Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  60 LSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVEETPVSKVMTKNPMFVLSETLAV 139
Cdd:cd17781   1 PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSAT 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15242788 140 EALQKMVQGKFRHLPVVE-NGEVIALLDIAKCLYDAIA 176
Cdd:cd17781  81 DALDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 405 FSFKIEDKKHRKHRF-ISDTRSLTEVITAIIQRVGDDIDPDNFPQILYEDEDHDKVLLASDSDLQAAIEHAKSIGWKSLR 483
Cdd:cd06409   1 FAFKFKDPKGRVHRFrLRPSESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLD 80

                ....*
gi 15242788 484 LHLDD 488
Cdd:cd06409  81 LHLHY 85

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  60 LSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVEETPVSKVMTKNPMFVLSETLAV 139
Cdd:cd17781   1 PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSAT 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15242788 140 EALQKMVQGKFRHLPVVE-NGEVIALLDIAKCLYDAIA 176
Cdd:cd17781  81 DALDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  55 VKRLRLSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVEETPVSKVMTKNPMFVLS 134
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSP 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 15242788 135 ETLAVEALQKMVQGKFRHLPVVENGEVIALLDI 167
Cdd:COG2905  81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIVSI 113

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 230 TKVLKVSPTDTVLTVAKKMVEFQSSCAVVIIED-KLRGIFTSKDILMRVVAENLPPSETLVETVMTQNPESTIVDTPIVE 308
Cdd:COG2905   7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDgRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAE 86

                        90
                ....*....|....*...
gi 15242788 309 ALHIMHEGKFLHLPVTDK 326
Cdd:COG2905  87 ALELMEEHRIRHLPVVDD 104

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788    404 TFSFKIEDKkHRKHRFISD-TRSLTEVITAIIQRVGDDIDPdnfPQILYEDEDHDKVLLASDSDLQAAIEHAKSIGWKSL 482
Cdd:smart00666   1 TVDVKLRYG-GETRRLSVPrDISFEDLRSKVAKRFGLDNQS---FTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKL 76

                   ....*
gi 15242788    483 RLHLD 487
Cdd:smart00666  77 RLHVF 81

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242788    55 VKRLRLSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVIS 111
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

inosine-5'-monophosphate dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  235 VSPTDTVLTVAK-KMVEFQSSCAVVI---IEDKLRGIFTSKDILmrvvaeNLPPSETLVETVMTQNPESTIVDTPIV--E 308
Cdd:PTZ00314 109 LSPNHTVADVLEiKEKKGFSSILITVdgkVGGKLLGIVTSRDID------FVKDKSTPVSEVMTPREKLVVGNTPISleE 182

                         90       100
                 ....*....|....*....|.
gi 15242788  309 ALHIMHEGKFLHLPVTDKEGD 329
Cdd:PTZ00314 183 ANEVLRESRKGKLPIVNDNGE 203

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 15242788    232 VLKVSPTDTVLTVAKKMVEFQSSCAVVIIED-KLRGIFTSKDIL 274
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEgRLVGIVTRRDII 45

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  60 LSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVEETPVSKVMTKNPMFVLSETLAV 139
Cdd:cd17781   1 PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSAT 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15242788 140 EALQKMVQGKFRHLPVVE-NGEVIALLDIAKCLYDAIA 176
Cdd:cd17781  81 DALDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  55 VKRLRLSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVEETPVSKVMTKNPMFVLS 134
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSP 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 15242788 135 ETLAVEALQKMVQGKFRHLPVVENGEVIALLDI 167
Cdd:COG2905  81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIVSI 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 231 KVLKVSPTDTVLTVAKKMVEFQSSCAVVIIED-KLRGIFTSKDILMRVVAENLPPSETLVETVMTQNPESTIVDTPIVEA 309
Cdd:cd17781   3 PALTVPETTTVAEAAQLMAAKRTDAVLVVDDDgGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSATDA 82

                        90       100
                ....*....|....*....|
gi 15242788 310 LHIMHEGKFLHLPVTDKEGD 329
Cdd:cd17781  83 LDLMVEGKFRHLPVVDDDGD 102

The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in meiosis and harbors a PB1 domain. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domains depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic amino acid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 405 FSFKIEDKKHRKHRF-ISDTRSLTEVITAIIQRVGDDIDPDNFPQILYEDEDHDKVLLASDSDLQAAIEHAKSIGWKSLR 483
Cdd:cd06409   1 FAFKFKDPKGRVHRFrLRPSESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLD 80

