NCBI Conserved Domain Search

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341388 [Multi-domain] Cd Length: 138 Bit Score: 265.19 E-value: 1.41e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 346 KCYDLIPTSAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKQQFVGMLTITDFIKILQMYYKSPNASMEQLEEHKLDT 425
Cdd:cd04618    1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 220950704 426 WRSVLHNQVM-PLVSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILR 482
Cdd:cd04618   81 WREIERQIGVpPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138

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

Pssm-ID: 341399 [Multi-domain] Cd Length: 124 Bit Score: 229.71 E-value: 2.36e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 508 TYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNEWFEGVQKC 587
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 220950704 588 NLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLV 631
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 89.15 E-value: 8.13e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDpATGNVLYILTHKRILRFLFLyinelPKPAYMQKSLRELKIGTY- 509
Cdd:COG3448    6 DIMtrDVVTVSPDTTLREALELMREHGIRGLPVVD-EDGRLVGIVTERDLLRALLP-----DRLDELEERLLDLPVEDVm 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 220950704 510 -NNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAE 560
Cdd:COG3448   80 tRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131

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

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 83.06 E-value: 6.43e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDlDVSLRKANEhrnewfEGVQKCNLD 590
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLAL-DTPVAEVMT------PDVITVSPD 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 220950704 591 ESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDIL 627
Cdd:cd02205   76 TDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 82.22 E-value: 2.33e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSL--RKANE--HRNewfegVQK 586
Cdd:COG3448   11 DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLldLPVEDvmTRP-----VVT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 220950704 587 CNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLV 631
Cdd:COG3448   86 VTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 77.98 E-value: 4.78e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 429 VLHNQVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDpATGNVLYILTHKRILRFLflyinelpkpAYMQKSLRELKI 506
Cdd:COG0517    1 MKVKDIMttDVVTVSPDATVREALELMSEKRIGGLPVVD-EDGKLVGIVTDRDLRRAL----------AAEGKDLLDTPV 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 220950704 507 GTY--NNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAE 560
Cdd:COG0517   70 SEVmtRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 76.44 E-value: 1.73e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 510 NNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKA-NEHrnewfegVQKCN 588
Cdd:COG0517    9 TDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVmTRP-------PVTVS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 220950704 589 LDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLV 631
Cdd:COG0517   82 PDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 77.23 E-value: 5.73e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 461 LPVIDPATGNVLYILTHKRILRFLFLYINELPKPAYMQKSLRELKIGTY--NNIETADETTSIITALKKFVERRVSALPL 538
Cdd:COG2524   43 LLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDImtKDVITVSPDTTLEEALELMLEKGISGLPV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 539 VDsDGRLVDIYAKFDVINLAAEKTYND----LDVSLRKanehrnewfegVQKCNLDESLYTIMERIVRAEVHRLVVVDEN 614
Cdd:COG2524  123 VD-DGKLVGIITERDLLKALAEGRDLLdapvSDIMTRD-----------VVTVSEDDSLEEALRLMLEHGIGRLPVVDDD 190

                        170
                 ....*....|....*.
gi 220950704 615 RKVIGIISLSDILLYL 630
Cdd:COG2524  191 GKLVGIITRTDILRAL 206

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 74.10 E-value: 1.03e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVslrKANE--HRNewfegVQKCN 588
Cdd:COG2905    8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDT---PVSEvmTRP-----PITVS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 220950704 589 LDESLYTIMERIVRAEVHRLVVVDENRkVIGIISLSDILLYL 630
Cdd:COG2905   80 PDDSLAEALELMEEHRIRHLPVVDDGK-LVGIVSITDLLRAL 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).

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 73.05 E-value: 1.57e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFLFlyinelPKPAYMQKSLRELKIgtyNNIETA 515
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDD-GKLVGIVTERDILRALV------EGGLALDTPVAEVMT---PDVITV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 220950704 516 DETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVIN 556
Cdd:cd02205   73 SPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 71.51 E-value: 7.01e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 354 SAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDsEKQQFVGMLTITDFIKILQMYYKSPNASMEqleehkldtwrsvlhnQ 433
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVD-DDGKLVGIVTERDILRALVEGGLALDTPVA----------------E 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 220950704 434 VM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDpATGNVLYILTHKRILR 482
Cdd:cd02205   64 VMtpDVITVSPDTDLEEALELMLEHGIRRLPVVD-DDGKLVGIVTRRDILR 113

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

Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 68.70 E-value: 6.41e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSlrkanEHRNEWFEGVQKcnlD 590
Cdd:cd09836    4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVE-----EIMTKNLVTVSP---D 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 220950704 591 ESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYL 630
Cdd:cd09836   76 ESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115

