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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQP---EVFSNFRQLTVKSFATKiat 396
Cdd:COG3448    7 IMTRD-VVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDrldELEERLLDLPVEDVMTR--- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145327199 397 ageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 451
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 145327199  89 VIEIQAETPVSEAVKILSDSKILSAPVINTDH-------ESSLDWRERYLGIIDYSSIILWVLESAELAA 151
Cdd:cd04586    5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGklvgivsEGDLLRREEPGTEPRRVWWLDALLESPERLA 74

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQP---EVFSNFRQLTVKSFATKiat 396
Cdd:COG3448    7 IMTRD-VVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDrldELEERLLDLPVEDVMTR--- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145327199 397 ageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 451
Cdd:COG3448   82 ---------PVVTVTPDTPLEEAAELMLEHGIHRLPV-VDDDGRLVGIVTRTDLL 126

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 248 PFLPVSTESSMLSVMLLLSKYRLRNVPVIKTGEPdiKNYVTQSAVVHGLEGCKGRDwfdhisALPISDLglpfMSPNeVI 327
Cdd:COG2524   95 DVITVSPDTTLEEALELMLEKGISGLPVVDDGKL--VGIITERDLLKALAEGRDLL------DAPVSDI----MTRD-VV 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 145327199 328 SIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI 369
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 145327199  320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLL 374
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 145327199  89 VIEIQAETPVSEAVKILSDSKILSAPVINTDH-------ESSLDWRERYLGIIDYSSIILWVLESAELAA 151
Cdd:cd04586    5 VVTVTPDTSVREAARLLLEHRISGLPVVDDDGklvgivsEGDLLRREEPGTEPRRVWWLDALLESPERLA 74

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

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145327199  88 RVIEIQAETPVSEAVKILSDSKILSAPVINTDhessldwreRYLGIIDYSSIILWVLESAEL 149
Cdd:COG2524   95 DVITVSPDTTLEEALELMLEKGISGLPVVDDG---------KLVGIITERDLLKALAEGRDL 147

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 145327199   89 VIEIQAETPVSEAVKILSDSKILSAPVINTDhessldwrERYLGIIDYSSIILWVLE 145
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDED--------GKLVGIVTLKDLLRALLG 57

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQP---EVFSNFRQLTVKSFATKiat 396
Cdd:COG3448    7 IMTRD-VVTVSPDTTLREALELMREHGIRGLPVVDE-DGRLVGIVTERDLLRALLPDrldELEERLLDLPVEDVMTR--- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145327199 397 ageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 451
Cdd:COG3448   82 ---------PVVTVTPDTPLEEAAELMLEHGIHRLPV-VDDDGRLVGIVTRTDLL 126

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRYLLLQPEVFSNfrqLTVKSFATKiatage 399
Cdd:COG2524   91 IMTKD-VITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDLLD---APVSDIMTR------ 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145327199 400 eyglaiPAITCRPDSTLGSVINSLASRSVHRVYVAaGDENELYGVITLRDVI 451
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 145327199 325 EVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQPEVFSNfrqLTVKSFATKiatageeygla 404
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDD-DGKLVGIVTERDILRALVEGGLALD---TPVAEVMTP----------- 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 145327199 405 iPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 451
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 145327199 321 MSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI----------RYLLLQPEVFSNFRQLT---V 387
Cdd:cd04586    1 MTTD-VVTVTPDTSVREAARLLLEHRISGLPVVDD-DGKLVGIVSEGDLlrreepgtepRRVWWLDALLESPERLAeeyV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145327199 388 KSFATK---IATAgeeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVAagDENELYGVITLRDVI 451
Cdd:cd04586   79 KAHGRTvgdVMTR--------PVVTVSPDTPLEEAARLMERHRIKRLPVV--DDGKLVGIVSRADLL 135

