NCBI Conserved Domain Search

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 87.23 E-value: 1.09e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   2 SVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEFRWNasrsgdqPRLTEEEQEEARR 81
Cdd:COG3448    1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLP-------DRLDELEERLLDL 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233620  82 LrmvifeemgkvpveVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKLISDR 153
Cdd:COG3448   74 P--------------VEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDgRLVGIVTRTDLLRALARL 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: 83.25 E-value: 4.49e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   9 MTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEfrwnasrsgdqpRLTEEEQEEARRLRMVIFE 88
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLR------------REEPGTEPRRVWWLDALLE 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233620  89 EMGKVPVE--------VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd04586   69 SPERLAEEyvkahgrtVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136

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: 1.27e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   7 EIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDItefrwnasrsgdqprlteeeqeearrLRMVI 86
Cdd:COG2905    3 DIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDL--------------------------RRRVL 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233620  87 FEEMGKVPVEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKLISD 152
Cdd:COG2905   57 AEGLDPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSE 122

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 72.22 E-value: 4.26e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   1 MSVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDnGDIIGIATLKDITEFRWNASRSGDQPrlteeeqeear 80
Cdd:COG2524   84 LKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLLDAP----------- 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233620  81 rlrmvifeemgkvpveVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDMLKLI 150
Cdd:COG2524  152 ----------------VSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 69.51 E-value: 6.93e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   3 VLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITefRWNASRSGDQPRLTeeeqeearrl 82
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLR--RALAAEGKDLLDTP---------- 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233620  83 rmvifeemgkvpveVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFV-TRDSKITGIITTYDMLKLISDR 153
Cdd:COG0517   69 --------------VSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLEP 126

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

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 62.26 E-value: 2.90e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  16 VPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEFRWNASRSGDQPrlteeeqeearrlrmvifeemgkvpv 95
Cdd:cd02205    7 VDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTP-------------------------- 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504233620  96 eVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLK 148
Cdd:cd02205   61 -VAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDgKLVGIVTRRDILR 113

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: 61.05 E-value: 1.01e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   7 EIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDdNGDIIGIATLKDITEfrwnasrsgdqprlTEEEQEEARRlrmvi 86
Cdd:cd04801    1 DIMTPEVVTVTPEMTVSELLDRMFEEKHLGYPVVE-NGRLVGIVTLEDIRK--------------VPEVEREATR----- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233620  87 feemgkvpveVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd04801   61 ----------VRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRTDLMR 112

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: 56.96 E-value: 5.48e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  29 LTDNEITGSPVTDDNGDIIGIATLKDITEFrwnASRSGDQPRLTEEEQEEARRLRMVifeemgkvpveVRDIMTPIVLSV 108
Cdd:cd04632   20 LREHGISRLPVVDDNGKLVGIVTTYDIVDF---VVRPGTKTRGGDRGGEKERMLDLP-----------VYDIMSSPVVTV 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 504233620 109 DEDTPVRDIANIMMREHLHRIFVTRDSKIT-GIITTYDMLK 148
Cdd:cd04632   86 TRDATVADAVERMLENDISGLVVTPDDNMViGILTKTDVLR 126

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: 56.29 E-value: 5.59e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  29 LTDNEITGSPVTDDNGDIIGIATLKDITEFRWNASRSGDQPRLteeeqeearrlrmvifeemgkvpveVRDIMTPIVLSV 108
Cdd:cd04629   21 LLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPGGT-------------------------VADYMSTEVLTV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 504233620 109 DEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd04629   76 SPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVLR 115

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: 54.42 E-value: 2.82e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  13 IKAVPHNWTMDRLARFLTDNEITGSPVTDDnGDIIGIATLKDItefrwnasrsgdqprlteeeqEEARRlrmvifEEMGK 92
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDV---------------------DKAKH------HGLGH 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504233620  93 VPVevRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd04595   56 APV--KGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVLR 109

