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Conserved domains on  [gi|2128734723|ref|WP_227931746|]
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CBS and ACT domain-containing protein [Granulicatella elegans]

Protein Classification

CBS and ACT domain-containing protein( domain architecture ID 10140009)

CBS and ACT domain-containing protein containing two tandem repeats of the cystathionine beta-synthase (CBS pair) at the N-terminus and an ACT domain at the C-terminus, may have a regulatory function; similar to Thermus thermophilus TTHA0829

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-132 4.67e-58

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: 179.15  E-value: 4.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQNSPSMATSLSVHELNYLLNKTTAKDIML 82
Cdd:cd04584     2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKATSLSIYELNYLLSKIPVKDIMT 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDAFI 132
Cdd:cd04584    82 KDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAFI 130
ACT super family cl09141
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 143-202 5.23e-05

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


The actual alignment was detected with superfamily member cd04879:

Pssm-ID: 471857  Cd Length: 71  Bit Score: 40.14  E-value: 5.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2128734723 143 RLFIeINEDKPGPLENISNVLRDHNVNVDTISVYhRDGKVQ---VVLHVDSENPDEVADFIAQ 202
Cdd:cd04879     1 RLLI-VHKDVPGVIGKVGTILGEHGINIAAMQVG-RKEKGGiayMVLDVDSPVPEEVLEELKA 61
 
Name Accession Description Interval E-value
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-132 4.67e-58

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: 179.15  E-value: 4.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQNSPSMATSLSVHELNYLLNKTTAKDIML 82
Cdd:cd04584     2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKATSLSIYELNYLLSKIPVKDIMT 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDAFI 132
Cdd:cd04584    82 KDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAFI 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-133 4.03e-36

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 123.44  E-value: 4.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAELVAQNSPSmatsLSVHELNYLLNKTTAKD 79
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLP----DRLDELEERLLDLPVED 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2128734723  80 IMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFID 133
Cdd:COG3448    78 VMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 3-128 2.27e-19

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 85.13  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDY---MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVaQNSPSMATSLSvhelnyllnkttakD 79
Cdd:pfam00478  79 VKRSesgMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDL-RFETDLSQPVS--------------E 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723  80 IMLK-QVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:pfam00478 144 VMTKeNLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIE 193
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
74-185 4.71e-13

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 67.16  E-value: 4.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  74 KTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFIDIsgyntpgsrLFIEINEDKP 153
Cdd:PRK14869   67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYMDI---------LDPEILSKSP 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2128734723 154 GPLENISNVLrDHNVNVDTISVYHRDGKVQVV 185
Cdd:PRK14869  138 TSLENIIRTL-DGEVLVGAEEDKVEEGKVVVA 168
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 85-127 2.36e-09

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: 51.36  E-value: 2.36e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2128734723   85 VITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
 143-202 5.23e-05

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151  Cd Length: 71  Bit Score: 40.14  E-value: 5.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2128734723 143 RLFIeINEDKPGPLENISNVLRDHNVNVDTISVYhRDGKVQ---VVLHVDSENPDEVADFIAQ 202
Cdd:cd04879     1 RLLI-VHKDVPGVIGKVGTILGEHGINIAAMQVG-RKEKGGiayMVLDVDSPVPEEVLEELKA 61
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
150-205 1.65e-04

ACT domain-containing protein [General function prediction only];


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 40.12  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2128734723 150 EDKPGPLENISNVLRDHNVNVDTI--SVYHRDGKVQVVLHVDseNPDEVADFIAQRGY 205
Cdd:COG4747    74 PDRPGGLAEILKALAEAGINIEYMyaFVGRPGGKAVLILRVD--DLEKAIEVLKENGI 129
CBS_CbpB NF041630
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ...
 34-131 7.04e-04

cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase.


Pssm-ID: 469514 [Multi-domain]  Cd Length: 143  Bit Score: 38.58  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  34 RLPVV-EGDKLVGLLTAELVaqnspsMATSLSVHELNY-LLNKTTAKDIMLKQVITVKPTAVLEEAASIMrqqgigV--- 108
Cdd:NF041630   44 KIPVLdKDKKFVGLISLSDI------TDYMLGLERIEFeKLSELKVADVMNTDVPTITDDYDLEEILHLL------Vdhp 111

                          90       100
                  ....*....|....*....|....
gi 2128734723 109 -LPVLESRGNLVGIITDKDIMDAF 131
Cdd:NF041630  112 fLPVVDEDGIFLGIITRREILKAV 135
 
Name Accession Description Interval E-value
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-132 4.67e-58

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: 179.15  E-value: 4.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQNSPSMATSLSVHELNYLLNKTTAKDIML 82
Cdd:cd04584     2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRASPSKATSLSIYELNYLLSKIPVKDIMT 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDAFI 132
Cdd:cd04584    82 KDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAFI 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-133 4.03e-36

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 123.44  E-value: 4.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAELVAQNSPSmatsLSVHELNYLLNKTTAKD 79
Cdd:COG3448     2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLP----DRLDELEERLLDLPVED 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2128734723  80 IMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFID 133
Cdd:COG3448    78 VMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-131 9.61e-34

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 119.60  E-value: 9.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQNSPSmatslsvhelNYLLNKTTAKDI 80
Cdd:COG2524    86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAE----------GRDLLDAPVSDI 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128734723  81 MLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAF 131
Cdd:COG2524   156 MTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
1-133 1.22e-31

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 111.88  E-value: 1.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAELVAQNSPSMATSLSvhelnyllnKTTAKD 79
Cdd:COG0517     1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVdEDGKLVGIVTDRDLRRALAAEGKDLL---------DTPVSE 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2128734723  80 IMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFID 133
Cdd:COG0517    72 VMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 8-129 4.43e-26

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: 96.93  E-value: 4.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAQNSPSMatslsvhelnYLLNKTTAKDIMLKQVI 86
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDgKLVGIVTERDILRALVEG----------GLALDTPVAEVMTPDVI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2128734723  87 TVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMD 129
Cdd:cd02205    71 TVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 3-133 1.08e-25

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 96.44  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTA-ELVAQnspsmatslsVHELNYLLNKTTAKDI 80
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDgRLVGIITDrDLRRR----------VLAEGLDPLDTPVSEV 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2128734723  81 MLKQVITVKPTAVLEEAASIMRQQGIGVLPVLEsRGNLVGIITDKDIMDAFID 133
Cdd:COG2905    71 MTRPPITVSPDDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRALSE 122
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 7-127 4.65e-25

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: 94.41  E-value: 4.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT-------AelVAQNSPsmatslsvhelnylLNKTTAKD 79
Cdd:cd04622     1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTdrdivvrA--VAEGKD--------------PNTTTVRE 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723  80 IMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd04622    65 VMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 3-131 6.76e-23