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

Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 65.72 E-value: 1.18e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 438 VSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILRFL-----FLYINELPKP---AYMQKSLRElkIGTY 509
Cdd:cd17779   11 ITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskYNLVEKKHNGnllAAINEPVRE--IMTR 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 220950704 510 NNIeTADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVI 555
Cdd:cd17779   89 DVI-SVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 63.73 E-value: 5.14e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 366 VKKAFYALVYNGVRAAPLWDsEKQQFVGMLTITDFIKILqmyyksPNASMEQLEEHKLDtwRSVlhNQVM--PLVSIGPD 443
Cdd:COG3448   21 LREALELMREHGIRGLPVVD-EDGRLVGIVTERDLLRAL------LPDRLDELEERLLD--LPV--EDVMtrPVVTVTPD 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 220950704 444 ASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFLF 485
Cdd:COG3448   90 TPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLLRALA 130

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

Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 63.59 E-value: 6.52e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDpatGNVLY-ILTHKRILRFlflyineLPKPAY------MQKSLRELKIG- 507
Cdd:cd04584    9 NVVTVTPDTSLAEARELMKEHKIRHLPVVD---DGKLVgIVTDRDLLRA-------SPSKATslsiyeLNYLLSKIPVKd 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 220950704 508 --TYNNIeTADETTSIITALKKFVERRVSALPLVDsDGRLVDI 548
Cdd:cd04584   79 imTKDVI-TVSPDDTVEEAALLMLENKIGCLPVVD-GGKLVGI 119

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 62.92 E-value: 9.36e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFLFLyinelpkpayMQKSLRELKIGTY- 509
Cdd:COG2905    3 DIMsrDVVTVSPDATVREAARLMTEKGVGSLVVVDDD-GRLVGIITDRDLRRRVLA----------EGLDPLDTPVSEVm 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 220950704 510 -NNIETADETTSIITALKKFVERRVSALPLVDsDGRLVDI 548
Cdd:COG2905   72 tRPPITVSPDDSLAEALELMEEHRIRHLPVVD-DGKLVGI 110

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 64.90 E-value: 1.21e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 354 SAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKqqFVGMLTITDFIKILqmyykspnASMEQLEEHKLDtwrsvlhnQ 433
Cdd:COG2524   93 TKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK--LVGIITERDLLKAL--------AEGRDLLDAPVS--------D 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 220950704 434 VM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFL 484
Cdd:COG2524  155 IMtrDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDD-GKLVGIITRTDILRAL 206

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

Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 60.91 E-value: 3.94e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNewfegVQKCNLD 590
Cdd:cd04629    4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPGGTVADYMSTE-----VLTVSPD 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 220950704 591 ESLYTIMERIVRAEVHRLVVVdENRKVIGIISLSDIL 627
Cdd:cd04629   79 TSIVDLAQLFLKNKPRRYPVV-EDGKLVGQISRRDVL 114

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

Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 60.52 E-value: 8.46e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKT----YNDLDVSLRKANEHRNEWFEG------ 583
Cdd:cd04586    7 TVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGTeprrVWWLDALLESPERLAEEYVKAhgrtvg 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 220950704 584 ------VQKCNLDESLYTIMERIVRAEVHRLVVVDENRkVIGIISLSDIL 627
Cdd:cd04586   87 dvmtrpVVTVSPDTPLEEAARLMERHRIKRLPVVDDGK-LVGIVSRADLL 135

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

Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 58.98 E-value: 3.09e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDpATGNVLYILT------------HKRILRFLFLYINELPKPAYMQKSLRE 503
Cdd:cd04586    4 DVVTVTPDTSVREAARLLLEHRISGLPVVD-DDGKLVGIVSegdllrreepgtEPRRVWWLDALLESPERLAEEYVKAHG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 220950704 504 LKIG---TYNNIeTADETTSIITALKKFVERRVSALPLVDsDGRLVDIYAKFDVI 555
Cdd:cd04586   83 RTVGdvmTRPVV-TVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLL 135

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

Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 57.54 E-value: 5.33e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDpaTGNVLYILTHKRILRFLFlyiNELPK---PAYMQKslrelkigtynNI 512
Cdd:cd04588    3 DLITLKPDATIKDAAKLLSENNIHGAPVVD--DGKLVGIVTLTDIAKALA---EGKENakvKDIMTK-----------DV 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 220950704 513 ETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINL 557
Cdd:cd04588   67 ITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 57.61 E-value: 8.90e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 508 TYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLaaektynDLDVSLRKANEHRnewfegVQKC 587
Cdd:COG4109   23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK-------DDDTPIEDVMTKN------PITV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 220950704 588 NLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDIL 627
Cdd:COG4109   90 TPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129