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: 53.19 E-value: 1.34e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   7 EIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDnGDIIGIATLKDITEfrwnASRSgdqpRLTEEEQEEARRLrmvi 86
Cdd:cd04584    4 DIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDD-GKLVGIVTDRDLLR----ASPS----KATSLSIYELNYL---- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233620  87 feeMGKVPVEvrDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKLI 150
Cdd:cd04584   71 ---LSKIPVK--DIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAF 129

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: 51.45 E-value: 1.35e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 504233620   97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFV-TRDSKITGIITTYDMLKLISD 152
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVvDEDGKLVGIVTLKDLLRALLG 57

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: 4.89e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  19 NWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEFRWNASRSGDQPRLTEEEQ--EEARRLRMVIFEEMGKVpve 96
Cdd:cd17789   11 NTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADStwKTFNEVQKLLSKTNGKV--- 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRI-FVTRDSKITGIITTYDMLK 148
Cdd:cd17789   88 VGDVMTPSPLVVREKTNLEDAARILLETKFRRLpVVDSDGKLVGIITRGNVVR 140

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 52.96 E-value: 4.96e-09

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233620  79 ARRLRMVIFEEMGKVPVEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKLISD 152
Cdd:COG2524   70 AAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE 143

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: 6.81e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  26 ARFLTDNEITGSPVTDDnGDIIGIATLKDITEfrwnasrsgdqprlteeeqeearrlrmVIFEemGKVPVEVRDIMTPIV 105
Cdd:cd04588   17 AKLLSENNIHGAPVVDD-GKLVGIVTLTDIAK---------------------------ALAE--GKENAKVKDIMTKDV 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504233620 106 LSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKL 149
Cdd:cd04588   67 ITIDKDEKIYDAIRLMNKHNIGRLIVVDDNgKPVGIITRTDILKV 111

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 51.40 E-value: 7.19e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDMLKLISDRDLTQR 158
Cdd:COG3448    4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLPDRLDEL 66

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: 49.92 E-value: 2.11e-08

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKLISDRDL 155
Cdd:cd04631    2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMRYLGSGEA 60

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: 49.34 E-value: 3.76e-08

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd04584    2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLR 53

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: 49.15 E-value: 3.96e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   7 EIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDnGDIIGIATLKDITEFrwnasrsgdqprLTEEEQEEarrlRMVI 86
Cdd:cd04631    4 DYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSD-GKLVGIVTSTDIMRY------------LGSGEAFE----KLKT 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233620  87 --FEEMGKVPVevRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKLI 150
Cdd:cd04631   67 gnIHEVLNVPI--SSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILRAI 130

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 47.52 E-value: 1.40e-07

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKLISDRDL 155
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDgRLVGIITDRDLRRRVLAEGL 60

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 46.01 E-value: 5.27e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKLISDRD 154
Cdd:COG0517    3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDgKLVGIVTDRDLRRALAAEG 61

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: 43.74 E-value: 1.01e-06

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504233620    7 EIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEF 58
Cdd:pfam00571   3 DIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54

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: 45.25 E-value: 1.14e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  38 PVTDDNGDIIGIATLKDITEFRWNASRSGDQPRLTEEEQEEARRlrmvifeemgkvPVEVRDIMTPIVLSVDEDTPVRDI 117
Cdd:cd04600   30 PVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRDR------------PETVGDIMTRPVVTVRPDTPIAEL 97

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504233620 118 ANIMMREHLHRIFVTRDS-KITGIITTYDML 147
Cdd:cd04600   98 VPLFSDGGLHHIPVVDADgRLVGIVTQSDLI 128

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: 44.72 E-value: 1.35e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKL 149
Cdd:cd04587   62 VSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDDGRVVGVVTATDLMRL 114