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: 89.21  E-value: 6.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAE-----LVAQNSPSMATSLSVHElnylLNKTTA 77
Cdd:cd04631     2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTdimryLGSGEAFEKLKTGNIHE----VLNVPI 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2128734723  78 KDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLEsRGNLVGIITDKDIMDAF 131
Cdd:cd04631    78 SSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVD-DGKLVGIITERDILRAI 130
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-130 1.53e-22

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: 88.64  E-value: 1.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT-AELVAQNS----PSMATSLSVHELNYL--------L 72
Cdd:cd04586     1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDgKLVGIVSeGDLLRREEpgtePRRVWWLDALLESPErlaeeyvkA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2128734723  73 NKTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDA 130
Cdd:cd04586    81 HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLLRA 137
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 3-130 2.59e-22

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: 87.77  E-value: 2.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQNSPSMATSLSVHELNYL-LNKTTAKDIM 81
Cdd:cd17778     2 VKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYFGSHEAKKRLTTGDIDeAYSTPVEEIM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723  82 LKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:cd17778    82 SKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIA 130
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-131 2.76e-21

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: 85.31  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT-AELVAQ----NSPSMATSLSVHELNYLLNKTTAKDI 80
Cdd:cd04600     1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRArRLVGIVTlADLLKHadldPPRGLRGRLRRTLGLRRDRPETVGDI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128734723  81 MLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAF 131
Cdd:cd04600    81 MTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLIAAL 131
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
1-130 1.69e-19

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 80.73  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   1 MEVKDYM-STNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAELVAQNSPSmatslsvhelnyllnkTTAK 78
Cdd:COG4109    16 LLVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVdENGRLVGIVTSKDILGKDDD----------------TPIE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2128734723  79 DIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:COG4109    80 DVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKA 131
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-128 1.77e-19

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 79.69  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQNSPsmatslsvhelnyllNKTTAkDIMLKQVI 86
Cdd:cd04599     1 MTRNPITISPLDSVARAAALMERQRIGGLPVVENGKLVGIITSRDVRRAHP---------------NRLVA-DAMSRNVV 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2128734723  87 TVKPTAVLEEAASIMRQQGIGVLPVLEsRGNLVGIITDKDIM 128
Cdd:cd04599    65 TISPEASLWEAKELMEEHGIERLVVVE-EGRLVGIITKSTLY 105
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-127 2.08e-19

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: 79.98  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVaqnSPSMAtslsvhelnylLNKTTAKDIM 81
Cdd:cd04605     2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDgKLIGIVTSWDI---SKAVA-----------LKKDSLEEIM 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  82 LKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd04605    68 TRNVITARPDEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 3-128 2.27e-19

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 85.13  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDY---MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVaQNSPSMATSLSvhelnyllnkttakD 79
Cdd:pfam00478  79 VKRSesgMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDL-RFETDLSQPVS--------------E 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723  80 IMLK-QVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:pfam00478 144 VMTKeNLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIE 193
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 8-129 2.48e-18

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: 76.80  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT----AELVAQNSPSMatslsvhelnyllnktTAKDIMLK 83
Cdd:cd04588     1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTltdiAKALAEGKENA----------------KVKDIMTK 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  84 QVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMD 129
Cdd:cd04588    65 DVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 7-128 3.83e-18

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: 76.43  E-value: 3.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT-----AELVAQNSPSmatslsvhelnyllNKTTAKDI 80
Cdd:cd17775     1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDgKPVGIVTdrdivVEVVAKGLDP--------------KDVTVGDI 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723  81 MLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd17775    67 MSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDIL 114
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 5-130 5.89e-18

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: 76.07  E-value: 5.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   5 DYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAqnspsmatslSVHELNYllNKTTAKDIMLKQ 84
Cdd:cd04801     1 DIMTPEVVTVTPEMTVSELLDRMFEEKHLGYPVVENGRLVGIVTLEDIR----------KVPEVER--EATRVRDVMTKD 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  85 VITVKPTAVLEEAASIMRQQGIGVLPVLEsRGNLVGIITDKDIMDA 130
Cdd:cd04801    69 VITVSPDADAMEALKLMSQNNIGRLPVVE-DGELVGIISRTDLMRA 113
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 2-131 1.30e-17

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: 75.73  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   2 EVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEG--DKLVGLLTA-------------ELVAQNspsmatslsvH 66
Cdd:cd17779     1 SIMAIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADAgtKRLEGIVTSmdivdflgggskyNLVEKK----------H 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2128734723  67 ELNYL--LNKTTaKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAF 131
Cdd:cd17779    71 NGNLLaaINEPV-REIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 7-131 3.72e-17

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: 74.10  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTA----ELVAQNSPsmatslsvhelnyllNKTTAKDIM 81
Cdd:cd09836     1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDgKPVGIVTErdivRAVAEGID---------------LDTPVEEIM 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723  82 LKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAF 131
Cdd:cd09836    66 TKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 12-131 9.51e-17

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: 73.53  E-value: 9.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  12 ITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAE-----LVAQNSPSMATSLSVHELNYLLNKTTAKDIMLKQVI 86
Cdd:cd17777    13 LSISPSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARdlvsyLGGGCLFKIVESRHQGDLYSALNREVVETIMTPNPV 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2128734723  87 TVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAF 131
Cdd:cd17777    93 YVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL 137
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-128 5.59e-16

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: 70.92  E-value: 5.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT-----AELVAQnspSMATSLSVHElnyllnkttakdIM 81
Cdd:cd04587     2 MSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTdrdlrNRVVAE---GLDPDTPVSE------------IM 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723  82 LKQVITVKPTAVLEEAASIMRQQGIGVLPVLEsRGNLVGIITDKDIM 128
Cdd:cd04587    67 TPPPVTIDADALVFEALLLMLERNIHHLPVVD-DGRVVGVVTATDLM 112
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
6-129 5.69e-16

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 75.49  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   6 YMSTNLITVEPTTTVMKALDLMKEHD-----VHRLPVV-EGDKLVGlltaelvaqnspsmatSLSVHELnyLLNK--TTA 77
Cdd:COG2239   134 LMTTEFVAVREDWTVGEALRYLRRQAedpetIYYIYVVdDDGRLVG----------------VVSLRDL--LLADpdTKV 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2128734723  78 KDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMD 129
Cdd:COG2239   196 SDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVD 247
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 8-130 6.13e-16

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: 71.35  E-value: 6.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTA-ELVAQNS------------PSMATSLSVHELNYLLN 73
Cdd:cd17789     2 KGKLHVVKPNTTVDEALELLVENRITGLPVIDEDwRLVGVVSDyDLLALDSisgrsqtdnnfpPADSTWKTFNEVQKLLS 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  74 KTTAK---DIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:cd17789    82 KTNGKvvgDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVRA 141
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 9-128 7.60e-16