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

Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 56.68 E-value: 1.18e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 437 LVSIGPDASLYDAIKILIHSRIHRLPVIDpATGNVLYILTHKRILRFLFL--YINELPKPA--YMQKslrelkigtynNI 512
Cdd:cd04629    5 PVTLTPDTSILEAVELLLEHKISGAPVVD-EQGRLVGFLSEQDCLKALLEasYHCEPGGTVadYMST-----------EV 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 220950704 513 ETADETTSIITALKKFVERRVSALPLVDsDGRLV 546
Cdd:cd04629   73 LTVSPDTSIVDLAQLFLKNKPRRYPVVE-DGKLV 105

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

Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 56.57 E-value: 1.37e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEH------RNEWFEGVQKC 587
Cdd:cd04632    6 TVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRGGDRGGEKERmldlpvYDIMSSPVVTV 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 220950704 588 NLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLY 629
Cdd:cd04632   86 TRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127

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

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 53.29 E-value: 3.17e-09

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 220950704   511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAA 559
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49

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

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 54.64 E-value: 7.14e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDpaTGNVLYILTHKRILRFL-----FLYINELPKPAYMQKSLRELK 505
Cdd:cd17778    4 EFMttPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFgsheaKKRLTTGDIDEAYSTPVEEIM 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 220950704 506 igtYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVI 555
Cdd:cd17778   82 ---SKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128

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

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 51.06 E-value: 2.39e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 220950704  587 CNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLV 631
Cdd:pfam00571  12 VSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56

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

Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 53.50 E-value: 2.48e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDpatGNVLY-ILTHKRILRFL----FLYINELPKPAYMQKSLRELKIGTY- 509
Cdd:cd17777   11 PVLSISPSAPILSAFEKMNRRGIRRLVVVD---ENKLEgILSARDLVSYLgggcLFKIVESRHQGDLYSALNREVVETIm 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 220950704 510 -NNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVI 555
Cdd:cd17777   88 tPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 52.52 E-value: 3.43e-08

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 220950704 433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDPatGNVLYILTHKRILRFL 484
Cdd:COG2905   69 EVMtrPPITVSPDDSLAEALELMEEHRIRHLPVVDD--GKLVGIVSITDLLRAL 120

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

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 50.67 E-value: 3.47e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 220950704  433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFL 484
Cdd:pfam00571   3 DIMtkDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRAL 55

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 52.18 E-value: 5.50e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 376 NGVRAAPLWDsEKQQFVGMLTITDFIKILqmyykspNASMEQLEEHKLDtwrsvlhnQVM--PLVSIGPDASLYDAIKIL 453
Cdd:COG0517   30 KRIGGLPVVD-EDGKLVGIVTDRDLRRAL-------AAEGKDLLDTPVS--------EVMtrPPVTVSPDTSLEEAAELM 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 220950704 454 IHSRIHRLPVIDpATGNVLYILTHKRILRFL 484
Cdd:COG0517   94 EEHKIRRLPVVD-DDGRLVGIITIKDLLKAL 123

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

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 52.18 E-value: 6.56e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFLflyinELPKPAYMQKSLRELKIGTYNN---- 511
Cdd:cd04600    4 DVVTVTPDTSLEEAWRLLRRHRIKALPVVDRA-RRLVGIVTLADLLKHA-----DLDPPRGLRGRLRRTLGLRRDRpetv 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 220950704 512 -------IETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVI 555
Cdd:cd04600   78 gdimtrpVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128

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

Pssm-ID: 341408 [Multi-domain] Cd Length: 112 Bit Score: 51.41 E-value: 7.56e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILRFLFLYINELPKPAYMQKslrelkigtynNIETA 515
Cdd:cd17772    3 PVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIYHGLGDLPVSEYMTT-----------EFATV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 220950704 516 DETTSIITALKKFVERRVSALPLVDsDGRLVDIYAKFDVINL 557
Cdd:cd17772   72 TPDAPLSEIQEIIVEQRQRLVPVVE-DGRLVGVITRTDLLNL 112

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341425 [Multi-domain] Cd Length: 141 Bit Score: 52.09 E-value: 9.00e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 508 TYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEhrnEW--FEGVQ 585
Cdd:cd17789    1 PKGKLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADS---TWktFNEVQ 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 220950704 586 KC------NLDESLYTIMERIVRAE--------------VHRLVVVDENRKVIGIISLSDIL 627
Cdd:cd17789   78 KLlsktngKVVGDVMTPSPLVVREKtnledaarilletkFRRLPVVDSDGKLVGIITRGNVV 139

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

Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 50.99 E-value: 9.73e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDsDGRLVDIYakfdvinlaaekTYNDLDVSLRKANEhrnewFEGVQKC------ 587
Cdd:cd04588    6 TLKPDATIKDAAKLLSENNIHGAPVVD-DGKLVGIV------------TLTDIAKALAEGKE-----NAKVKDImtkdvi 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 220950704 588 --NLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDIL 627
Cdd:cd04588   68 tiDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDIL 109