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: 44.63 E-value: 2.17e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   7 EIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDnGDIIGIATLKDITEfrwNASRSGDQPRLTEEEQEEArrlrmvi 86
Cdd:cd17778    4 EFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSG-GKLVGIVTAMDIVK---YFGSHEAKKRLTTGDIDEA------- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233620  87 feemgkVPVEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDML 147
Cdd:cd17778   73 ------YSTPVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVdDEGELKGIITERDVL 128

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 44.52 E-value: 2.52e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   1 MSVLAHEIMT-PTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEFrwnasrsgdqprlteeeqeea 79
Cdd:COG4109   14 EILLVEDIMTlEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK--------------------- 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  80 rrlrmvifeeMGKVPVEvrDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDMLK 148
Cdd:COG4109   73 ----------DDDTPIE--DVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVdDDGRLLGIISRQDVLK 130

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. 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: 341403 [Multi-domain] Cd Length: 116 Bit Score: 43.37 E-value: 4.06e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233620  99 DIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKL-ISDRDLTQR 158
Cdd:cd09833    1 RIVSTSLLTCSPDTPLADAAARMAERRCSSILIVENGEIVGIWTERDALKLdFSDPDAFRR 61

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. 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: 341366 [Multi-domain] Cd Length: 119 Bit Score: 43.64 E-value: 4.26e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233620  97 VRDIMTPI--VLSVDEDTPVRDIANIMMREHLHRIFVTRDSK--ITGIITTYDMLKLISDRDLT 156
Cdd:cd04590    2 VREVMTPRtdVVALDADATLEELLELILESGYSRFPVYEGDLdnIIGVLHVKDLLAALLEGREK 65

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and 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 eukaryotes and 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: 341367 [Multi-domain] Cd Length: 114 Bit Score: 43.28 E-value: 4.71e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   4 LAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGD--IIGIATLKDItefrwnasrsgdqprlteeeqeearr 81
Cdd:cd04591    1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTESqtLVGFILRSQL-------------------------- 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233620  82 lrMVIFEEMgkvpveVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd04591   55 --ILLLEAD------LRPIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLR 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: 43.28 E-value: 4.82e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   9 MTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDItefrwnasrsgdqprlteeeqeearrLRMVIFE 88
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDI--------------------------VRAVAEG 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233620  89 EMGKVPVEvrDIMTPIVLSVDEDTPVRDIAnIMMREH--LHRIFVTRDSKITGIITTYDMLKLIS 151
Cdd:cd09836   55 IDLDTPVE--EIMTKNLVTVSPDESIYEAA-ELMREHniRHLPVVDGGGKLVGVISIRDLARELS 116

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: 42.94 E-value: 6.17e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  14 KAVPHNWTMDRLARFLTDNEITGSPVTDDN-GDIIGIATLKDItefrwnasrsgdqprlteeeqEEArrlrmvIFEEMGK 92
Cdd:cd17772    5 ISVEPDTTIAEAAELMTRYNINALPVVDGGtGRLVGIITRQVA---------------------EKA------IYHGLGD 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504233620  93 VPVevRDIMTPIVLSVDEDTPVRDIANIMMrEHLHRIF-VTRDSKITGIITTYDMLKL 149
Cdd:cd17772   58 LPV--SEYMTTEFATVTPDAPLSEIQEIIV-EQRQRLVpVVEDGRLVGVITRTDLLNL 112

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: 341393 [Multi-domain] Cd Length: 120 Bit Score: 42.58 E-value: 9.83e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504233620  95 VEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDML 147
Cdd:cd04630   66 VNVYEIMTKPAISVSPDLDIKYAARLMARFNLKRAPVIENNELIGIVSMTDLV 118

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 42.55 E-value: 1.30e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504233620   1 MSVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDI 55
Cdd:COG0517   65 LDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDL 119

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: 40.19 E-value: 1.96e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 504233620   105 VLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDMLKLI 150
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLVGIVTRRDIIKAL 48

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 43.28 E-value: 2.21e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDMLKLISDRD 154
Cdd:PRK14869  70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVdEEGKLLGLVSLSDLARAYMDIL 128

