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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQP---EVFSNFRQLTVKSFATKiat 367
Cdd:COG3448   7 IMTRD-VVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDrldELEERLLDLPVEDVMTR--- 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42563087 368 ageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 422
Cdd:COG3448  82 ---------PVVTVTPDTPLEEAAELMLEHGIHRLPV-VDDDGRLVGIVTRTDLL 126

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087  60 VIEIQAETPVSEAVKILSDSKILSAPVINTDH-------ESSLDWRERYLGIIDYSSIILWVLESAELAA 122
Cdd:cd04586   5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGklvgivsEGDLLRREEPGTEPRRVWWLDALLESPERLA 74

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQP---EVFSNFRQLTVKSFATKiat 367
Cdd:COG3448   7 IMTRD-VVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDrldELEERLLDLPVEDVMTR--- 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42563087 368 ageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 422
Cdd:COG3448  82 ---------PVVTVTPDTPLEEAAELMLEHGIHRLPV-VDDDGRLVGIVTRTDLL 126

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 219 PFLPVSTESSMLSVMLLLSKYRLRNVPVIKTGEPdiKNYVTQSAVVHGLEGCKGRDwfdhisALPISDLglpfMSPNeVI 298
Cdd:COG2524  95 DVITVSPDTTLEEALELMLEKGISGLPVVDDGKL--VGIITERDLLKALAEGRDLL------DAPVSDI----MTRD-VV 161

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 42563087 299 SIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI 340
Cdd:COG2524 162 TVSEDDSLEEALRLMLEHGIGRLPVVDD-DGKLVGIITRTDI 202

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 42563087   291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLL 345
Cdd:pfam00571   4 IMTKD-VVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRALL 56

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

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087  60 VIEIQAETPVSEAVKILSDSKILSAPVINTDH-------ESSLDWRERYLGIIDYSSIILWVLESAELAA 122
Cdd:cd04586   5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGklvgivsEGDLLRREEPGTEPRRVWWLDALLESPERLA 74

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087  29 RKNLPKSLQETLNSAFAGIPVSSFPQVPggrVIEIQAETPVSEAVKILSDSKILSAPVINTDHessldwreRYLGIIDYS 108
Cdd:COG3448  55 LRALLPDRLDELEERLLDLPVEDVMTRP---VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDG--------RLVGIVTRT 123

                        90
                ....*....|...
gi 42563087 109 SIILWVLESAELA 121
Cdd:COG3448 124 DLLRALARLLEEE 136

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

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 42563087     59 RVIEIQAETPVSEAVKILSDSKILSAPVINTDhessldwrERYLGIIDYSSII 111
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE--------GRLVGIVTRRDII 45

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQP---EVFSNFRQLTVKSFATKiat 367
Cdd:COG3448   7 IMTRD-VVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDrldELEERLLDLPVEDVMTR--- 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42563087 368 ageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 422
Cdd:COG3448  82 ---------PVVTVTPDTPLEEAAELMLEHGIHRLPV-VDDDGRLVGIVTRTDLL 126

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRYLLLQPEVFSNfrqLTVKSFATKiatage 370
Cdd:COG2524  91 IMTKD-VITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDLLD---APVSDIMTR------ 158

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42563087 371 eyglaiPAITCRPDSTLGSVINSLASRSVHRVYVAaGDENELYGVITLRDVI 422
Cdd:COG2524 159 ------DVVTVSEDDSLEEALRLMLEHGIGRLPVV-DDDGKLVGIITRTDIL 203

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 42563087 296 EVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQPEVFSNfrqLTVKSFATKiatageeygla 375
Cdd:cd02205   3 DVVTVDPDTTVREALELMAENGIGALPVVDD-DGKLVGIVTERDILRALVEGGLALD---TPVAEVMTP----------- 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42563087 376 iPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 422
Cdd:cd02205  68 -DVITVSPDTDLEEALELMLEHGIRRLPV-VDDDGKLVGIVTRRDIL 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).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 292 MSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI----------RYLLLQPEVFSNFRQLT---V 358
Cdd:cd04586   1 MTTD-VVTVTPDTSVREAARLLLEHRISGLPVVDD-DGKLVGIVSEGDLlrreepgtepRRVWWLDALLESPERLAeeyV 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42563087 359 KSFATK---IATAgeeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVAagDENELYGVITLRDVI 422
Cdd:cd04586  79 KAHGRTvgdVMTR--------PVVTVSPDTPLEEAARLMERHRIKRLPVV--DDGKLVGIVSRADLL 135