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 145327199 321 MSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDI--RYLLLQpevfSNFRQLTVKSFATKiatag 398
Cdd:cd04622    1 MTRD-VVTVSPDTTLREAARLMRDLDIGALPVCE--GDRLVGMVTDRDIvvRAVAEG----KDPNTTTVREVMTG----- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145327199 399 eeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVAAgDENELYGVITLRDV 450
Cdd:cd04622   69 -------DVVTCSPDDDVEEAARLMAEHQVRRLPVVD-DDGRLVGIVSLGDL 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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 321 MSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIRYLLLQpevfSNFRQLTVKSFATKiatagee 400
Cdd:cd09836    1 MSKP-VVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVAE----GIDLDTPVEEIMTK------- 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145327199 401 yglaiPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVI 451
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 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRY-------LLLQPEVFSNFRQLTVKSFAT 392
Cdd:cd04584    5 IMTKN-VVTVTPDTSLAEARELMKEHKIRHLPVVD--DGKLVGIVTDRDLLRaspskatSLSIYELNYLLSKIPVKDIMT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145327199 393 KiatageeyglaiPAITCRPDSTLGSVINSLASrsvHRVyvaaG-----DENELYGVITLRDVISCFV 455
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 145327199 323 PNEVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI-RYLLLQPEvfsNFRQLTVKSFATKiatageey 401
Cdd:cd04623    1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDD-GGRLVGILSERDYvRKLALRGA---SSLDTPVSEIMTR-------- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145327199 402 glaiPAITCRPDSTLGSVinsLASRSVHRV-YVAAGDENELYGVITLRDVI 451
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 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI 369
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 145327199 326 VISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRYLLLqpevfSNFRQLTVKSFATKiatageeyglai 405
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLRYGHTGLPVVE--DGKLVGIISRRDVDKAKH-----HGLGHAPVKGYMST------------ 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145327199 406 PAITCRPDSTLGSVINSLASRSVHRVYVAagDENELYGVITLRDVI 451
Cdd:cd04595   65 NVITIDPDTSLEEAQELMVEHDIGRLPVV--EEGKLVGIVTRSDVL 108

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199  325 EVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRylllqpevFSNFRQLTVKSFATKiatageeygla 404
Cdd:pfam00478  89 DPVTLSPDATVADALALMERYGISGVPVVD--DGKLVGIVTNRDLR--------FETDLSQPVSEVMTK----------- 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 145327199  405 IPAITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDV 450
Cdd:pfam00478 148 ENLVTAPEGTTLEEAKEILHKHKIEKLPV-VDDNGRLVGLITIKDI 192

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 145327199 321 MSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRY 371
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 145327199 313 ISDLGLPFmspneVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDI-RYLLLQPEVFSnfrqLTVKSFA 391
Cdd:cd04608    4 VRRLDLGA-----PVTVLPDDTLGEAIEIMREYGVDQLPVVDE-DGRVVGMVTEGNLlSSLLAGRAQPS----DPVSKAM 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145327199 392 TKiatageeyglaiPAITCRPDSTLGSVinslaSRSVHRVYVA--AGDENELYGVITLRDVIS 452
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 145327199 309 SALPISDlglpFMSpNEVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDI 369
Cdd:cd04801   57 EATRVRD----VMT-KDVITVSPDADAMEALKLMSQNNIGRLPVVE--DGELVGIISRTDL 110

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 325 EVISIESEELILEAFKRMRDNNIGGLPVVEGlNKKIVGNISMRDIrylllqpevfSNFrqlTVKSfaTKIATAGEEYG-- 402
Cdd:cd04632    3 EVITVNEDDTIGKAINLLREHGISRLPVVDD-NGKLVGIVTTYDI----------VDF---VVRP--GTKTRGGDRGGek 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145327199 403 -----------LAIPAITCRPDSTLGSVINSLASRSVHRVyVAAGDENELYGVITLRDVIS 452
Cdd:cd04632   67 ermldlpvydiMSSPVVTVTRDATVADAVERMLENDISGL-VVTPDDNMVIGILTKTDVLR 126