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 70.13  E-value: 7.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   9 TNLITVEPTTTVMKALDLMKEHDVHRLPVVE-GDKLVGLLTAELVaQNSPSMATSLSvhelnyllnkttakDIMLKQ--V 85
Cdd:cd04601     2 TDPVTLSPDATVADVLELKAEYGISGVPVTEdGGKLVGIVTSRDI-RFETDLSTPVS--------------EVMTPDerL 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2128734723  86 ITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd04601    67 VTAPEGITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIE 109
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 11-130 9.49e-16

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: 70.44  E-value: 9.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  11 LITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLT----AELVAQNSPSMATSLSVHELNYLLNkTTAKDIMLKQV 85
Cdd:cd04632     4 VITVNEDDTIGKAINLLREHGISRLPVVdDNGKLVGIVTtydiVDFVVRPGTKTRGGDRGGEKERMLD-LPVYDIMSSPV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2128734723  86 ITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:cd04632    83 VTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 7-130 1.24e-15

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: 69.77  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTaelvaqnspsmatslsvhE---LNYLLNKT------- 75
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQgRLVGFLS------------------EqdcLKALLEASyhcepgg 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2128734723  76 TAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDA 130
Cdd:cd04629    63 TVADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDVLRA 116
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 7-127 1.84e-15

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: 69.27  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTA-ELVAQNSpsmatslsvhelnyllnKTTAKDIMLKQV 85
Cdd:cd04610     1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAkDLLGKDD-----------------DEKVSEIMSRDT 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2128734723  86 ITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd04610    64 VVADPDMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDV 105
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 8-128 2.33e-15

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: 69.06  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQnspsmatslsvhELNYLLNKTTAKDIMLKQVIT 87
Cdd:cd04595     1 SSPVKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDVDK------------AKHHGLGHAPVKGYMSTNVIT 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2128734723  88 VKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIM 128
Cdd:cd04595    69 IDPDTSLEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVL 108
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 7-129 2.78e-15

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 69.28  E-value: 2.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHD-----VHRLPVV-EGDKLVGlltaelvaqnspsmatSLSVHELnyLLNK--TTAK 78
Cdd:cd04606     7 MTTEFVAVRPDWTVEEALEYLRRLApdpetIYYIYVVdEDRRLLG----------------VVSLRDL--LLADpdTKVS 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128734723  79 DIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMD 129
Cdd:cd04606    69 DIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLD 119
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 8-122 6.04e-15

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: 67.83  E-value: 6.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEG-DKLVGLLT----AELVAQNSPSmatSLSvhelnyllnkTTAKDIML 82
Cdd:cd04623     1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSerdyVRKLALRGAS---SLD----------TPVSEIMT 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGII 122
Cdd:cd04623    68 RDVVTCTPDDTVEECMALMTERRIRHLPVVED-GKLVGIV 106
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 9-130 2.18e-14

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


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 66.68  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   9 TNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAQNspsmaTSLSVHELNyllnkTTAKDIMLKQVIT 87
Cdd:cd17784     2 KNVITAKPNEGVVEAFEKMLKHKISALPVVDDEgKLIGIVTATDLGHN-----LILDKYELG-----TTVEEVMVKDVAT 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723  88 VKPTAVLEEAASIMRQQG-----IGVLPVLESrGNLVGIITDKDIMDA 130
Cdd:cd17784    72 VHPDETLLEAIKKMDSNApdeeiINQLPVVDD-GKLVGIISDGDIIRA 118
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-48 7.61e-14

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: 65.21  E-value: 7.61e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT 48
Cdd:cd04595    58 VKGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLVGIVT 103
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
74-185 4.71e-13

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 67.16  E-value: 4.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  74 KTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFIDIsgyntpgsrLFIEINEDKP 153
Cdd:PRK14869   67 KPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYMDI---------LDPEILSKSP 137

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2128734723 154 GPLENISNVLrDHNVNVDTISVYHRDGKVQVV 185
Cdd:PRK14869  138 TSLENIIRTL-DGEVLVGAEEDKVEEGKVVVA 168
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 77-133 5.47e-13

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: 61.08  E-value: 5.47e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2128734723  77 AKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFID 133
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-48 7.04e-13

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: 63.22  E-value: 7.04e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT 48
Cdd:cd04586    85 VGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVS 130
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 3-130 1.10e-12

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: 62.23  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV---EGDKLvGLLTAELVAQNspSMATSLSVHELN-Yllnkttak 78
Cdd:cd04630     1 VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVEkrhEHDAY-GIVTYTDILKK--VIAEDRDPDLVNvY-------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2128734723  79 DIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDA 130
Cdd:cd04630    70 EIMTKPAISVSPDLDIKYAARLMARFNLKRAPVIEN-NELIGIVSMTDLVLD 120
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 9-123 2.22e-12

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: 61.00  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   9 TNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAQNspsMATSLSVhelnyllnkttaKDIMLKQVIT 87
Cdd:cd04583     2 TNPVTITPERTLAQAIEIMREKRVDSLLVVDKDnVLLGIVDIEDINRN---YRKAKKV------------GEIMERDVFT 66

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2128734723  88 VKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIIT 123
Cdd:cd04583    67 VKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVT 102
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 16-130 4.14e-12

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: 60.18  E-value: 4.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  16 PTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAQNSPSmatslsvhelnyllnkTTAKDIMLKQVITVKPTAVL 94
Cdd:cd04596     9 ETDTVRDYKQLSEETGHSRFPVVDEEnRVVGIVTAKDVIGKEDD----------------TPIEKVMTKNPITVKPKTSV 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2128734723  95 EEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:cd04596    73 ASAAHMMIWEGIELLPVVDENRKLLGVISRQDVLKA 108
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 13-123 5.27e-12

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


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 60.63  E-value: 5.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  13 TVEPTTTVMKALDLM----------KEHDVHRLP------VVEGDKLVGLLTA----ELVAQNSPsmatslsvhelnylL 72
Cdd:cd04620    11 TVSPDTPVIEAIALMsqtrssccllSEDSIITEArsscvlVVENQQLVGIFTErdvvRLTASGID--------------L 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2128734723  73 NKTTAKDIMLKQVITVK------PTAVLeeaaSIMRQQGIGVLPVLESRGNLVGIIT 123
Cdd:cd04620    77 SGVTIAEVMTQPVITLKesefqdIFTVL----SLLRQHQIRHLPIVDDQGQLVGLIT 129
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 1-48 5.99e-12

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: 59.89  E-value: 5.99e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT 48
Cdd:cd04801    59 TRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIIS 106
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 7-130 7.79e-12

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: 59.66  E-value: 7.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD--KLVGLLTAELVAQNSPSMATSLsvhelnyllnkttakdIMLKQ 84
Cdd:cd04638     1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKEtgKLVGIVTRKDLLRNPDEEQIAL----------------LMSRD 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  85 VITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDA 130
Cdd:cd04638    65 PITISPDDTLSEAAELMLEHNIRRVPVVDD-DKLVGIVTVADLVRA 109
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 7-139 8.57e-12