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];

Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 43.18 E-value: 2.38e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  64 RSGDQPRLTEEE---------------QEEARRLRMVIfeEMGKVPVevRDIMTPI--VLSVDEDTPVRDIANIMMREHL 126
Cdd:COG1253  172 PAEEEPAVTEEElralveeseesgvieEEEREMIENVF--EFGDRTV--REVMTPRtdVVALDLDDTLEEALELILESGH 247

                         90       100       110
                 ....*....|....*....|....*....|
gi 504233620 127 HRIFVTRDSK--ITGIITTYDMLKLISDRD 154
Cdd:COG1253  248 SRIPVYEGDLddIVGVVHVKDLLRALLEGE 277

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: 40.87 E-value: 3.30e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   9 MTPTIKAVPHNWTMDRLARFLTDNEItGS-PVTDdNGDIIGIATLKDITefrwnasrsgdqprlteeeqeearrLRmVIF 87
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDI-GAlPVCE-GDRLVGMVTDRDIV-------------------------VR-AVA 52

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  88 EEMGKVPVEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDM 146
Cdd:cd04622   53 EGKDPNTTTVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVdDDGRLVGIVSLGDL 112

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: 41.06 E-value: 3.94e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   7 EIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTD-DNGDIIGIATLKDITEFRWNASRSgdqpRLTEEEQEeaRRLRMV 85
Cdd:cd17779    4 AIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADaGTKRLEGIVTSMDIVDFLGGGSKY----NLVEKKHN--GNLLAA 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233620  86 IFEEmgkvpveVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRI-FVTRDSKITGIITTYDMLKLI 150
Cdd:cd17779   78 INEP-------VREIMTRDVISVKENASIDDAIELMLEKNVGGLpIVDKDGKVIGIVTERDFLKFL 136

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: 40.68 E-value: 4.46e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHL-HRIFVTRDSKITGIITTYDMLKLIS 151
Cdd:cd04605    2 VEDIMSKDVATIREDISIEEAAKIMIDKNVtHLPVVSEDGKLIGIVTSWDISKAVA 57

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. 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: 341366 [Multi-domain] Cd Length: 119 Bit Score: 40.56 E-value: 5.44e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   5 AHEIMTPT--IKAVPHNWTMDRLARFLTDNEITGSPVTDDNGD-IIGIATLKDIteFRWNASrsgdqprlteeeqeearr 81
Cdd:cd04590    2 VREVMTPRtdVVALDADATLEELLELILESGYSRFPVYEGDLDnIIGVLHVKDL--LAALLE------------------ 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233620  82 lrmvifeemGKVPVEVRDIMTPiVLSVDEDTPVRDIANIMMREHLHRIFVTRD-SKITGIITTYDML 147
Cdd:cd04590   62 ---------GREKLDLRALLRP-PLFVPETTPLDDLLEEFRKERSHMAIVVDEyGGTAGIVTLEDIL 118

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: 40.31 E-value: 5.67e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504233620   2 SVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDI 55
Cdd:cd02205   58 DTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). 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: 341386 [Multi-domain] Cd Length: 150 Bit Score: 40.73 E-value: 8.15e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  37 SPVTDDNGDIIGIATLKDITefrwNASRSGDQPRLTEE---EQEEA---RRLRMVIFEEMG----KVPVE-VRDIMTPIV 105
Cdd:cd04614   30 APVLDSEGKLVGIVTERDLI----DVSRIVESEEESGMsiaDDEDEwswEGIRDVMSLYYPtsnvELPDKpVKDVMTKDV 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 504233620 106 LSVDEDTPVRDIANIMMREHLHRI-FVTRDSKITGIITTYDMLK 148
Cdd:cd04614  106 VTAFPSSTVSEAAKKMIRNDIEQLpVVSGEGDLAGMLRDVDLLK 149

