258
Cdd:cd04594    67 PTSSLEEAWEIMMRNKS-RWVAVVEKGKFLGIITLDDLLEA 106

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).

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 41.36 E-value: 8.28e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVI-HLAAQQTynHLDMSVGEALRQRtlclegVLSCQ 217
Cdd:cd04608    10 GAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLsSLLAGRA--QPSDPVSKAMYKQ------FKQVD 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958801841 218 PHESLGEViDRIArEQVHRLVLVDETQHLLGVVSLSDIL 256
Cdd:cd04608    82 LDTPLGAL-SRIL-ERDHFALVVDGQGKVLGIVTRIDLL 118

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

Pssm-ID: 341407 [Multi-domain] Cd Length: 115 Bit Score: 41.15 E-value: 8.81e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQTYNhLDMSVGEALRQRTLCLEgvlscqP 218
Cdd:cd17771     4 REPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQID-LDAPISEVMTPDPVRLP------P 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQhLLGVVSLSDIL 256
Cdd:cd17771    77 SASAFEAALLMAEHGFRHVCVVDNGR-LVGVVSERDLF 113

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

Pssm-ID: 341396 [Multi-domain] Cd Length: 109 Bit Score: 40.40 E-value: 1.32e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 152 TALDIFVDRRVSALPVVN-ESGQVVGLYSRFDVIHlaaqqtyNHldmsvgEALRQRTLCLEGVLSCQPHESLGEVIDRIA 230
Cdd:cd04638    16 DVLEILKKKAISGVPVVKkETGKLVGIVTRKDLLR-------NP------DEEQIALLMSRDPITISPDDTLSEAAELML 82

                          90       100
                  ....*....|....*....|....*...
gi 1958801841 231 REQVHRLVLVDETQhLLGVVSLSDILQA 258
Cdd:cd04638    83 EHNIRRVPVVDDDK-LVGIVTVADLVRA 109

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).

Pssm-ID: 341363 [Multi-domain] Cd Length: 114 Bit Score: 40.49 E-value: 1.35e-04

                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLD 94
Cdd:cd04587    68 PPPVTIDADALVFEALLLMLERNIHHLPVVD 98

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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).

Pssm-ID: 341371 [Multi-domain] Cd Length: 108 Bit Score: 39.76 E-value: 2.00e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 166 PVVNESGQVVGLYSRFDVIHLAAQQTYNHLdMSvgealRQrtlclegVLSCQPHESLGEVIDRIAREQVHRLVLVDETQH 245
Cdd:cd04596    29 PVVDEENRVVGIVTAKDVIGKEDDTPIEKV-MT-----KN-------PITVKPKTSVASAAHMMIWEGIELLPVVDENRK 95

                          90
                  ....*....|...
gi 1958801841 246 LLGVVSLSDILQA 258
Cdd:cd04596    96 LLGVISRQDVLKA 108

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).

Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 39.70 E-value: 2.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  67 VSISPNDSLFEAVYALIKNRIHRLPVLDPVsGTVLYILThKRLLKFLHIFGALL-----PRPsflcrtiqdlgigtfrDL 141
Cdd:cd04601     5 VTLSPDATVADVLELKAEYGISGVPVTEDG-GKLVGIVT-SRDIRFETDLSTPVsevmtPDE----------------RL 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958801841 142 AVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDV 183
Cdd:cd04601    67 VTAPEGITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDI 108

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 42.36 E-value: 2.10e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958801841 213 VLSCQPHESLGEVIDRIAR-----EQVHRLVLVDETQHLLGVVSLSDILQA 258
Cdd:COG2239   139 FVAVREDWTVGEALRYLRRqaedpETIYYIYVVDDDGRLVGVVSLRDLLLA 189

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).

Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 39.83 E-value: 2.62e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFD-VIHLAAQQTyNHLDMSVGEALRQRTLCLegvlscQ 217
Cdd:cd17775     3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDiVVEVVAKGL-DPKDVTVGDIMSADLITA------R 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958801841 218 PHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQAL 259
Cdd:cd17775    76 EDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117

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

Pssm-ID: 341407 [Multi-domain] Cd Length: 115 Bit Score: 39.61 E-value: 3.15e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801841 214 LSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALVLSPAGIDA 268
Cdd:cd17771     7 VTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDLDA 61

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

Pssm-ID: 341385 [Multi-domain] Cd Length: 119 Bit Score: 39.10 E-value: 3.83e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVIHLAAQQtynhldmSVGEALRQRTLCLEGVLSCQP 218
Cdd:cd04613     3 RKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEE-------ELWDLVVVKDLATTDVITVTP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQH--LLGVVSLSDILQA 258
Cdd:cd04613    76 DDDLYTALLKFTSTNLDQLPVVDDDDPgkVLGMLSRRDVIAA 117

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).