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


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 60.24  E-value: 8.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD--------KLVGLLTAELVAQnspsmatsLSVHELNylLNKTTAK 78
Cdd:cd17774     3 MTTRVIHAPPTASVLELAQLMAEHRVSCVVIVEEDeqqeknklIPVGIVTERDIVQ--------FQALGLD--LSQTQAQ 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2128734723  79 DIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFIDISGYNT 139
Cdd:cd17774    73 TVMSSPLFSLRPDDSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSLLQALDPLEMYHV 133
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
74-131 1.70e-11

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 61.05  E-value: 1.70e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2128734723  74 KTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDAF 131
Cdd:COG2524    85 KMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKAL 141
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 1-47 3.83e-11

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: 57.81  E-value: 3.83e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLL 47
Cdd:cd04623    60 TPVSEIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVEDGKLVGIV 106
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 3-50 1.08e-10

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: 55.30  E-value: 1.08e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAE 50
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDgKLVGIVTLK 49
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 1-48 1.39e-10

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: 56.27  E-value: 1.39e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDK-LVGLLT 48
Cdd:cd04622    60 TTVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGrLVGIVS 108
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 3-48 2.49e-10

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: 55.71  E-value: 2.49e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT 48
Cdd:cd02205    61 VAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDgKLVGIVT 107
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-49 2.96e-10

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: 55.51  E-value: 2.96e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTA 49
Cdd:cd04587    62 VSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDDGRVVGVVTA 108
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 3-49 3.11e-10

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: 55.61  E-value: 3.11e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTA 49
Cdd:cd09836    61 VEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGgKLVGVISI 108
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 3-48 4.78e-10

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: 55.14  E-value: 4.78e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT 48
Cdd:cd04629    64 VADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQIS 109
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-130 7.20e-10

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 54.85  E-value: 7.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT-----AELVAQNSpsmatslsvhelnylLNKTT 76
Cdd:cd04608     4 VRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDgRVVGMVTegnllSSLLAGRA---------------QPSDP 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2128734723  77 AKDIMLKQVITVKPTAVLEEAASIMrQQGIGVLpVLESRGNLVGIITDKDIMDA 130
Cdd:cd04608    69 VSKAMYKQFKQVDLDTPLGALSRIL-ERDHFAL-VVDGQGKVLGIVTRIDLLNY 120
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-128 1.62e-09

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: 53.68  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDK---LVGLLT-AELVA--QNSPSMATSLSvhelnyllnktt 76
Cdd:cd04591     2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTEsqtLVGFILrSQLILllEADLRPIMDPS------------ 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2128734723  77 akdimlkqVITVKPTAVLEEAASIMRQQGIGVLPVlESRGNLVGIITDKDIM 128
Cdd:cd04591    70 --------PFTVTEETSLEKVHDLFRLLGLRHLLV-TNNGRLVGIVTRKDLL 112
CBS_pair_bac cd17783
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 13-128 1.90e-09

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: 341419 [Multi-domain]  Cd Length: 108  Bit Score: 53.35  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  13 TVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAqNSPSMATSLSVHELNYllnkttakdimlkQVITVKPTA 92
Cdd:cd17783     6 PLKPTDSVEKALDWMEEFRVSQLPVVDNGQYLGLISEDDLL-ELNDPEAPLSNLPLSL-------------KDVFVYEDQ 71

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2128734723  93 VLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd17783    72 HFYDVIRLASEYKLEVVPVLDEENEYLGVITVNDLL 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 85-127 2.36e-09

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: 51.36  E-value: 2.36e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2128734723   85 VITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 3-50 2.56e-09

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: 52.93  E-value: 2.56e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAE 50
Cdd:cd17775    63 VGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDgELVGIVTLD 111
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 7-130 3.70e-09

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: 52.79  E-value: 3.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQnspsmatslSVHELNYLLNKTTAKDIMLKQVI 86
Cdd:cd17776     1 MTTDVVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALH---------AGYATDDPFSEIPVRAVASRPLV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2128734723  87 TVKPTAVLEEAASIMRQQGIGVLPVLEsRGNLVGIITDKDIMDA 130
Cdd:cd17776    72 TISPTATLREAAERMVDEGVKKLPVVD-GLDLVGILTATDIIRA 114
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 6-130 7.10e-09

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: 52.67  E-value: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   6 YMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT----------AELVAQNSPSMAT------------- 61
Cdd:cd04614     1 YAGKGVVPVWDETPLPVALRAMRLANVPAAPVLDSEgKLVGIVTerdlidvsriVESEEESGMSIADdedewswegirdv 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  62 -SLSVHELNYLLNKTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:cd04614    81 mSLYYPTSNVELPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDLLKA 150
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 12-131 8.23e-09

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


Pssm-ID: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 51.58  E-value: 8.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  12 ITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTaelvaqnspsmatslsvheLNYLLNKTTAK--DIMLKQVITV 88
Cdd:cd04594     5 IKVSAYDTVERALKIMRENNLLSLPVVdNDSNFLGAVY-------------------LRDIENKSPGKvgKYVVRGSPYV 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2128734723  89 KPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDAF 131
Cdd:cd04594    66 TPTSSLEEAWEIMMRNKSRWVAVVEK-GKFLGIITLDDLLEAY 107
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 83-133 9.62e-09

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: 51.48  E-value: 9.62e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFID 133
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE 52
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 8-127 1.13e-08

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


Pssm-ID: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 51.03  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEG--DKLVGLLTAELVAQnspsmatslsvhELNYLLNKTTAKDIMLKQV 85
Cdd:cd17772     1 SSPVISVEPDTTIAEAAELMTRYNINALPVVDGgtGRLVGIITRQVAEK------------AIYHGLGDLPVSEYMTTEF 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2128734723  86 ITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDI 127
Cdd:cd17772    69 ATVTPDAPLSEIQEIIVEQRQRLVPVVED-GRLVGVITRTDL 109
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 74-130 2.12e-08

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 50.61  E-value: 2.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2128734723  74 KTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:cd04608     1 DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSS 57
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 83-128 2.16e-08

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: 50.49  E-value: 2.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYV 47
CBS_pair_ABC_OpuCA_assoc cd04582
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 7-130 2.22e-08

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: 341359 [Multi-domain]  Cd Length: 111  Bit Score: 50.46  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAQNSPSMATslSVHELNyllnkttakdimlkqv 85
Cdd:cd04582     3 AATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADgRPLGYVTRRDARGASGTCGD--FAHPFK---------------- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2128734723  86 ITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDA 130
Cdd:cd04582    65 ATVPVDENLRVVLSRMYEHNTSWLPVVDEDGRYAGEVTQDSIADY 109
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-48 2.71e-08

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 50.03  E-value: 2.71e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT 48
Cdd:cd04599    55 VADAMSRNVVTISPEASLWEAKELMEEHGIERLVVVEEGRLVGIIT 100
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 2-120 2.79e-08

