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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506  79 DYMSPPVIVKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRASMIGEDIHTMPISVNMSRMPNLTYLEEDE 158
Cdd:cd04617     1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1126136506 159 LIIYAADQMIEKEIDSIPIVKnKGNNKYQVTGRISKTTIAKLFVSL 204
Cdd:cd04617    81 SVLEAARKLIEHEIDSLPVVE-KEDGKLKVVGRITKTNITRLFVEL 125

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506  79 DYMSPPVIVKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRASMIGEDIHTMPISVNMSRMPNLTYLEEDE 158
Cdd:cd04617     1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1126136506 159 LIIYAADQMIEKEIDSIPIVKnKGNNKYQVTGRISKTTIAKLFVSL 204
Cdd:cd04617    81 SVLEAARKLIEHEIDSLPVVE-KEDGKLKVVGRITKTNITRLFVEL 125

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1126136506   8 EQIIEIV-KSGGPITGEHIAEKLDLTRATLRPDLAILTMSGF-LEARPRVGY 57
Cdd:pfam08279   1 LQILQLLlEARGPISGQELAEKLGVSRRTIRRDIKILEELGVpIEAEPGRGY 52

DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1126136506   1 MELSKRQEQIIEIVKSGGPITGEHIAEKLDLTRATLRPDLAILTMSGFLE 50
Cdd:COG1349     1 MLAEERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLR 50

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        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506  79 DYMSPPVIVKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRASMIGEDIHTMPISVNMSRMPNLTYLEEDE 158
Cdd:cd04617     1 DIMSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPNIVTVTPDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1126136506 159 LIIYAADQMIEKEIDSIPIVKnKGNNKYQVTGRISKTTIAKLFVSL 204
Cdd:cd04617    81 SVLEAARKLIEHEIDSLPVVE-KEDGKLKVVGRITKTNITRLFVEL 125

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506  77 VKDYMS-PPVIVKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRASMI-GEDIHTMPISVNMSRmpNLTYL 154
Cdd:COG2905     1 VKDIMSrDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAeGLDPLDTPVSEVMTR--PPITV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1126136506 155 EEDELIIYAADQMIEKEIDSIPIVKNKgnnkyQVTGRISKTTIAKLF 201
Cdd:COG2905    79 SPDDSLAEALELMEEHRIRHLPVVDDG-----KLVGIVSITDLLRAL 120

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 1126136506  81 MSPPVIVKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRASMIGEDIHTMPISVNMSrmPNLTYLEEDELI 160
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMT--PDVITVSPDTDL 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1126136506 161 IYAADQMIEKEIDSIPIVKNKGNnkyqVTGRISKTTIAK 199
Cdd:cd02205    79 EEALELMLEHGIRRLPVVDDDGK----LVGIVTRRDILR 113

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1126136506   8 EQIIEIV-KSGGPITGEHIAEKLDLTRATLRPDLAILTMSGF-LEARPRVGY 57
Cdd:pfam08279   1 LQILQLLlEARGPISGQELAEKLGVSRRTIRRDIKILEELGVpIEAEPGRGY 52

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 1126136506  82 SPPVIVKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRASMIGEDIHTmPISVNMSRmpNLTYLEEDELII 161
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDT-PVEEIMTK--NLVTVSPDESIY 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1126136506 162 YAADQMIEKEIDSIPIVKNKGnnkyQVTGRISKTTIAK 199
Cdd:cd09836    80 EAAELMREHNIRHLPVVDGGG----KLVGVISIRDLAR 113

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 1126136506  77 VKDYMSPPVI-VKEDMTVYDAICTIFLEDAGTLFITNEhNDFIGVCSRKDLLRAS----------MIGEDIHTMPISVNM 145
Cdd:cd04584     2 VKDIMTKNVVtVTPDTSLAEARELMKEHKIRHLPVVDD-GKLVGIVTDRDLLRASpskatslsiyELNYLLSKIPVKDIM 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1126136506 146 SRmpNLTYLEEDELIIYAADQMIEKEIDSIPIVKNKgnnkyQVTGRISKTTIAKLFV 202
Cdd:cd04584    81 TK--DVITVSPDDTVEEAALLMLENKIGCLPVVDGG-----KLVGIITETDILRAFI 130

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506  76 VVKDYMS-PPVIVKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRAsmIGEDIHTmpISVNMSRmpNLTYL 154
Cdd:cd04605     1 LVEDIMSkDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKA--VALKKDS--LEEIMTR--NVITA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1126136506 155 EEDELIIYAADQMIEKEIDSIPIVknkgNNKYQVTGRISKTTIAKL 200
Cdd:cd04605    75 RPDEPIELAARKMEKHNISALPVV----DDDRRVIGIITSDDISRL 116