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 39.14 E-value: 3.84e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDvIHLAAQQTYNHLD--MSvgealrqrtlclEGVLSC 216
Cdd:cd04605     8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWD-ISKAVALKKDSLEeiMT------------RNVITA 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958801841 217 QPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDI 255
Cdd:cd04605    75 RPDEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113

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).

Pssm-ID: 341412 [Multi-domain] Cd Length: 115 Bit Score: 38.16 E-value: 9.49e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801841  20 VGMLTITDFILVLHRYYRsPL--VQIYEIEEHkietwreiylqgcfkPLVSISPNDSLFEAVYALIKNRIHRLPVLD 94
Cdd:cd17776    38 AGILTETDALHAGYATDD-PFseIPVRAVASR---------------PLVTISPTATLREAAERMVDEGVKKLPVVD 98

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).

Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 37.79 E-value: 1.41e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841 213 VLSCQPHESLGEVIDRIAREQVHRLVLVDEtQHLLGVVSLSDILQAL 259
Cdd:cd04584    10 VVTVTPDTSLAEARELMKEHKIRHLPVVDD-GKLVGIVTDRDLLRAS 55

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).

Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 37.39 E-value: 1.52e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVihlaaqQTYNHLDMSVGEALRQRtlclEGVLSCQP 218
Cdd:cd04601     2 TDPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDI------RFETDLSTPVSEVMTPD----ERLVTAPE 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDIL 256
Cdd:cd04601    72 GITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIE 109

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341418 [Multi-domain] Cd Length: 118 Bit Score: 37.23 E-value: 1.90e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  65 PLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLkfLHIFGALL------------PRPSFlcrtiqd 132
Cdd:cd17782     3 PPPLVSPKTTVREAARLMKENRTTAVLVMDN-SGKVIGIFTSKDVV--LRVLAAGLdpattsvvrvmtPNPET------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958801841 133 lgigtfrdlavVLETAPILTALDIFVDRRVSALPVVNESGQVVGLysrFDVIHL 186
Cdd:cd17782    73 -----------APPSTTILDALHKMHEGKFLNLPVVDDEGEIVGL---VDVLQL 112

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.

Pssm-ID: 341394 [Multi-domain] Cd Length: 130 Bit Score: 37.59 E-value: 1.94e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 148 APILTALDIFVDRRVSALPVVNEsGQVVGLYSRFDVIH-LAAQQTYNHLDM-SVGEALRQR--TLCLEGVLSCQPHESLG 223
Cdd:cd04631    17 TPIEDVAKIMVRNGFRRLPVVSD-GKLVGIVTSTDIMRyLGSGEAFEKLKTgNIHEVLNVPisSIMKRDIITTTPDTDLG 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958801841 224 EVIDRIAREQVHRLVLVDEtQHLLGVVSLSDILQAL 259
Cdd:cd04631    96 EAAELMLEKNIGALPVVDD-GKLVGIITERDILRAI 130

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).

Pssm-ID: 341366 [Multi-domain] Cd Length: 119 Bit Score: 37.09 E-value: 1.94e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  66 LVSISPNDSLFEAVYALIKNRIHRLPVLDPVSGTVLYILTHKRLLKFLhifgaLLPRPSFLCRTIQdlgigtfRDLAVVL 145
Cdd:cd04590    12 VVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAAL-----LEGREKLDLRALL-------RPPLFVP 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958801841 146 ETAPILTALDIFVDRRVS-ALpVVNESGQVVGL 177
Cdd:cd04590    80 ETTPLDDLLEEFRKERSHmAI-VVDEYGGTAGI 111

voltage-gated chloride channel ClcB;

Pssm-ID: 234987 [Multi-domain] Cd Length: 574 Bit Score: 39.34 E-value: 2.19e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 143 VVLETAPILTALDIFVDRRVSALPVVNESGQVVGLYSRFDVihlaaqqTYNHLDMSVGEALRQRTLCLEGVLSCQPHESL 222
Cdd:PRK01862  459 VVPPTASVADMTRVFLEYPVKYLYVVDDDGRFRGAVALKDI-------TSDLLDKRDTTDKTAADYAHTPFPLLTPDMPL 531

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958801841 223 GEVIDRIAREQVHRLVLVDETQH--LLGVVSLSDILQALV 260
Cdd:PRK01862  532 GDALEHFMAFQGERLPVVESEASptLAGVVYKTSLLDAYR 571

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 36.78 E-value: 2.46e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958801841 139 RDLAVVLETAPILTALDIFVDRRVSALPVVnESGQVVGLYSRFDVIH 185
Cdd:cd04801    67 KDVITVSPDADAMEALKLMSQNNIGRLPVV-EDGELVGIISRTDLMR 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).

Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 36.74 E-value: 2.96e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841   4 NGVRAAPLWDSKKqsFVGMLTITDFILVLHRyyrsplvqiyEIEEHKIEtwrEIYLqgcfKPLVSISPNDSLFEAVYALI 83
Cdd:cd04588    23 NNIHGAPVVDDGK--LVGIVTLTDIAKALAE----------GKENAKVK---DIMT----KDVITIDKDEKIYDAIRLMN 83

                          90       100
                  ....*....|....*....|....*...
gi 1958801841  84 KNRIHRLPVLDPvSGTVLYILTHKRLLK 111
Cdd:cd04588    84 KHNIGRLIVVDD-NGKPVGIITRTDILK 110

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

Pssm-ID: 341384 [Multi-domain] Cd Length: 131 Bit Score: 36.93 E-value: 3.24e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  74 SLFEAVYALIKNRIHRLPVLDPVSGtvLYILTHKRLLKFL------HIFGALLPRPsflcrtiqdlgigtfrdLAVVLET 147
Cdd:cd04611    23 SLAEAARRMRSHRADAAVIECPDGG--LGILTERDLVRFIarhpgnTPVGELASRP-----------------LLTVGAE 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958801841 148 APILTALDIFVDRRVSALPVVNESGQVVGL 177
Cdd:cd04611    84 DSLIHARDLLIDHRIRHLAVVDEDGQVTGL 113

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).

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 36.74 E-value: 3.44e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  64 KPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSGTVLYILTHKRLLKflhifgALLPRPSFLCRTIQDLgigTFRDLAV 143
Cdd:cd04608    10 GAPVTVLPDDTLGEAIEIMREYGVDQLPVVDE-DGRVVGMVTEGNLLS------SLLAGRAQPSDPVSKA---MYKQFKQ 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958801841 144 VLETAPILTALDIFvDRRVSALpVVNESGQVVGLYSRFDVI 184
Cdd:cd04608    80 VDLDTPLGALSRIL-ERDHFAL-VVDGQGKVLGIVTRIDLL 118

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.

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 34.80 E-value: 3.61e-03

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958801841    1 MVANGVRAAPLWDSKKQsFVGMLTITDFILVLH 33
Cdd:smart00116  18 LRENGIRRLPVVDEEGR-LVGIVTRRDIIKALA 49

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 36.43 E-value: 4.38e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841  19 FVGMLTITDFILVLhryyrsPLVQIYEIeehkietwreiylqgCFKPLVSISPNDSLFEAVYALIKNRIHRLPVLDPvSG 98
Cdd:COG4109    60 LVGIVTSKDILGKD------DDTPIEDV---------------MTKNPITVTPDTSLASAAHKMIWEGIELLPVVDD-DG 117

                          90
                  ....*....|....*.
gi 1958801841  99 TVLYILTHKRLLKFLH 114
Cdd:COG4109   118 RLLGIISRQDVLKALQ 133

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).

Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 35.94 E-value: 5.23e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 143 VVLETAPILTALDIFVDRRVSALPVVNEsGQVVGLYSRFDVIHlAAQQTYNHLD----MSvgealrqrtlclEGVLSCQP 218
Cdd:cd04595     6 TVSPDTTIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDVDK-AKHHGLGHAPvkgyMS------------TNVITIDP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958801841 219 HESLGEVIDRIAREQVHRLVLVDETQhLLGVVSLSDILQA 258
Cdd:cd04595    72 DTSLEEAQELMVEHDIGRLPVVEEGK-LVGIVTRSDVLRY 110

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).

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 36.00 E-value: 6.07e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958801841 213 VLSCQPHESLGEVIDRIAREQVHRLVLVDETQHLLGVVSLSDILQALVLSPAG 265
Cdd:cd04600     5 VVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPR 57

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).

Pssm-ID: 341365 [Multi-domain] Cd Length: 113 Bit Score: 35.63 E-value: 6.28e-03

                          10        20        30
                  ....*....|....*....|....*....|
gi 1958801841  65 PLVSISPNDSLFEAVYALIKNRIHRLPVLD 94
Cdd:cd04589    68 PLISVEPDDFLFNALLLMTRHRVKRVVVRE 97

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

Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 35.39 E-value: 7.81e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958801841  67 VSISPNDSLFEAVYALIKNRIHRLPVLDpvSGTVLYILTHKRLL 110
Cdd:cd04599    64 VTISPEASLWEAKELMEEHGIERLVVVE--EGRLVGIITKSTLY 105

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

Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 35.01 E-value: 9.76e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801841 161 RVSALPVVNEsGQVVGLYSRFDVIhlaaqqtYNHLDMSVGEALRqrtlclEGVLSCQPHESLGEVIDRIAREQVHRLVLV 240
Cdd:cd04599    25 RIGGLPVVEN-GKLVGIITSRDVR-------RAHPNRLVADAMS------RNVVTISPEASLWEAKELMEEHGIERLVVV 90

                          90
                  ....*....|....*.
gi 1958801841 241 DETQhLLGVVSLSDIL 256
Cdd:cd04599    91 EEGR-LVGIITKSTLY 105