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: 39.72 E-value: 9.87e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233620 100 IMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITtydmlklisDRDLTQRCA 160
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVT---------DRDLRNRVV 52

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: 39.42 E-value: 1.20e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  39 VTDDNGDIIGIATLKDITEFRWNASRsgdqprlteeeqeearrlrmvifeemgkvpveVRDIMTPIVLSVDEDTPVRDIA 118
Cdd:cd04583   30 VVDKDNVLLGIVDIEDINRNYRKAKK--------------------------------VGEIMERDVFTVKEDSLLRDTV 77

                         90       100
                 ....*....|....*....|....*
gi 504233620 119 NIMMREHLHRIFVT-RDSKITGIIT 142
Cdd:cd04583   78 DRILKRGLKYVPVVdEQGRLVGLVT 102

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: 39.32 E-value: 1.51e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  21 TMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDItefrwnasrsgdqprlteeeqeeARRLRmvifeEMGKVPVE--VR 98
Cdd:cd04623   12 TVAEALRLLAEKNIGALVVVDDGGRLVGILSERDY-----------------------VRKLA-----LRGASSLDtpVS 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504233620  99 DIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd04623   64 EIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVEDGKLVGIVSIGDVVK 113

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 40.82 E-value: 1.55e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   8 IMTPTIKAVPHNWT----MDRLARFLTDNEITGS-PVTDDNGDIIGIATLKDItefrwnasrsgdqprLTEEEQeearrl 82
Cdd:COG2239  134 LMTTEFVAVREDWTvgeaLRYLRRQAEDPETIYYiYVVDDDGRLVGVVSLRDL---------------LLADPD------ 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233620  83 rmvifeemgkvpVEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVT-RDSKITGIITTYDMLKLI 150
Cdd:COG2239  193 ------------TKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVdEEGRLVGIITVDDVVDVI 249

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: 38.76 E-value: 1.91e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504233620 105 VLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKLISDRDLTQ 157
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDgKLVGIVTERDILRALVEGGLAL 57

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: 38.55 E-value: 2.53e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504233620 101 MTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITtydmlklisDRDLTQRC 159
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVT---------DRDIVVRA 50

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: 37.52 E-value: 6.69e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504233620   2 SVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEF 58
Cdd:cd17775   60 DVTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILEL 116

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: 37.52 E-value: 7.10e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504233620  95 VEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKLI 150
Cdd:cd17775   61 VTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDgELVGIVTLDDILELL 117

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: 36.92 E-value: 9.29e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504233620 101 MTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLKLISDRDL 155
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLGKDDDEKV 55

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: 36.94 E-value: 1.20e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504233620  96 EVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRI-FVTRDSKITGIITTYDMLKLI 150
Cdd:cd17777   82 VVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLpVVDRDGRPVGIVTERDLVLYL 137

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: 36.83 E-value: 1.23e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   8 IMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITEfrwnaSRSGDQPRLTEeeqeearrlrmvif 87
Cdd:cd04605    5 IMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISK-----AVALKKDSLEE-------------- 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233620  88 eemgkvpvevrdIMTPIVLSVDEDTPVRDIANIMmreHLHRI----FVTRDSKITGIITTYDMLKL 149
Cdd:cd04605   66 ------------IMTRNVITARPDEPIELAARKM---EKHNIsalpVVDDDRRVIGIITSDDISRL 116

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: 36.61 E-value: 1.27e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504233620 101 MTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDML 147
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDAL 47

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: 36.35 E-value: 1.49e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504233620 101 MTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKLISDR 153
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDgKPVGIVTERDIVRAVAEG 54

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; 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: 341396 [Multi-domain] Cd Length: 109 Bit Score: 36.17 E-value: 1.52e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 504233620 100 IMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDM 146
Cdd:cd04638   60 LMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVADL 106