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126136506  69 TDKLRQYVVKDYMSPPVI-VKEDMTVYDAICTIFLEDAGTLFITNEHNDFIGVCSRKDLLRA 129
Cdd:cd04632    66 KERMLDLPVYDIMSSPVVtVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127

Biotin operon repressor [Transcription];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506   1 MELSKRQeQIIEIVKSGGPITGEHIAEKLDLTRATLRPDLAILTMSGF-LEARPRVGYYYSGKsknklmTDKLRQYVVKD 79
Cdd:COG1654     1 MMSSTRL-KLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGYeIESVPGKGYRLAEP------PDLLDPEEIRA 73

                          90
                  ....*....|
gi 1126136506  80 YMSPPVIVKE 89
Cdd:COG1654    74 GLSTKRLGRE 83

Transcriptional regulator of NAD metabolism, contains HTH and 3H domains [Transcription, Coenzyme transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506   1 MELSKRQEQIIEIVK-SGGPITGEHIAEKLDLTRATLRPDLAILTMSGF-LEARPRvGYYYSGKSKNKLMTdklRQYVVK 78
Cdd:COG1827     1 MDGEERREKILEILKeSKEPISGSELAKKFGVSRQVIVQDIALLRAKGEpIIATPR-GYILLKAESSKGFT---RVIACK 76

Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126136506   1 MELSKRQEQIIEIVKSGGPITGEHIAEKLDLTRATLRPDLAILTMSGF-LEARPRV--GYYYS 60
Cdd:COG2378     1 MSRLERLLALLQLLQSRRGVTAAELAERLEVSERTIYRDIDALRELGVpIEAERGRggGYRLR 63

DeoR-like helix-turn-helix domain;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1126136506   6 RQEQIIEIVKSGGPITGEHIAEKLDLTRATLRPDLAILTMSGFLE 50
Cdd:pfam08220   1 RIQQILELLKQQGTLSVEELAELLGVSEMTIRRDLNELEEQGLLT 45

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126136506  80 YMSPPVI-VKEDMTVYDAICTI--FLEDAGT---LFITNEHNDFIGVCSRKDLLRAS---MIGEDIHTMPISVNmsrmpn 150
Cdd:COG2239   134 LMTTEFVaVREDWTVGEALRYLrrQAEDPETiyyIYVVDDDGRLVGVVSLRDLLLADpdtKVSDIMDTDVISVP------ 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1126136506 151 lTYLEEDEliiyAADQMIEKEIDSIPIVknkgNNKYQVTGRI 192
Cdd:COG2239   208 -ADDDQEE----VARLFERYDLLALPVV----DEEGRLVGII 240

Predicted transcriptional regulator [Transcription];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126136506   3 LSKRQEQI-IEIVKSGGPITGEHIAEKLDLTRATLRPDLAILTMSGFLEARPRV----GYYYS 60
Cdd:COG3355    25 LSETDAEVyLILLENGEPLTVEELAEALDRSRSTVYRSLQKLLEAGLVEREKRNleggGYPYV 87

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 1126136506  44 TMSGFLEARPRVGYYYSGKSKNKLMTDKLRQY---VVKDYMSPPVI-VKEDMTVYDAICTIFLEDAGTLFITNEHNDFIG 119
Cdd:cd17778    41 KLVGIVTAMDIVKYFGSHEAKKRLTTGDIDEAystPVEEIMSKEVVtIEPDADIAEAARLMIKKNVGSLLVVDDEGELKG 120

                          90
                  ....*....|
gi 1126136506 120 VCSRKDLLRA 129
Cdd:cd17778   121 IITERDVLIA 130

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 1126136506  76 VVKDYMSPPVIVkedmtvydAICTIFLEDAGTLFITNE--------HNDFIGVCSRKDLLR--------ASMIGEDIH-- 137
Cdd:cd04631     1 VVEDYMTKNVIT--------ATPGTPIEDVAKIMVRNGfrrlpvvsDGKLVGIVTSTDIMRylgsgeafEKLKTGNIHev 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1126136506 138 -TMPISVNMSRmpNLTYLEEDELIIYAADQMIEKEIDSIPIVKN 180
Cdd:cd04631    73 lNVPISSIMKR--DIITTTPDTDLGEAAELMLEKNIGALPVVDD 114