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 51.45 E-value: 1.16e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 438 VSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFL-FLYINELpkpayMQKslrelkigtynNIETAD 516
Cdd:COG4109   28 ATLSEDDTVEDALELLEKTGHSRFPVVDEN-GRLVGIVTSKDILGKDdDTPIEDV-----MTK-----------NPITVT 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 220950704 517 ETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVIN 556
Cdd:COG4109   91 PDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130

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

Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 50.50 E-value: 1.28e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDsDGRLV------DIyakfdVIN-LAAEKTYNDLDVslrkanehRNEWFEG 583
Cdd:cd04622    4 DVVTVSPDTTLREAARLMRDLDIGALPVCE-GDRLVgmvtdrDI-----VVRaVAEGKDPNTTTV--------REVMTGD 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 220950704 584 VQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDI 626
Cdd:cd04622   70 VVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

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

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 48.28 E-value: 1.50e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 220950704   590 DESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYL 630
Cdd:smart00116   8 DTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48

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

Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 50.60 E-value: 1.60e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFLFL-YINELPKPAYMQKslrelkigtynNIET 514
Cdd:cd09836    4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDD-GKPVGIVTERDIVRAVAEgIDLDTPVEEIMTK-----------NLVT 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 220950704 515 ADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVIN 556
Cdd:cd09836   72 VSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113

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

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 48.28 E-value: 1.63e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 220950704   436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFL 484
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKAL 48

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

Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 53.93 E-value: 2.35e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704  438 VSIGPDASLYDAIKILIHSRIHRLPVIDpaTGNVLYILThKRILRFlflyinelpkPAYMQKSLRElkIGTYNNIETADE 517
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVD--DGKLVGIVT-NRDLRF----------ETDLSQPVSE--VMTKENLVTAPE 155

                          90       100
                  ....*....|....*....|....*....
gi 220950704  518 TTSIITALKKFVERRVSALPLVDSDGRLV 546
Cdd:pfam00478 156 GTTLEEAKEILHKHKIEKLPVVDDNGRLV 184

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

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 49.93 E-value: 2.44e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 510 NNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKtYNDLDVSLRKanehrnewfeGVQKCNL 589
Cdd:cd04605    8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALK-KDSLEEIMTR----------NVITARP 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 220950704 590 DESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDI 626
Cdd:cd04605   77 DEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113

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

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 49.72 E-value: 2.45e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 437 LVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFLFLyinelpkpayMQKSLRELKIGTY--NNIET 514
Cdd:cd04623    4 VVTVSPDATVAEALRLLAEKNIGALVVVDDG-GRLVGILSERDYVRKLAL----------RGASSLDTPVSEImtRDVVT 72

                         90       100       110
                 ....*....|....*....|....*....|....
gi 220950704 515 ADETTSIITALKKFVERRVSALPLVDsDGRLVDI 548
Cdd:cd04623   73 CTPDDTVEECMALMTERRIRHLPVVE-DGKLVGI 105

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

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 49.34 E-value: 3.95e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 510 NNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKtynDLDVSLRKANEH--RNewfegVQKC 587
Cdd:cd04623    2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALR---GASSLDTPVSEImtRD-----VVTC 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 220950704 588 NLDESLYTIMERIVRaevHR---LVVVDENRkVIGIISLSDI 626
Cdd:cd04623   74 TPDDTVEECMALMTE---RRirhLPVVEDGK-LVGIVSIGDV 111

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

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 45.67 E-value: 1.75e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 220950704  511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAE 560
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

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

Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 47.02 E-value: 2.36e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 438 VSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILThKRILRFlflyINELPKP--AYMQKslRELKIgtynnieTA 515
Cdd:cd04601    5 VTLSPDATVADVLELKAEYGISGVPVTEDG-GKLVGIVT-SRDIRF----ETDLSTPvsEVMTP--DERLV-------TA 69

                         90       100       110
                 ....*....|....*....|....*....|...
gi 220950704 516 DETTSIITALKKFVERRVSALPLVDSDGRLVDI 548
Cdd:cd04601   70 PEGITLEEAKEILHKHKIEKLPIVDDNGELVGL 102

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

Pssm-ID: 341385 [Multi-domain] Cd Length: 119 Bit Score: 46.80 E-value: 2.79e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 513 ETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDL----DVSLRKanehrnewfegVQKCN 588
Cdd:cd04613    6 TVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEELWDLvvvkDLATTD-----------VITVT 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 220950704 589 LDESLYTIMERIVRAEVHRLVVVDEN--RKVIGIISLSDIL 627
Cdd:cd04613   75 PDDDLYTALLKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVI 115