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327199 318 LPFMSPNEVISIESEELILEAFKRMRDNNIGGLPVVEGlnKKIVGNISMRD-IRYLL---LQPEVFSNFrQLTVKSFATK 393
Cdd:cd17777    4 LMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDE--NKLEGILSARDlVSYLGggcLFKIVESRH-QGDLYSALNR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145327199 394 iaTAGEEYGLAIPaITCRPDSTLGSVINSLASRSVHRVYVaAGDENELYGVITLRDVISCF 454
Cdd:cd17777   81 --EVVETIMTPNP-VYVYEDSDLIEALTIMVTRGIGSLPV-VDRDGRPVGIVTERDLVLYL 137

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 145327199 264 LLSKYRLRNVPVIKTGEpdIKNYVTQS----AVVHGLEGCKgrdwfdhisalpISDLglpfMSPNeVISIESEELILEAF 339
Cdd:cd04588   19 LLSENNIHGAPVVDDGK--LVGIVTLTdiakALAEGKENAK------------VKDI----MTKD-VITIDKDEKIYDAI 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 145327199 340 KRMRDNNIGGLPVVEGlNKKIVGNISMRDI 369
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 145327199 320 FMSpNEVISIESEELILEAFKRMRDNNIGGLPVVEGlnKKIVGNISMRDIRYLLLQPEVFSNFRQLTVKSFATKIatagE 399
Cdd:cd17778    5 FMT-TPVVTIYPDDTLKEAMELMVTRGFRRLPVVSG--GKLVGIVTAMDIVKYFGSHEAKKRLTTGDIDEAYSTP----V 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145327199 400 EYGLAIPAITCRPDSTLGSVINSLASRSVHRVYVAaGDENELYGVITLRDVI 451
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 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDIRYLLLQPEVFS-----NFRQLT---VKSFA 391
Cdd:cd04631    5 YMTKN-VITATPGTPIEDVAKIMVRNGFRRLPVVS--DGKLVGIVTSTDIMRYLGSGEAFEklktgNIHEVLnvpISSIM 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145327199 392 TKiatageeyglaiPAITCRPDSTLGSVINSLASRSVHRVYVAagDENELYGVITLRDVISCF 454
Cdd:cd04631   82 KR------------DIITTTPDTDLGEAAELMLEKNIGALPVV--DDGKLVGIITERDILRAI 130

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; 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 145327199 323 PNeVISIESEELILEAFKRMRDNNIGGLPVVEGLNK--KIVGNISMRDIRYLLLQ 375
Cdd:cd04617   71 PN-IVTVTPDDSVLEAARKLIEHEIDSLPVVEKEDGklKVVGRITKTNITRLFVE 124

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 145327199 326 VISIESEELILEAFKRMRDNNIGGLPVVEGLNkKIVGNISMRDIRYLLLQpevfSNFR-QLTVKSFATKiatageeygla 404
Cdd:cd17784    4 VITAKPNEGVVEAFEKMLKHKISALPVVDDEG-KLIGIVTATDLGHNLIL----DKYElGTTVEEVMVK----------- 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145327199 405 iPAITCRPDSTLGSVI-----NSLASRSVHRVYVAagDENELYGVITLRDVIS 452
Cdd:cd17784   68 -DVATVHPDETLLEAIkkmdsNAPDEEIINQLPVV--DDGKLVGIISDGDIIR 117

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 145327199 320 FMSPnEVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDI 369
Cdd:cd04629   67 YMST-EVLTVSPDTSIVDLAQLFLKNKPRRYPVVE--DGKLVGQISRRDV 113

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 145327199 409 TCRPDSTLGSVINSLASRSVHRVyVAAGDENELYGVITLRDVISCFV 455
Cdd:cd04641   79 TCTLNDTLETIIDRIVKAEVHRL-VVVDEEDRLEGIVSLSDILKYLV 124

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 145327199  406 PAITCRPDSTLGSVINSLASRSVHRVYVAaGDENELYGVITLRDVIS 452
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVV-DEDGKLVGIVTLKDLLR 53

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 145327199 320 FMSPNeVISIESEELILEAFKRMRDNNIGGLPVVEglNKKIVGNISMRDI 369
Cdd:cd04595   61 YMSTN-VITIDPDTSLEEAQELMVEHDIGRLPVVE--EGKLVGIVTRSDV 107