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: 341421 [Multi-domain] Cd Length: 136 Bit Score: 36.48 E-value: 1.72e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233620  96 EVRDIMTPIVLSVDEDTPVRDIANIMMREHLHR-IFVTR-DSKITGIITTYDMLKLISDRD 154
Cdd:cd17785    3 DIYNLITKKPSVVHENTSIRDVIDKMIEDPKTRsVYVVDdDEKLLGIITLMELLKYIGYRF 63

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain] Cd Length: 108 Bit Score: 35.14 E-value: 4.24e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620  23 DRLARFLTDNEITGS---PVTDDNGDIIGIATLKDItefrwnASRSGDQPrlteeeqeearrlrmvifeemgkvpveVRD 99
Cdd:cd04596   11 DTVRDYKQLSEETGHsrfPVVDEENRVVGIVTAKDV------IGKEDDTP---------------------------IEK 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504233620 100 IMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLK 148
Cdd:cd04596   58 VMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDENrKLLGVISRQDVLK 107

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: 35.07 E-value: 5.03e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   9 MTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDnGDIIGIATLKDITEfrwnASRSGDQPrlteeeqeearrlrmviFE 88
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERMLRNRVGSVVVTDD-GTPAGILTETDALH----AGYATDDP-----------------FS 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504233620  89 EmgkvpVEVRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDML 147
Cdd:cd17776   59 E-----IPVRAVASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLDLVGILTATDII 112

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 35.19 E-value: 5.44e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504233620   1 MSVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDnGDIIGIATLKDITEFR 59
Cdd:COG2905   63 LDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRAL 120

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: 34.82 E-value: 5.99e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504233620   2 SVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDIT 56
Cdd:cd17786   59 EVPVKLVMRKPIPKVKSDYDVKDVAAFLSENGLERCAVVDDNGRVVGIVTITDLS 113

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: 35.00 E-value: 6.82e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFVTRDSKITGIITTYDMLK 148
Cdd:cd17778    2 VKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVK 53

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) 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: 341381 [Multi-domain] Cd Length: 112 Bit Score: 34.34 E-value: 7.25e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504233620   1 MSVLAHEIMTPTIKAVPHNWTMDRLARFLTDNEITGSPVTDDNGDIIGIATLKDITE 57
Cdd:cd04607   56 LDAPVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLLA 112

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: 341393 [Multi-domain] Cd Length: 120 Bit Score: 34.50 E-value: 7.73e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233620  97 VRDIMTPIVLSVDEDTPVRDIANIMMREHLHRIFV--TRDSKITGIITTYDMLK--LISDRD 154
Cdd:cd04630    1 VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVekRHEHDAYGIVTYTDILKkvIAEDRD 62

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: 341373 [Multi-domain] Cd Length: 121 Bit Score: 34.33 E-value: 9.04e-03

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                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233620  91 GKVPVEVrdIMTPIVLSVDEDTPVRDIANIMM---REHLHRIF-VTRDSKITGIITTYDMLK 148
Cdd:cd04598   61 GKRPCSL--FMDKDPLVVDADTPIEELSQLATsrdQRYLYDGFiITENGRYLGVGTGRDLLR 120

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: 341397 [Multi-domain] Cd Length: 120 Bit Score: 34.47 E-value: 9.22e-03

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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233620   9 MTPTIKAVPHNWTMDRLArfltDNEITGS------PVTDDNGDIIGIATLKDitefrwnasrsgdqprlteeeqeearrL 82
Cdd:cd04639    3 MVTEFPIVDADLTLREFA----DDYLIGKkswrefLVTDEAGRLVGLITVDD---------------------------L 51

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233620  83 RMVIFEEMGKVPVevRDIMTPI--VLSVDEDTPVRDIANIMMREHLHRIFVTRDS-KITGIITTYDMLKLI 150
Cdd:cd04639   52 RAIPTSQWPDTPV--RELMKPLeeIPTVAADQSLLEVVKLLEEQQLPALAVVSENgTLVGLIEKEDIIELL 120