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

Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 47.23 E-value: 3.47e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 510 NNIETADETTSIITALKKFVERRVSALPLVDS-DGRLVDIYAKFDVIN--------LAAEKTYNDldvSLRKA-NEHRNE 579
Cdd:cd17779    8 KDVITIPPTTTIIGAIKTMTEKGFRRLPVADAgTKRLEGIVTSMDIVDflgggskyNLVEKKHNG---NLLAAiNEPVRE 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 220950704 580 WFEG-----VQKCNLDESLYTIMERIVRAevhrLVVVDENRKVIGIISLSDILLYL 630
Cdd:cd17779   85 IMTRdvisvKENASIDDAIELMLEKNVGG----LPIVDKDGKVIGIVTERDFLKFL 136

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

Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 45.49 E-value: 1.01e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDV-INLAAEKTYNDLDVSlrkanehrNEWFEGVQKCNL 589
Cdd:cd17784    3 NVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLgHNLILDKYELGTTVE--------EVMVKDVATVHP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 220950704 590 DESLYTIMERIVRAE-----VHRLVVVDENrKVIGIISLSDILLYL 630
Cdd:cd17784   75 DETLLEAIKKMDSNApdeeiINQLPVVDDG-KLVGIISDGDIIRAI 119

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 45.29 E-value: 1.42e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 387 EKQQFVGMLTITDFIKilqmyyKSPNASMEQleehkldtwrsvlhnqVM--PLVSIGPDASLYDAIKILIHSRIHRLPVI 464
Cdd:COG4109   56 ENGRLVGIVTSKDILG------KDDDTPIED----------------VMtkNPITVTPDTSLASAAHKMIWEGIELLPVV 113

                         90       100
                 ....*....|....*....|
gi 220950704 465 DPaTGNVLYILTHKRILRFL 484
Cdd:COG4109  114 DD-DGRLLGIISRQDVLKAL 132

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

Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 44.25 E-value: 1.90e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 532 RVSALPLVDsDGRLVDIYAKFDVinlaaektyndldvslRKANEHR---NEWFEGVQKCNLDESLYTIMERIVRAEVHRL 608
Cdd:cd04599   25 RIGGLPVVE-NGKLVGIITSRDV----------------RRAHPNRlvaDAMSRNVVTISPEASLWEAKELMEEHGIERL 87

                         90       100
                 ....*....|....*....|.
gi 220950704 609 VVVDENRKViGIISLSDILLY 629
Cdd:cd04599   88 VVVEEGRLV-GIITKSTLYLE 107

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

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 42.50 E-value: 1.95e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 220950704   357 LVVFDTQLLVKKAFYALVYNGVRAAPLWDsEKQQFVGMLTITDFIKILQ 405
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVD-EEGRLVGIVTRRDIIKALA 49

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

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 44.48 E-value: 2.46e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNEwfegvqkcnLDESL 593
Cdd:cd04600    7 TVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRD---------RPETV 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 220950704 594 YTIMERIVR-----------------AEVHRLVVVDENRKVIGIISLSDIL--LY 629
Cdd:cd04600   78 GDIMTRPVVtvrpdtpiaelvplfsdGGLHHIPVVDADGRLVGIVTQSDLIaaLY 132

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

Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 44.73 E-value: 2.75e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 376 NGVRAAPLWDsEKQQFVGMLTITDFIK------------ILQMYYKSPNASMEQLeeHKLdTWRSVlhNQVM--PLVSIG 441
Cdd:cd04586   24 HRISGLPVVD-DDGKLVGIVSEGDLLRreepgteprrvwWLDALLESPERLAEEY--VKA-HGRTV--GDVMtrPVVTVS 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 220950704 442 PDASLYDAIKILIHSRIHRLPVIDPatGNVLYILTHKRILR 482
Cdd:cd04586   98 PDTPLEEAARLMERHRIKRLPVVDD--GKLVGIVSRADLLR 136

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

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 44.24 E-value: 2.86e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 354 SAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKqqFVGMLTITDFIKilqmyYKSPNASMEQLEEHKLDTWRSVLHNQ 433
Cdd:cd17778    7 TTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK--LVGIVTAMDIVK-----YFGSHEAKKRLTTGDIDEAYSTPVEE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 220950704 434 VM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFL 484
Cdd:cd17778   80 IMskEVVTIEPDADIAEAARLMIKKNVGSLLVVDDE-GELKGIITERDVLIAL 131

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

Pssm-ID: 341394 [Multi-domain] Cd Length: 130 Bit Score: 43.76 E-value: 4.65e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 354 SAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKqqFVGMLTITDFIKIL---QMYYKSPNASMEQLEEHKLdtwRSVL 430
Cdd:cd04631    7 TKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGK--LVGIVTSTDIMRYLgsgEAFEKLKTGNIHEVLNVPI---SSIM 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 220950704 431 HNQVmplVSIGPDASLYDAIKILIHSRIHRLPVIDpaTGNVLYILTHKRILR 482
Cdd:cd04631   82 KRDI---ITTTPDTDLGEAAELMLEKNIGALPVVD--DGKLVGIITERDILR 128