                ....*
gi 15242788 484 LHLDD 488
Cdd:cd06409  81 LHLHY 85

CBS domain [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  54 TVKRLRLSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVEETPVSKVMTKNPMFVL 133
Cdd:COG0517   2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVS 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15242788 134 SETLAVEALQKMVQGKFRHLPVVENGE----VIALLDIAKCLYDAIA 176
Cdd:COG0517  82 PDTSLEEAAELMEEHKIRRLPVVDDDGrlvgIITIKDLLKALLEPLA 128

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  65 TVPATTTIYEACKRMASRRVDALLLTDSNEmLCGILTDKDIATRVISQELNVEETPVSKVMTKNPMFVLSETLAVEALQK 144
Cdd:cd04622   7 TVSPDTTLREAARLMRDLDIGALPVCEGDR-LVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARL 85

                        90       100
                ....*....|....*....|....*...
gi 15242788 145 MVQGKFRHLPVVENGE----VIALLDIA 168
Cdd:cd04622  86 MAEHQVRRLPVVDDDGrlvgIVSLGDLA 113

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  61 SKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVeETPVSKVMTKNPMFVLSETLAVE 140
Cdd:cd02205   2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLAL-DTPVAEVMTPDVITVSPDTDLEE 80

                        90       100
                ....*....|....*....|....*.
gi 15242788 141 ALQKMVQGKFRHLPVV-ENGEVIALL 165
Cdd:cd02205  81 ALELMLEHGIRRLPVVdDDGKLVGIV 106

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  61 SKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIaTRVISQELnVEETPVSKVMTKNPMFVLSETLAVE 140
Cdd:cd09836   3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDI-VRAVAEGI-DLDTPVEEIMTKNLVTVSPDESIYE 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 15242788 141 ALQKMVQGKFRHLPVVENGE----VIALLDIAK 169
Cdd:cd09836  81 AAELMREHNIRHLPVVDGGGklvgVISIRDLAR 113

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  54 TVKRLRLSKALTVPATTTIYEACKRMASRRVDALLLTDSNEmLCGILTDKDIAtRVISQELNVEETPVSKVMTKNPMFVL 133
Cdd:COG2524  87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK-LVGIITERDLL-KALAEGRDLLDAPVSDIMTRDVVTVS 164

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15242788 134 SETLAVEALQKMVQGKFRHLPVVE-NGEVIALL---DIAKCL 171
Cdd:COG2524 165 EDDSLEEALRLMLEHGIGRLPVVDdDGKLVGIItrtDILRAL 206

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 230 TKVLKVSPTDTVLTVAKKMVEFQSSCAVVIIEDKLRGIFTSKDILMRVVAENLPPSETLVETVMTQNPESTIVDTPIVEA 309
Cdd:cd04622   3 RDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEA 82

                        90
                ....*....|....*....
gi 15242788 310 LHIMHEGKFLHLPVTDKEG 328
Cdd:cd04622  83 ARLMAEHQVRRLPVVDDDG 101

PB1 domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788   404 TFSFKIEDKKHRKH-RFISDTRSLTEVITAIIQRVGDDidpDNFPQILYEDEDHDKVLLASDSDLQAAIEHAKSIGWKSL 482
Cdd:pfam00564   1 TVRLKLRYGGGIRRfLSVSRGISFEELRALVEQRFGLD---DVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSL 77

                  ....*.
gi 15242788   483 RLHLDD 488
Cdd:pfam00564  78 RLHVFP 83

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  65 TVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELN-----VEETPVSKVMTKNPMFVLSETLAV 139
Cdd:COG3448  14 TVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerLLDLPVEDVMTRPVVTVTPDTPLE 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15242788 140 EALQKMVQGKFRHLPVV-ENGEVIALL---DIAKCLYDAIAR 177
Cdd:COG3448  94 EAAELMLEHGIHRLPVVdDDGRLVGIVtrtDLLRALARLLEE 135

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 229 DTKVLKVSPTDTVLTVAKKMVEFQSScAVVIIED--KLRGIFTSKDILMRVVAENLPPSETLVETVMTQNPESTIVDTPI 306
Cdd:cd04623   1 GRDVVTVSPDATVAEALRLLAEKNIG-ALVVVDDggRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTV 79