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: 50.73  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   2 EVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD--KLVGLLTAE-----LVAQNSPSMATSLSVHELNYLLNK 74
Cdd:cd17785     3 DIYNLITKKPSVVHENTSIRDVIDKMIEDPKTRSVYVVDDdeKLLGIITLMellkyIGYRFGVTIYKGVSFGLLLRISLK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  75 TTAKDIMlKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVG 120
Cdd:cd17785    83 EKAKDIM-LSPIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIG 127
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 2-49 4.07e-08

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: 49.71  E-value: 4.07e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723   2 EVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTA 49
Cdd:cd17776    61 PVRAVASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLDLVGILTA 108
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 81-143 4.61e-08

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: 49.74  E-value: 4.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2128734723  81 MLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFIDISGYNTPGSR 143
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPGGT 63
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 10-50 1.14e-07

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: 46.74  E-value: 1.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2128734723   10 NLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAE 50
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLVGIVTRR 42
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 80-127 1.28e-07

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: 48.19  E-value: 1.28e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723  80 IMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDI 127
Cdd:cd04587     1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDD-GRLVGIVTDRDL 47
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 9-129 3.61e-07

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 46.96  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   9 TNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAqnspsmatslsvhelnyllnkTTAKDIMLKQ-VI 86
Cdd:cd04597     5 DKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNgKLIGLLSISDIA---------------------RTVDYIMTKDnLI 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2128734723  87 TVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMD 129
Cdd:cd04597    64 VFKEDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 76-128 4.60e-07

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: 47.22  E-value: 4.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2128734723  76 TAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLeSRGNLVGIITDKDIM 128
Cdd:cd04631     1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIM 52
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 76-127 4.75e-07

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: 46.85  E-value: 4.75e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2128734723  76 TAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd04605     1 LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDI 52
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 3-47 6.56e-07

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: 47.27  E-value: 6.56e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEG-DKLVGLL 47
Cdd:cd04614    97 VKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGeGDLAGML 142
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 83-129 6.90e-07

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: 46.56  E-value: 6.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMD 129
Cdd:cd04632     2 EEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVD 48
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 77-138 7.48e-07

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: 46.56  E-value: 7.48e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2128734723  77 AKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLeSRGNLVGIITDKDI------MDAFIDISGYN 138
Cdd:cd17778     2 VKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVV-SGGKLVGIVTAMDIvkyfgsHEAKKRLTTGD 68
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 69-122 1.27e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 45.84  E-value: 1.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2128734723  69 NYLLNKTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGII 122
Cdd:cd04604    64 GLDILNLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGIL 117
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-48 1.65e-06

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: 45.25  E-value: 1.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT 48
Cdd:cd17772    58 LPVSEYMTTEFATVTPDAPLSEIQEIIVEQRQRLVPVVEDGRLVGVIT 105
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
3-48 2.32e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 47.52  E-value: 2.32e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLT 48
Cdd:PRK14869   70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVdEEGKLLGLVS 116
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 6-127 2.33e-06

CBS domain protein; 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 45.00  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   6 YMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTA----ELVAQNSPSMATSLSvhelnyllnkttakDI 80
Cdd:cd17771     1 LIRREPVTCSPDTPLRAALETMHERRVGSMVVVDANrRPVGIFTLrdllSRVALPQIDLDAPIS--------------EV 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723  81 MLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDI 127
Cdd:cd17771    67 MTPDPVRLPPSASAFEAALLMAEHGFRHVCVVDN-GRLVGVVSERDL 112
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 1-48 3.96e-06

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: 44.06  E-value: 3.96e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT 48
Cdd:cd04588    56 AKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNgKPVGIIT 104
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-123 4.50e-06

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: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 44.28  E-value: 4.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAELVAQ---NSPSMATSLSVHELNYLLNKTTAKDIML 82
Cdd:cd04592     1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVdSDDFLIGILTLGDIQRflkRAKADNEDPKTILVSSICTRNGGYCRGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  83 kqvITVKPTAVLEEAASIMRQQGIGVLPVL-----ESRGNLVGIIT 123
Cdd:cd04592    81 ---WTCTPDMDLLTAKMLMEARGINQLPVVkrggeERRRRVVGLLD 123
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 5-127 4.95e-06

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: 44.14  E-value: 4.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   5 DYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLT-AELVAQN-SPSMATSLSVHELnyllnkttakdiML 82
Cdd:cd09833     1 RIVSTSLLTCSPDTPLADAAARMAERRCSSILIVENGEIVGIWTeRDALKLDfSDPDAFRRPISEV------------MS 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd09833    69 SPVLTIPQDTTLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDV 113
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 3-48 6.17e-06

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 43.56  E-value: 6.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723   3 VKDYMSTN--LITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLT 48
Cdd:cd04601    56 VSEVMTPDerLVTAPEGITLEEAKEILHKHKIEKLPIVdDNGELVGLIT 104
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 85-130 6.37e-06

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: 43.64  E-value: 6.37e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723  85 VITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDA 130
Cdd:cd04595     4 VKTVSPDTTIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDVDKA 48
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 3-48 7.52e-06

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: 43.86  E-value: 7.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLV-GLLT 48
Cdd:cd04632    74 VYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMViGILT 120
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 12-127 1.04e-05

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 45.35  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  12 ITVEPTTTVMKALDLMKEHDVHRLPVVE----GDKLVGLLTAelvaqnspsmatslsvHELNYLLNKTTA-KDIM--LKQ 84
Cdd:PTZ00314  107 YVLSPNHTVADVLEIKEKKGFSSILITVdgkvGGKLLGIVTS----------------RDIDFVKDKSTPvSEVMtpREK 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2128734723  85 VITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:PTZ00314  171 LVVGNTPISLEEANEVLRESRKGKLPIVNDNGELVALVSRSDL 213
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 12-122 2.11e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 42.19  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  12 ITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAQNSpsMATSLSVhelnyllNKTTAKDIMLKQVITVKP 90
Cdd:cd17781     5 LTVPETTTVAEAAQLMAAKRTDAVLVVDDDgGLSGIFTDKDLARRV--VASGLDP-------RSTLVSSVMTPNPLCVTM 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2128734723  91 TAVLEEAASIMRQQGIGVLPVLESRGNLVGII 122
Cdd:cd17781    76 DTSATDALDLMVEGKFRHLPVVDDDGDVVGVL 107
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-131 2.42e-05

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


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 42.18  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAelvaQNSPSMATSLSVHELnyllnkTTAKDIMLKQV 85
Cdd:cd04613     1 MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVdEQGRLTGILSI----QDVRGVLFEEELWDL------VVVKDLATTDV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723  86 ITVKPTAVLEEAASIMRQQGIGVLPVLES--RGNLVGIITDKDIMDAF 131
Cdd:cd04613    71 ITVTPDDDLYTALLKFTSTNLDQLPVVDDddPGKVLGMLSRRDVIAAY 118
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 5-127 3.10e-05