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 43.32 E-value: 6.76e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 220950704 584 VQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLRpsgegvGGSESSLRASD 650
Cdd:COG0517   11 VVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAE------GKDLLDTPVSE 71

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 42.89 E-value: 8.63e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 220950704 582 EGVQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLR 633
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAE 58

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

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 41.93 E-value: 2.38e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDsDGRLVDIYAKFDVI-NLAAEKTYNDLDV-SLRKANEHRNEWF--EGVQK 586
Cdd:cd17778    9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVkYFGSHEAKKRLTTgDIDEAYSTPVEEImsKEVVT 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 220950704 587 CNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYL 630
Cdd:cd17778   88 IEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131

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

Pssm-ID: 341412 [Multi-domain] Cd Length: 115 Bit Score: 41.24 E-value: 2.39e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDsDGRLVDIYAKFDVinLAAEKTYNDL--DVSLRKANEHRNEWFEgvqkcnLDE 591
Cdd:cd17776    7 TVDADASLEDAAERMLRNRVGSVVVTD-DGTPAGILTETDA--LHAGYATDDPfsEIPVRAVASRPLVTIS------PTA 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 220950704 592 SLYTIMERIVRAEVHRLVVVDENrKVIGIISLSDIL 627
Cdd:cd17776   78 TLREAAERMVDEGVKKLPVVDGL-DLVGILTATDII 112

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

Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 41.33 E-value: 2.47e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDsDGRLVDIYAKFDVinlaaektyndldvslRKANEHR--NEWFEGVQKCNL-- 589
Cdd:cd04595    6 TVSPDTTIEEARKIMLRYGHTGLPVVE-DGKLVGIISRRDV----------------DKAKHHGlgHAPVKGYMSTNVit 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 220950704 590 ---DESLYTIMERIVRAEVHRLVVVDENrKVIGIISLSDILLY 629
Cdd:cd04595   69 idpDTSLEEAQELMVEHDIGRLPVVEEG-KLVGIVTRSDVLRY 110

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

Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 40.99 E-value: 3.67e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 220950704 590 DESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYL 630
Cdd:cd17775   77 DDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117

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

Pssm-ID: 341418 [Multi-domain] Cd Length: 118 Bit Score: 40.69 E-value: 4.06e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRI-LRFLFLYINelPKpaymQKSLreLKIGTyNNIET 514
Cdd:cd17782    3 PPPLVSPKTTVREAARLMKENRTTAVLVMDNS-GKVIGIFTSKDVvLRVLAAGLD--PA----TTSV--VRVMT-PNPET 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 220950704 515 ADETTSIITALKKFVERRVSALPLVDSDGRLVDIyakFDVINL 557
Cdd:cd17782   73 APPSTTILDALHKMHEGKFLNLPVVDDEGEIVGL---VDVLQL 112

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

Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 40.02 E-value: 6.71e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDpaTGNVLYILTHKRILRFlflYINELPKPAyMQKslrelkigtynNIETA 515
Cdd:cd04599    4 NPITISPLDSVARAAALMERQRIGGLPVVE--NGKLVGIITSRDVRRA---HPNRLVADA-MSR-----------NVVTI 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 220950704 516 DETTSIITALKKFVERRVSALPLVDsDGRLVDIYAKFDVI 555
Cdd:cd04599   67 SPEASLWEAKELMEEHGIERLVVVE-EGRLVGIITKSTLY 105

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

Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 39.61 E-value: 8.19e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 438 VSIGPDASLYDAIKILIHSRIHRLPVIDpaTGNVLYILTHKRILRFLFlyiNELPKPAyMQKslrelkigtynNIETADE 517
Cdd:cd04610    6 ITVSPDDTVKDVIKLIKETGHDGFPVVD--DGKVVGYVTAKDLLGKDD---DEKVSEI-MSR-----------DTVVADP 68

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 220950704 518 TTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVI 555
Cdd:cd04610   69 DMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106

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

Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 39.81 E-value: 8.33e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 438 VSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRIlrflflyiNELPKPAymqKSLRELkigTYNNIETADE 517
Cdd:cd04583    5 VTITPERTLAQAIEIMREKRVDSLLVVDKD-NVLLGIVDIEDI--------NRNYRKA---KKVGEI---MERDVFTVKE 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 220950704 518 TTSIITALKKFVERRVSALPLVDSDGRLVDI 548
Cdd:cd04583   70 DSLLRDTVDRILKRGLKYVPVVDEQGRLVGL 100