                        90
                ....*....|....*....
gi 15242788 307 VEALHIMHEGKFLHLPVTD 325
Cdd:cd04623  80 EECMALMTERRIRHLPVVE 98

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  66 VPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIAtRVISQELNVEETPVSKVMTKNPMFVLSETLAVEALQKM 145
Cdd:cd04604  18 VSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLR-RALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELM 96

                        90       100
                ....*....|....*....|...
gi 15242788 146 VQGKFRHLPVV-ENGEVIALLDI 167
Cdd:cd04604  97 EEHKITVLPVVdEDGKPVGILHL 119

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  63 ALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIATRVISQELNVEeTPVSKVMTKNPMFVLSETLAVEAL 142
Cdd:cd17771   6 PVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDLD-APISEVMTPDPVRLPPSASAFEAA 84

                        90       100
                ....*....|....*....|...
gi 15242788 143 QKMVQGKFRHLPVVENGEVIALL 165
Cdd:cd17771  85 LLMAEHGFRHVCVVDNGRLVGVV 107

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  62 KALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIatrvisQELNVEETPVSKVMTKNPMFVLSETLAVEA 141
Cdd:cd04583   3 NPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDI------NRNYRKAKKVGEIMERDVFTVKEDSLLRDT 76

                        90
                ....*....|....*..
gi 15242788 142 LQKMVQGKFRHLPVVEN 158
Cdd:cd04583  77 VDRILKRGLKYVPVVDE 93

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  65 TVPATTTIYEACKRMASRRVDALLLTDSNEmLCGILTDKDI-------ATRVISQELN--VEETPVSKVMTKNPMFVLSE 135
Cdd:cd04584  12 TVTPDTSLAEARELMKEHKIRHLPVVDDGK-LVGIVTDRDLlraspskATSLSIYELNylLSKIPVKDIMTKDVITVSPD 90

                        90       100
                ....*....|....*....|....*..
gi 15242788 136 TLAVEALQKMVQGKFRHLPVVENGEVI 162
Cdd:cd04584  91 DTVEEAALLMLENKIGCLPVVDGGKLV 117

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 121 VSKVMTKNPMFVLSETLAVEALQKMVQGKFRHLPVVENGEVIALL---DIakclydaiarmeRAAekgkaiaaavegvek 197
Cdd:cd04584   2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVtdrDL------------LRA--------------- 54

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15242788 198 swgTNTSVPNTFIETLRDRMFRPSLSTIIPddTKVLKVSPTDTVLTVAKKMVEFQSSCAVVIIEDKLRGIFTSKDIL 274
Cdd:cd04584  55 ---SPSKATSLSIYELNYLLSKIPVKDIMT--KDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDIL 126

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 121 VSKVMTKNPMFVLSETLAVEALQKMVQGKFRHLPVV-ENGEVIALL---DIAKCLydAIARMERAAEKGKAIaaavegve 196
Cdd:COG3448   4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVterDLLRAL--LPDRLDELEERLLDL-------- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 197 kswgtntsvpntfieTLRDRMFRPslstiipddtkVLKVSPTDTVLTVAKKMVEFQSSCAVVIIED-KLRGIFTSKDILm 275
Cdd:COG3448  74 ---------------PVEDVMTRP-----------VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDgRLVGIVTRTDLL- 126

                ....*...
gi 15242788 276 RVVAENLP 283
Cdd:COG3448 127 RALARLLE 134

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; 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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788 250 EFQSSCAVVIIEDKLRGIFTSKDILmRVVAENLPPSETLVETVMTQNP----ESTIVDtpIVEALHIMHEGKFLHLPVTD 325
Cdd:cd04620  43 EARSSCVLVVENQQLVGIFTERDVV-RLTASGIDLSGVTIAEVMTQPVitlkESEFQD--IFTVLSLLRQHQIRHLPIVD 119

                ...
gi 15242788 326 KEG 328
Cdd:cd04620 120 DQG 122

Predicted transcriptional regulator containing CBS domains [Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242788  58 LRLSKALTVPATTTIYEACKRMASRRVDALLLTDSNEMLCGILTDKDIatrvisqeLNVEE-TPVSKVMTKNPMFVLSET 136
Cdd:COG4109  22 MTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDI--------LGKDDdTPIEDVMTKNPITVTPDT 93