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: 41.79  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   5 DYMSTNLITVEPTTTVMKALD--LMKEHDVHRLPVVEGD-KLVGLLTAELVAQNSPSMATSLSVHELnyllnkttakdiM 81
Cdd:cd04639     1 DAMVTEFPIVDADLTLREFADdyLIGKKSWREFLVTDEAgRLVGLITVDDLRAIPTSQWPDTPVREL------------M 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723  82 --LKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd04639    69 kpLEEIPTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDI 116
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04589
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-47 4.67e-05

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: 341365 [Multi-domain]  Cd Length: 113  Bit Score: 41.40  E-value: 4.67e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLL 47
Cdd:cd04589    59 TPVGEIATFPLISVEPDDFLFNALLLMTRHRVKRVVVREGEEIVGVL 105
ACT_3PGDH-like cd04879
ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate ...
 143-202 5.23e-05

ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); ACT_3PGDH-like: The ACT_3PGDH-like CD includes the C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with or without an extended C-terminal (xct) region found in various bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback controlled by the end product L-serine in an allosteric manner. In the Escherichia coli homotetrameric enzyme, the interface at adjacent ACT (regulatory) domains couples to create an extended beta-sheet. Each regulatory interface forms two serine-binding sites. The mechanism by which serine transmits inhibition to the active site is postulated to involve the tethering of the regulatory domains together to create a rigid quaternary structure with a solvent-exposed active site cleft. This CD also includes the C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillus, and Treponema species. LSD enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in E. coli, and other Enterobacteriales, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153151  Cd Length: 71  Bit Score: 40.14  E-value: 5.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2128734723 143 RLFIeINEDKPGPLENISNVLRDHNVNVDTISVYhRDGKVQ---VVLHVDSENPDEVADFIAQ 202
Cdd:cd04879     1 RLLI-VHKDVPGVIGKVGTILGEHGINIAAMQVG-RKEKGGiayMVLDVDSPVPEEVLEELKA 61
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 2-50 5.36e-05

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: 41.07  E-value: 5.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723   2 EVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAE 50
Cdd:cd04605    62 SLEEIMTRNVITARPDEPIELAARKMEKHNISALPVVDDDrRVIGIITSD 111
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-47 8.83e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 40.83  E-value: 8.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLL 47
Cdd:cd04604    72 AKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDgKPVGIL 117
ACT_Bt0572_2 cd04882
C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD ...
 143-208 9.44e-05

C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD is the C-terminal ACT domain of a novel protein composed of just two ACT domains, as seen in the yet uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related proteins. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153154  Cd Length: 65  Bit Score: 39.12  E-value: 9.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2128734723 143 RLFIEInEDKPGPLENISNVLRDHNVNVDTISVY--HRDGKVQVVLHVdsENPDEVADFIAQRGYRII 208
Cdd:cd04882     1 VLAVEV-PDKPGGLHEILQILSEEGINIEYMYAFveKKGGKALLIFRT--EDIEKAIEVLQERGVELV 65
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 141-208 1.00e-04

C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD includes the C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB. AcuB is putatively involved in the anaerobic catabolism of acetoin, and related proteins. Studies report the induction of AcuB by nitrate respiration and also by fermentation. Since acetoin can be secreted and later serve as a source of carbon, it has been proposed that, during anaerobic growth when other carbon sources are exhausted, the induction of the AcuB protein results in acetoin catabolism. AcuB-like proteins have two N-terminal tandem CBS domains and a single C-terminal ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153155  Cd Length: 72  Bit Score: 39.16  E-value: 1.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723 141 GSRLFIEInEDKPGPLENISNVLRDHNVNVDTISVY--HRDGKVQVVLHVDSENPDEVADFIAQRGYRII 208
Cdd:cd04883     1 SSQIEVRV-PDRPGQLADIAAIFKDRGVNIVSVLVYpsKEEDNKILVFRVQTMNPRPIIEDLRRAGYEVL 69
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 3-48 1.45e-04

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: 40.53  E-value: 1.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT 48
Cdd:cd17789    88 VGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDgKLVGIIT 134
CBS_pair_arch1_repeat1 cd17780
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 8-129 1.47e-04

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: 341416 [Multi-domain]  Cd Length: 106  Bit Score: 39.64  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLLTAELVAQNSPSMATSLSVhelnyllnkttakdiMLKQVIT 87
Cdd:cd17780     1 TTEFVEVDADTRLGKVRGLFEDENPKGVVVTDDGEYEGVVTERQLLQSHVEDDAKVGA---------------LVRAAPK 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2128734723  88 VKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMD 129
Cdd:cd17780    66 VDRTEDVREVARLLVEGGTKVAPVFEG-GSLWGVVTADAILE 106
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
150-205 1.65e-04

ACT domain-containing protein [General function prediction only];


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 40.12  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2128734723 150 EDKPGPLENISNVLRDHNVNVDTI--SVYHRDGKVQVVLHVDseNPDEVADFIAQRGY 205
Cdd:COG4747    74 PDRPGGLAEILKALAEAGINIEYMyaFVGRPGGKAVLILRVD--DLEKAIEVLKENGI 129
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 3-47 1.67e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 39.88  E-value: 1.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLL 47
Cdd:cd17781    62 VSSVMTPNPLCVTMDTSATDALDLMVEGKFRHLPVVDDDgDVVGVL 107
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 79-127 2.02e-04

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 39.25  E-value: 2.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723  79 DIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd04597     1 DLEYDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDI 49
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-48 2.04e-04

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


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 39.48  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD---KLVGLLT 48
Cdd:cd04613    62 VKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDDDdpgKVLGMLS 110
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 75-136 2.48e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 39.29  E-value: 2.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2128734723  75 TTAKDIMLK--QVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI---MDAFIDISG 136
Cdd:cd04604     3 LRVSDLMHTgdELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLrraLEKGLDILN 69
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 83-131 2.56e-04

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: 39.05  E-value: 2.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723  83 KQVITVKPTAVLEEAASIMRQQGIGVLPVLESrGNLVGIITDKDIMDAF 131
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD-GKLVGIVTLTDIAKAL 49
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 3-48 3.03e-04

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: 38.97  E-value: 3.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT 48
Cdd:cd04607    60 VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQgRVVGLET 106
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-53 3.29e-04

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: 39.08  E-value: 3.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT-AELVA 53
Cdd:cd04600    77 VGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADgRLVGIVTqSDLIA 129
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
3-48 3.93e-04

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 40.44  E-value: 3.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLT 48
Cdd:COG2239   195 VSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVdEEGRLVGIIT 241
ACT_LSD cd04903
C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; ...
 145-202 4.76e-04