CBS domain [Signal transduction mechanisms];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 223 VSTESSMLSVMLLLSKYRLRNVPVI-KTGEPD-IknyVTQSAVVHGLEGcKGRDWFDhisaLPISDlglpFMSPNeVISI 300
Cdd:COG0517  14 VSPDATVREALELMSEKRIGGLPVVdEDGKLVgI---VTDRDLRRALAA-EGKDLLD----TPVSE----VMTRP-PVTV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42563087 301 ESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQP 347
Cdd:COG0517  81 SPDTSLEEAAELMEEHKIRRLPVVDD-DGRLVGIITIKDLLKALLEP 126

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 42563087 292 MSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQpevfSNFRQLTVKSFATKiatagee 371
Cdd:cd09836   1 MSKP-VVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVAE----GIDLDTPVEEIMTK------- 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 42563087 372 yglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 422
Cdd:cd09836  68 -----NLVTVSPDESIYEAAELMREHNIRHLPV-VDGGGKLVGVISIRDLA 112

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 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRY-------LLLQPEVFSNFRQLTVKSFAT 363
Cdd:cd04584   5 IMTKN-VVTVTPDTSLAEARELMKEHKIRHLPVVD--DGKLVGIVTDRDLLRaspskatSLSIYELNYLLSKIPVKDIMT 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42563087 364 KiatageeyglaiPAITCRPDSTLGSVINSLASrsvHRVyvaaG-----DENELYGVITLRDVISCFV 426
Cdd:cd04584  82 K------------DVITVSPDDTVEEAALLMLE---NKI----GclpvvDGGKLVGIITETDILRAFI 130

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 42563087 294 PNEVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI-RYLLLQPEvfsNFRQLTVKSFATKiatageey 372
Cdd:cd04623   1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDD-GGRLVGILSERDYvRKLALRGA---SSLDTPVSEIMTR-------- 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 42563087 373 glaiPAITCRPDSTLGSVinsLASRSVHRV-YVAAGDENELYGVITLRDVI 422
Cdd:cd04623  69 ----DVVTCTPDDTVEEC---MALMTERRIrHLPVVEDGKLVGIVSIGDVV 112

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
                ....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI 340
Cdd:cd09836  64 IMTKN-LVTVSPDESIYEAAELMREHNIRHLPVVDG-GGKLVGVISIRDL 111

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 297 VISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRYLLLqpevfSNFRQLTVKSFATKiatageeyglai 376
Cdd:cd04595   4 VKTVSPDTTIEEARKIMLRYGHTGLPVVE--DGKLVGIISRRDVDKAKH-----HGLGHAPVKGYMST------------ 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 42563087 377 PAITCRPDSTLGSVINSLASRSVHRVYVAagDENELYGVITLRDVI 422
Cdd:cd04595  65 NVITIDPDTSLEEAQELMVEHDIGRLPVV--EEGKLVGIVTRSDVL 108

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 42563087    377 PAITCRPDSTLGSVINSLASRSVHRVYVAaGDENELYGVITLRDVISCF 425
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVV-DEEGRLVGIVTRRDIIKAL 48

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 42563087 292 MSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRY 342
Cdd:cd04599   1 MTRN-PITISPLDSVARAAALMERQRIGGLPVVE--NGKLVGIITSRDVRR 48

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 284 ISDLGLPFmspneVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI-RYLLLQPEVFSnfrqLTVKSFA 362
Cdd:cd04608   4 VRRLDLGA-----PVTVLPDDTLGEAIEIMREYGVDQLPVVDE-DGRVVGMVTEGNLlSSLLAGRAQPS----DPVSKAM 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563087 363 TKiatageeyglaiPAITCRPDSTLGSVinslaSRSVHRVYVA--AGDENELYGVITLRDVIS 423
Cdd:cd04608  74 YK------------QFKQVDLDTPLGAL-----SRILERDHFAlvVDGQGKVLGIVTRIDLLN 119

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

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42563087 280 SALPISDlglpFMSpNEVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDI 340
Cdd:cd04801  57 EATRVRD----VMT-KDVITVSPDADAMEALKLMSQNNIGRLPVVE--DGELVGIISRTDL 110

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
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42563087 279 ISALPISDLglpfMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI 340
Cdd:cd04604  67 ILNLPAKDV----MTRN-PKTISPDALAAEALELMEEHKITVLPVVDE-DGKPVGILHLHDL 122