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

Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 39.81 E-value: 8.57e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDSDGRLVDiYAKFDVINLAAEKTYNDLDVSLRKanehrnewfegVQKCNLDESL 593
Cdd:cd04583    6 TITPERTLAQAIEIMREKRVDSLLVVDKDNVLLG-IVDIEDINRNYRKAKKVGEIMERD-----------VFTVKEDSLL 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 220950704 594 YTIMERIVRAEVHRLVVVDENRKVIGII---SLSDIL 627
Cdd:cd04583   74 RDTVDRILKRGLKYVPVVDEQGRLVGLVtraSLVDIV 110

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

Pssm-ID: 341363 [Multi-domain] Cd Length: 114 Bit Score: 39.33 E-value: 1.05e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 220950704 433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDpaTGNVLYILTHKRILRF 483
Cdd:cd04587   64 EIMtpPPVTIDADALVFEALLLMLERNIHHLPVVD--DGRVVGVVTATDLMRL 114

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

Pssm-ID: 341385 [Multi-domain] Cd Length: 119 Bit Score: 39.48 E-value: 1.28e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 386 SEKQQFVGMLTITDFIKILqmyykspnasmeqLEEHKLDTwrsVLHNQVM--PLVSIGPDASLYDAIKILIHSRIHRLPV 463
Cdd:cd04613   33 DEQGRLTGILSIQDVRGVL-------------FEEELWDL---VVVKDLAttDVITVTPDDDLYTALLKFTSTNLDQLPV 96

                         90       100
                 ....*....|....*....|.
gi 220950704 464 IDPA-TGNVLYILTHKRILRF 483
Cdd:cd04613   97 VDDDdPGKVLGMLSRRDVIAA 117

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

Pssm-ID: 341398 [Multi-domain] Cd Length: 133 Bit Score: 39.47 E-value: 1.39e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 220950704 597 MERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLRPSGEGvGGSESSLRASD 650
Cdd:cd04640   20 LEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPLKIVQER-GIPREELLVAD 72

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

Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 39.06 E-value: 1.56e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 220950704 433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFL 484
Cdd:cd17775   65 DIMsaDLITAREDDGLFEALERMREKGVRRLPVVDDD-GELVGIVTLDDILELL 117

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

Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 38.68 E-value: 2.17e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLA 558
Cdd:cd17775   73 TAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117

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

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 38.67 E-value: 2.25e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPaTGNVLYILTHKRILRFLFlyinelpkpayMQKSLRELKIGT--YNNIE 513
Cdd:cd04608   11 APVTVLPDDTLGEAIEIMREYGVDQLPVVDE-DGRVVGMVTEGNLLSSLL-----------AGRAQPSDPVSKamYKQFK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 220950704 514 TADETTSiITALKKFVERRVSALpLVDSDGRLVDIYAKFDVIN 556
Cdd:cd04608   79 QVDLDTP-LGALSRILERDHFAL-VVDGQGKVLGIVTRIDLLN 119

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

Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 38.25 E-value: 2.65e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 436 PLVSIGPDASLYDAIKILIHSRIHRLPVIDPatGNVLYILTHKRILRFLFLYINELPKPAYMQKslrelkigtynNIETA 515
Cdd:cd04595    3 PVKTVSPDTTIEEARKIMLRYGHTGLPVVED--GKLVGIISRRDVDKAKHHGLGHAPVKGYMST-----------NVITI 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 220950704 516 DETTSIITALKKFVERRVSALPLVDsDGRLVDIYAKFDVIN 556
Cdd:cd04595   70 DPDTSLEEAQELMVEHDIGRLPVVE-EGKLVGIVTRSDVLR 109

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

Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 38.86 E-value: 2.72e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 503 ELKIGTYNNIETADETTSIITALKKFVERRVSALPLVDSD--------GRLVDIYAKFDVINLAAEKTYNDLDVSLRKAN 574
Cdd:cd17777    3 ELMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDENklegilsaRDLVSYLGGGCLFKIVESRHQGDLYSALNREV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 220950704 575 ehrnewFEGVQKCN-----LDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYL 630
Cdd:cd17777   83 ------VETIMTPNpvyvyEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL 137

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

Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 38.09 E-value: 2.98e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 515 ADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVinlaAEKTYNDLDVSLRKanehrnewfeGVQKCNLDESLY 594
Cdd:cd04594    7 VSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDI----ENKSPGKVGKYVVR----------GSPYVTPTSSLE 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 220950704 595 TIMERIVRAEVhRLVVVDENRKVIGIISLSDIL 627
Cdd:cd04594   73 EAWEIMMRNKS-RWVAVVEKGKFLGIITLDDLL 104