C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit; The C-terminal ACT domain of the L-serine dehydratase (LSD), iron-sulfur-dependent, beta subunit, found in various bacterial anaerobes such as Clostridium, Bacillis, and Treponema species. These enzymes catalyze the deamination of L-serine, producing pyruvate and ammonia. Unlike the eukaryotic L-serine dehydratase, which requires the pyridoxal-5'-phosphate (PLP) cofactor, the prokaryotic L-serine dehydratase contains an [4Fe-4S] cluster instead of a PLP active site. The LSD alpha and beta subunits of the 'clostridial' enzyme are encoded by the sdhA and sdhB genes. The single subunit bacterial homologs of L-serine dehydratase (LSD1, LSD2, TdcG) present in Escherichia coli, and other enterobacterials, lack the ACT domain described here. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153175  Cd Length: 71  Bit Score: 37.51  E-value: 4.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2128734723 145 FIEINEDKPGPLENISNVLRDHNVNVDTISVYhRDGKVQ---VVLHVDSENPDEVADFIAQ 202
Cdd:cd04903     2 LIVVHKDKPGAIAKVTSVLADHEINIAFMRVS-RKEKGDqalMVIEVDQPIDEEVIEEIKK 61
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 75-128 4.90e-04

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: 38.19  E-value: 4.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2128734723  75 TTAKDIMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd04607    58 APVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLL 111
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
12-126 5.56e-04

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 40.27  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  12 ITVEPTTTVMKALDLMKEHdVHRLPVV--EGDKLVGLLTAelvaqnspsmatslsvHELNYLLNKTTAKDIMLKQVITVK 89
Cdd:PRK07807  100 VTLSPDDTVGDALALLPKR-AHGAVVVvdEEGRPVGVVTE----------------ADCAGVDRFTQVRDVMSTDLVTLP 162

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2128734723  90 PTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKD 126
Cdd:PRK07807  163 AGTDPREAFDLLEAARVKLAPVVDADGRLVGVLTRTG 199
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 5-134 6.28e-04

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 38.24  E-value: 6.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   5 DYMSTNlITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVG------LLTAELVAQNSPSMATSLsvhelnyllnktta 77
Cdd:cd04617     1 DIMSVP-VVVDETTSVYDAIVTLFLEDVGSLFVVdEEGYLVGvvsrkdLLKATLGGQDLEKTPVSM-------------- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2128734723  78 kdIM--LKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGN---LVGIITDKDIMDAFIDI 134
Cdd:cd04617    66 --IMtrMPNIVTVTPDDSVLEAARKLIEHEIDSLPVVEKEDGklkVVGRITKTNITRLFVEL 125
CBS_CbpB NF041630
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ...
 34-131 7.04e-04

cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase.


Pssm-ID: 469514 [Multi-domain]  Cd Length: 143  Bit Score: 38.58  E-value: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  34 RLPVV-EGDKLVGLLTAELVaqnspsMATSLSVHELNY-LLNKTTAKDIMLKQVITVKPTAVLEEAASIMrqqgigV--- 108
Cdd:NF041630   44 KIPVLdKDKKFVGLISLSDI------TDYMLGLERIEFeKLSELKVADVMNTDVPTITDDYDLEEILHLL------Vdhp 111

                          90       100
                  ....*....|....*....|....
gi 2128734723 109 -LPVLESRGNLVGIITDKDIMDAF 131
Cdd:NF041630  112 fLPVVDEDGIFLGIITRREILKAV 135
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 11-52 7.05e-04

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: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 38.12  E-value: 7.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723  11 LITVEPTTTVMKALDLMKEHDVHRLPVVEGD------KLVGLLTAELV 52
Cdd:cd04592    80 LWTCTPDMDLLTAKMLMEARGINQLPVVKRGgeerrrRVVGLLDRDSI 127
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
2-49 7.12e-04

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 39.89  E-value: 7.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723   2 EVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTA 49
Cdd:PRK07807  149 QVRDVMSTDLVTLPAGTDPREAFDLLEAARVKLAPVVDADgRLVGVLTR 197
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 9-132 7.33e-04

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


Pssm-ID: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 38.26  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   9 TNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTA----ELVAQNSPSmATSLSVHELnyLLNKTTAkdimLK 83
Cdd:cd04641     3 ENIATASMDTPVIDALNLFVERRVSALPIVdEDGRVVDIYAKfdviNLAAEKTYN-NLDLTVGEA--LQHRSED----FE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723  84 QVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMDAFI 132
Cdd:cd04641    76 GVHTCTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 148-202 7.88e-04

ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.


Pssm-ID: 153139 [Multi-domain]  Cd Length: 60  Bit Score: 36.50  E-value: 7.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2128734723 148 INEDKPGPLENISNVLRDHNVNVDTISVYHRDGKVQVVLHVDSENPDEVADFIAQ 202
Cdd:cd02116     4 SGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLEKLLEA 58
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 3-48 8.07e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 38.08  E-value: 8.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLT 48
Cdd:cd04606    67 VSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVdEEGRLVGIIT 113
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 3-48 8.50e-04

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


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 38.29  E-value: 8.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLT 48
Cdd:cd17774    71 AQTVMSSPLFSLRPDDSLWTAHQLMQQRRIRRLVVVgEQGELLGIVT 117
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 3-128 1.43e-03

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: 37.09  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   3 VKDYMS--TNLITVEPTTTVMKALDLMKEHDVHRLPVVEG--DKLVGLLTA-ELvaqnspsmatslsvheLNYLLNKTTA 77
Cdd:cd04590     2 VREVMTprTDVVALDADATLEELLELILESGYSRFPVYEGdlDNIIGVLHVkDL----------------LAALLEGREK 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2128734723  78 KDI--MLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd04590    66 LDLraLLRPPLFVPETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 3-50 1.51e-03

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


Pssm-ID: 341389 [Multi-domain]  Cd Length: 136  Bit Score: 37.52  E-value: 1.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2128734723   3 VKDYMSTNLITV--EPTTTVMKALDLMKEHDVHRLPVV-EGDKLVGLLTAE 50
Cdd:cd04620    81 IAEVMTQPVITLkeSEFQDIFTVLSLLRQHQIRHLPIVdDQGQLVGLITPE 131
ACT_3PGDH-xct cd04902
C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The ...
 144-202 1.89e-03