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 322 PVVEGlNKKIVGNISMRDIRYLLLQPEVFsnfRQLTVKSFATKiatageeyglaiPAITCRPDSTLGSVINSLASRSV-H 400
Cdd:cd04613  30 PVVDE-QGRLTGILSIQDVRGVLFEEELW---DLVVVKDLATT------------DVITVTPDDDLYTALLKFTSTNLdQ 93

                        90       100
                ....*....|....*....|....*
gi 42563087 401 RVYVAAGDENELYGVITLRDVISCF 425
Cdd:cd04613  94 LPVVDDDDPGKVLGMLSRRDVIAAY 118

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 235 LLSKYRLRNVPVIKTGEpdIKNYVTQS----AVVHGLEGCKgrdwfdhisalpISDLglpfMSPNeVISIESEELILEAF 310
Cdd:cd04588  19 LLSENNIHGAPVVDDGK--LVGIVTLTdiakALAEGKENAK------------VKDI----MTKD-VITIDKDEKIYDAI 79

                        90       100       110
                ....*....|....*....|....*....|
gi 42563087 311 KRMRDNNIGGLPVVEGlNKKIVGNISMRDI 340
Cdd:cd04588  80 RLMNKHNIGRLIVVDD-NGKPVGIITRTDI 108

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSpNEVISIESEELILEAFKRMRDNNIGGLPVVEGlnKKIVGNISMRDIRYLLLQPEVFSNFRQLTVKSFATKIatagE 370
Cdd:cd17778   5 FMT-TPVVTIYPDDTLKEAMELMVTRGFRRLPVVSG--GKLVGIVTAMDIVKYFGSHEAKKRLTTGDIDEAYSTP----V 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 42563087 371 EYGLAIPAITCRPDSTLGSVINSLASRSVHRVYVAaGDENELYGVITLRDVI 422
Cdd:cd17778  78 EEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVV-DDEGELKGIITERDVL 128

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRYLLLQPEVFS-----NFRQLT---VKSFA 362
Cdd:cd04631   5 YMTKN-VITATPGTPIEDVAKIMVRNGFRRLPVVS--DGKLVGIVTSTDIMRYLGSGEAFEklktgNIHEVLnvpISSIM 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42563087 363 TKiatageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVAagDENELYGVITLRDVISCF 425
Cdd:cd04631  82 KR------------DIITTTPDTDLGEAAELMLEKNIGALPVV--DDGKLVGIITERDILRAI 130

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 293 SPneVISIESEELILEAFKRMRDNNIGGLPVVEGLNKKIVGNISMRDIrylllQPEVFSNFRQLTVKSF-ATKIATAGee 371
Cdd:cd17772   2 SP--VISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVA-----EKAIYHGLGDLPVSEYmTTEFATVT-- 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 42563087 372 yglaipaitcrPDSTLGSVINSLASRsvHRVYVAAGDENELYGVITLRDVI 422
Cdd:cd17772  73 -----------PDAPLSEIQEIIVEQ--RQRLVPVVEDGRLVGVITRTDLL 110

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

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 42563087 296 EVISIESEELILEAFKRMRDNNIGGLPVVEGLNKKIvGNISMRDI 340
Cdd:cd04597   6 KVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLI-GLLSISDI 49

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42563087 297 VISIESEELILEAFKRMRDNNIGGLPVVEGLNkKIVGNISMRDIRYLLLQpevfSNFR-QLTVKSFATKiatageeygla 375
Cdd:cd17784   4 VITAKPNEGVVEAFEKMLKHKISALPVVDDEG-KLIGIVTATDLGHNLIL----DKYElGTTVEEVMVK----------- 67

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42563087 376 iPAITCRPDSTLGSVI-----NSLASRSVHRVYVAagDENELYGVITLRDVIS 423
Cdd:cd17784  68 -DVATVHPDETLLEAIkkmdsNAPDEEIINQLPVV--DDGKLVGIISDGDIIR 117

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).

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 42563087 380 TCRPDSTLGSVINSLASRSVHRVyVAAGDENELYGVITLRDVISCFV 426
Cdd:cd04641  79 TCTLNDTLETIIDRIVKAEVHRL-VVVDEEDRLEGIVSLSDILKYLV 124

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 42563087 291 FMSPNEVISieseelilEAFKRMRDNNIGGLPVVEGLNkKIVGNISMRDIRYL 343
Cdd:cd04601   6 TLSPDATVA--------DVLELKAEYGISGVPVTEDGG-KLVGIVTSRDIRFE 49

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

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 42563087 291 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDI 340
Cdd:cd04595  61 YMSTN-VITIDPDTSLEEAQELMVEHDIGRLPVVE--EGKLVGIVTRSDV 107