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

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 38.31 E-value: 3.72e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 377 GVRAAPLWDSEkQQFVGMLTITDFIKILQMyykSPNASMEQLEEHKL--DTWRSVLHNQVM--PLVSIGPDASLYDAIKI 452
Cdd:cd04600   25 RIKALPVVDRA-RRLVGIVTLADLLKHADL---DPPRGLRGRLRRTLglRRDRPETVGDIMtrPVVTVRPDTPIAELVPL 100

                         90       100
                 ....*....|....*....|....
gi 220950704 453 LIHSRIHRLPVIDpATGNVLYILT 476
Cdd:cd04600  101 FSDGGLHHIPVVD-ADGRLVGIVT 123

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

Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 37.55 E-value: 4.48e-03

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 220950704 590 DESLYTIMERIVRAEVHRLVVVDENRkVIGIISLSDIL 627
Cdd:cd04801   75 DADAMEALKLMSQNNIGRLPVVEDGE-LVGIISRTDLM 111

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

Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 37.98 E-value: 5.02e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 366 VKKAFYALVYNGVRAAPLWDSEKQQFVGMLTITDFI---------KILQMYYK-----SPNASMeqleehkldtwRSVLH 431
Cdd:cd17779   19 IIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVdflgggskyNLVEKKHNgnllaAINEPV-----------REIMT 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 220950704 432 NQVmplVSIGPDASLYDAIKILIHSRIHRLPVIDPAtGNVLYILTHKRILRFL 484
Cdd:cd17779   88 RDV---ISVKENASIDDAIELMLEKNVGGLPIVDKD-GKVIGIVTERDFLKFL 136

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.

Pssm-ID: 341372 [Multi-domain] Cd Length: 106 Bit Score: 37.33 E-value: 5.12e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 438 VSIGPDASLYDAIKILIHSRIHRLPVIDPaTGNVLYILTHKRILRFLfLYInelpkpayMQKSlrelKIGTYNNIETADE 517
Cdd:cd04597    8 EPLSPETSIKDAWNLMDENNLKTLPVTDD-NGKLIGLLSISDIARTV-DYI--------MTKD----NLIVFKEDDYLDE 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 220950704 518 TTSIITalkkfvERRVSALPLVDSDGRLVDIYAKFDVIN 556
Cdd:cd04597   74 VKEIML------NTNFRNYPVVDENNKFLGTISRKHLIN 106

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

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 37.51 E-value: 5.68e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 514 TADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNdLDVSLRKANEHRnewfegVQKCNLDES- 592
Cdd:cd04608   14 TVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQ-PSDPVSKAMYKQ------FKQVDLDTPl 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 220950704 593 --LYTIMERivraeVHRLVVVDENRKVIGIISLSDILLY 629
Cdd:cd04608   87 gaLSRILER-----DHFALVVDGQGKVLGIVTRIDLLNY 120

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.

Pssm-ID: 341372 [Multi-domain] Cd Length: 106 Bit Score: 36.94 E-value: 6.59e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 509 YNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAkfdVINLAAEKTYndldvSLRKanehrnewfEGVQKCN 588
Cdd:cd04597    4 YDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLS---ISDIARTVDY-----IMTK---------DNLIVFK 66

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 220950704 589 LDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDIL 627
Cdd:cd04597   67 EDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLI 105

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

Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 37.52 E-value: 7.75e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 220950704 433 QVM--PLVSIGPDASLYDAIKILIHSRIHRLPVIDPaTGNVLYILTHKRILR 482
Cdd:cd17774   73 TVMssPLFSLRPDDSLWTAHQLMQQRRIRRLVVVGE-QGELLGIVTQTSLLQ 123

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

Pssm-ID: 341422 [Multi-domain] Cd Length: 114 Bit Score: 36.74 E-value: 8.72e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 511 NIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRnewfegVQKCNLD 590
Cdd:cd17786    3 NFKTINWNATVFDAVKIMNENHLYGLVVKDDDGNYVGLISERSIIKRFIPRNVKPDEVPVKLVMRKP------IPKVKSD 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 220950704 591 ESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDI 626
Cdd:cd17786   77 YDVKDVAAFLSENGLERCAVVDDNGRVVGIVTITDL 112

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

Pssm-ID: 341385 [Multi-domain] Cd Length: 119 Bit Score: 36.79 E-value: 9.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 220950704 451 KILIHSRIHRLPVIDpATGNVLYILTHKRILRFLFlyinelpkpaymQKSLRELKIgtYNNIETADETT-----SIITAL 525
Cdd:cd04613   19 EFIAGTRQHYFPVVD-EQGRLTGILSIQDVRGVLF------------EEELWDLVV--VKDLATTDVITvtpddDLYTAL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 220950704 526 KKFVERRVSALPLVDSD--GRLVDIYAKFDVInlaaeKTYN 564
Cdd:cd04613   84 LKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVI-----AAYN 119