C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH); The C-terminal ACT (regulatory) domain of D-3-phosphoglycerate dehydrogenase (3PGDH), with an extended C-terminal (xct) region from bacteria, archaea, fungi, and plants. 3PGDH is an enzyme that belongs to the D-isomer specific, 2-hydroxyacid dehydrogenase family and catalyzes the oxidation of D-3-phosphoglycerate to 3- phosphohydroxypyruvate, which is the first step in the biosynthesis of L-serine, using NAD+ as the oxidizing agent. In bacteria, 3PGDH is feedback-controlled by the end product L-serine in an allosteric manner. Some 3PGDH enzymes have an additional domain formed by an extended C-terminal region. This additional domain introduces significant asymmetry to the homotetramer. Adjacent ACT (regulatory) domains interact, creating two serine-binding sites, however, this asymmetric arrangement results in the formation of two different and distinct domain interfaces between identical domains in the asymmetric unit. How this asymmetry influences the mechanism of effector inhibition is still unknown. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153174  Cd Length: 73  Bit Score: 35.91  E-value: 1.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2128734723 144 LFIEiNEDKPGPLENISNVLRDHNVNVDTISV--YHRDGKVQVVLHVDSENPDEVADFIAQ 202
Cdd:cd04902     2 LVVR-NTDRPGVIGKVGTILGEAGINIAGMQVgrDEPGGEALMVLSVDEPVPDEVLEELRA 61
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 3-47 2.34e-03

CBS domain protein; 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 36.53  E-value: 2.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2128734723   3 VKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLL 47
Cdd:cd17771    63 ISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVDNGRLVGVV 107
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 34-131 2.94e-03

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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 36.32  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  34 RLPVV-EGDKLVGLLTAELVaqnspsMATSLSVHELNY-LLNKTTAKDIMLKQVITVKPTAVLEEAASIMRQQGIgvLPV 111
Cdd:cd04643    32 RIPVLdKDYKLVGLISLSMI------LDAILGLERIEFeKLSELKVEEVMNTDVPTVSPDDDLEEVLHLLVDHPF--LCV 103

                          90       100
                  ....*....|....*....|
gi 2128734723 112 LESRGNLVGIITDKDIMDAF 131
Cdd:cd04643   104 VDEDGYFLGIITRREILKAV 123
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 8-123 3.20e-03

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


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 36.07  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723   8 STNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTAELVAqnSPSMATSLSVHElnyllnkTTAKDIMLKQVI 86
Cdd:cd17782     1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMDNSgKVIGIFTSKDVV--LRVLAAGLDPAT-------TSVVRVMTPNPE 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2128734723  87 TVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIIT 123
Cdd:cd17782    72 TAPPSTTILDALHKMHEGKFLNLPVVDDEGEIVGLVD 108
CBS_pair_GGDEF_EAL cd04598
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-47 3.32e-03

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: 36.26  E-value: 3.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2128734723   7 MSTNLITVEPTTTVMKALDLMKEH-DVHRLPVVEGDKLVGLL 47
Cdd:cd04598     1 LLEEAPPVSPDTTNDEVYELFEENpDLHALPVVDNGRPVGLI 42
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
1-47 3.53e-03

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 37.39  E-value: 3.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2128734723   1 MEVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGDKLVGLL 47
Cdd:PRK10892  269 ASIADVMTPGGIRVRPGILAVDALNLMQSRHITSVLVADGDHLLGVL 315
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 85-127 3.86e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 36.03  E-value: 3.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2128734723  85 VITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd17781     4 ALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDL 46
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 2-48 4.63e-03

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: 36.16  E-value: 4.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2128734723   2 EVKDYMSTNLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLT 48
Cdd:cd17778    76 PVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEgELKGIIT 123
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 82-128 4.70e-03

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


Pssm-ID: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 36.00  E-value: 4.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2128734723  82 LKQV--ITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd04640     2 FRRVppVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDIL 50
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 80-129 5.17e-03

CBS domain protein; 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 35.37  E-value: 5.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2128734723  80 IMLKQVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIMD 129
Cdd:cd17771     1 LIRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLS 50
ACT_CBS cd04884
C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in ...
 150-207 6.65e-03

C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in Thermotoga maritima, Tm0935, and delta proteobacteria; This CD includes the C-terminal ACT domain of the cystathionine beta-synthase (CBS) domain protein found in Thermotoga maritima, Tm0935, and delta proteobacteria. This protein has two N-terminal tandem CBS domains and a single C-terminal ACT domain. The CBS domain is found in a wide range of proteins, often in tandem arrangements and together with a variety of other functional domains. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153156  Cd Length: 72  Bit Score: 34.38  E-value: 6.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2128734723 150 EDKPGPLENISNVLRDHNVNVDTISVYHR---DGKVQVVLHVDSENPDEVADFIAQRGYRI 207
Cdd:cd04884     7 EDKPGTLKPVVDTLREFNARIISILTAFEdapDGMRRVFIRVTPMDRSKENELIEELKAKF 67
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 85-128 7.25e-03

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


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 35.30  E-value: 7.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2128734723  85 VITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDIM 128
Cdd:cd17782     4 PPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVV 47
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 76-133 7.48e-03

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: 35.16  E-value: 7.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2128734723  76 TAKDIM--LKQVITVKPTAVLEEAASIMRQQGIGVLPVLE-SRGNLVGIITDKDIMDAFID 133
Cdd:cd04590     1 TVREVMtpRTDVVALDADATLEELLELILESGYSRFPVYEgDLDNIIGVLHVKDLLAALLE 61
CBS_pair_Thermoplasmatales cd17786
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 10-127 9.56e-03

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: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2128734723  10 NLITVEPTTTVMKALDLMKEHDVHRLPVVEGD-KLVGLLTA-----ELVAQNSPsmATSLSVhelnyllnkttaKDIMLK 83
Cdd:cd17786     3 NFKTINWNATVFDAVKIMNENHLYGLVVKDDDgNYVGLISErsiikRFIPRNVK--PDEVPV------------KLVMRK 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2128734723  84 QVITVKPTAVLEEAASIMRQQGIGVLPVLESRGNLVGIITDKDI 127
Cdd:cd17786    69 PIPKVKSDYDVKDVAAFLSENGLERCAVVDDNGRVVGIVTITDL 112
ACT_ThrD-II-like cd04886
C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and ...
 144-208 9.89e-03

C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains; This CD includes the C-terminal ACT domain of biodegradative (catabolic) threonine dehydratase II (ThrD-II) and other related ACT domains. The Escherichia coli tdcB gene product, ThrD-II, anaerobically catalyzes the pyridoxal phosphate-dependent dehydration of L-threonine and L-serine to ammonia and to alpha-ketobutyrate and pyruvate, respectively. Tetrameric ThrD-II is subject to allosteric activation by AMP, inhibition by alpha-keto acids, and catabolite inactivation by several metabolites of glycolysis and the citric acid cycle. Also included in this CD are N-terminal ACT domains present in smaller (~170 a.a.) archaeal proteins of unknown function. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153158 [Multi-domain]  Cd Length: 73  Bit Score: 33.67  E-value: 9.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2128734723 144 LFIEInEDKPGPLENISNVLRDHNVNVdtISVYH-------RDGKVQVVLHV---DSENPDEVADFIAQRGYRII 208
Cdd:cd04886     1 LRVEL-PDRPGQLAKLLAVIAEAGANI--IEVSHdrafktlPLGEVEVELTLetrGAEHIEEIIAALREAGYDVR 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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