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Conserved domains on  [gi|446557232|ref|WP_000634578|]
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MULTISPECIES: acetoin utilization AcuB family protein [Bacillus]

Protein Classification

acetoin utilization AcuB family protein( domain architecture ID 10140007)

acetoin utilization AcuB family protein contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains and a C-terminal ACT domain, similar to Bacillus subtilis acetoin utilization protein AcuB that is involved in the anaerobic catabolism of acetoin

Gene Ontology:  GO:0045150|GO:0030435
PubMed:  10368162|9020585

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 ...
 2-128 5.12e-47

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: 151.03  E-value: 5.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPSILD----EQVSIDMLQQPLELI 77
Cdd:cd04584    1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRASPSKATslsiYELNYLLSKIPVKDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  78 MKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLHTLV 128
Cdd:cd04584   80 MTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAFI 130
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 137-208 9.94e-35

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: 118.13  E-value: 9.94e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557232 137 SSQIEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQTMNPLKVIDALEAEGYRVLWPN 208
Cdd:cd04883    1 SSQIEVRVPDRPGQLADIAAIFKDRGVNIVSVLVYPSKEEDNKILVFRVQTMNPRPIIEDLRRAGYEVLWPN 72
 
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 ...
 2-128 5.12e-47

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: 151.03  E-value: 5.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPSILD----EQVSIDMLQQPLELI 77
Cdd:cd04584    1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRASPSKATslsiYELNYLLSKIPVKDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  78 MKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLHTLV 128
Cdd:cd04584   80 MTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAFI 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-134 9.36e-42

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 138.07  E-value: 9.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDEQVSIDMLQQPLELIMKH 80
Cdd:COG3448    2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVEDVMTR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446557232  81 PVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTLVKLTGAH 134
Cdd:COG3448   82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVdDDGRLVGIVTRTDLLRALARLLEEE 136
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 137-208 9.94e-35

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: 118.13  E-value: 9.94e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557232 137 SSQIEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQTMNPLKVIDALEAEGYRVLWPN 208
Cdd:cd04883    1 SSQIEVRVPDRPGQLADIAAIFKDRGVNIVSVLVYPSKEEDNKILVFRVQTMNPRPIIEDLRRAGYEVLWPN 72
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 3-56 4.53e-14

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: 64.16  E-value: 4.53e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446557232    3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDA 56
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 10-53 1.28e-10

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: 54.83  E-value: 1.28e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 446557232    10 NVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 138-199 3.27e-07

ACT domain; This family of domains generally have a regulatory role. ACT domains are 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 ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 46.15  E-value: 3.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557232  138 SQIEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQ-TMNPLKVIDALEA 199
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVdEEDLEEVLEALKK 63
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
3-52 9.86e-07

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 48.67  E-value: 9.86e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRD 52
Cdd:PRK14869  70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSD 119
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
96-202 7.51e-05

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


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 40.89  E-value: 7.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  96 TLFFENKIGCLpvTKAGKL-----VGII-------SESTVLHTLV--------KLTGAHQPSSQIE---IQVKNEPGILG 152
Cdd:COG4747    4 SVFLENKPGRL--AEVTRLlgdagINIRalsiadtSDFGILRLIVddpekareVLKEAGFTVSETDvlaVELPDRPGGLA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557232 153 KVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQtmNPLKVIDALEAEGY 202
Cdd:COG4747   82 EILKALAEAGINIEYMYAFVGRPGGKAVLILRVD--DLEKAIEVLKENGI 129
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 2-63 5.98e-03

Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 129495 [Multi-domain]  Cd Length: 449  Bit Score: 37.11  E-value: 5.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557232    2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDE 63
Cdd:TIGR00400 196 ILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSEATE 257
 
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 ...
 2-128 5.12e-47

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: 151.03  E-value: 5.12e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPSILD----EQVSIDMLQQPLELI 77
Cdd:cd04584    1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRASPSKATslsiYELNYLLSKIPVKDI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  78 MKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLHTLV 128
Cdd:cd04584   80 MTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAFI 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-134 9.36e-42

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 138.07  E-value: 9.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDEQVSIDMLQQPLELIMKH 80
Cdd:COG3448    2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVEDVMTR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446557232  81 PVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTLVKLTGAH 134
Cdd:COG3448   82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVdDDGRLVGIVTRTDLLRALARLLEEE 136
ACT_AcuB cd04883
C-terminal ACT domain of the Bacillus subtilis acetoin utilization protein, AcuB; This CD ...
 137-208 9.94e-35

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: 118.13  E-value: 9.94e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557232 137 SSQIEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQTMNPLKVIDALEAEGYRVLWPN 208
Cdd:cd04883    1 SSQIEVRVPDRPGQLADIAAIFKDRGVNIVSVLVYPSKEEDNKILVFRVQTMNPRPIIEDLRRAGYEVLWPN 72
CBS COG0517
CBS domain [Signal transduction mechanisms];
1-130 2.42e-32

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 113.81  E-value: 2.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDAspsiLDEQvSIDMLQQPLELIMKH 80
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRA----LAAE-GKDLLDTPVSEVMTR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  81 PVMTCHPLDFVEEIATLFFENKIGCLPV-TKAGKLVGIISESTVLHTLVKL 130
Cdd:COG0517   76 PPVTVSPDTSLEEAAELMEEHKIRRLPVvDDDGRLVGIITIKDLLKALLEP 126
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 3-127 8.83e-30

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 106.84  E-value: 8.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDAspsILDEQvsIDMLQQPLELIMKHPV 82
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRR---VLAEG--LDPLDTPVSEVMTRPP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446557232  83 MTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLHTL 127
Cdd:COG2905   76 ITVSPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRAL 120
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-127 3.02e-27

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 103.04  E-value: 3.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPSildeqvSIDMLQQPLELIMKH 80
Cdd:COG2524   86 MKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAE------GRDLLDAPVSDIMTR 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446557232  81 PVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTL 127
Cdd:COG2524  159 DVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 8-124 1.33e-22

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: 88.07  E-value: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSildeqvSIDMLQQPLELIMKHPVMTCHP 87
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE------GGLALDTPVAEVMTPDVITVSP 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446557232  88 LDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVL 124
Cdd:cd02205   75 DTDLEEALELMLEHGIRRLPVVdDDGKLVGIVTRRDIL 112
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-126 3.36e-21

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: 85.17  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV--------RDASPSILD---------EQVSIDM 69
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLlrreepgtEPRRVWWLDallesperlAEEYVKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446557232  70 LQQPLELIMKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLHT 126
Cdd:cd04586   81 HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLRA 137
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 7-124 3.47e-19

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: 79.40  E-value: 3.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISdrdvrdaspsildEQvsiDMLQQPLEL---------- 76
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLS-------------EQ---DCLKALLEAsyhcepggtv 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557232  77 --IMKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVL 124
Cdd:cd04629   65 adYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVL 114
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
1-130 4.48e-19

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 79.57  E-value: 4.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   1 MIVEEIM-NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSIldeqvsidmlqqPLELIMK 79
Cdd:COG4109   16 LLVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDT------------PIEDVMT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446557232  80 HPVMTCHPLDFVEEIATLFFENKIGCLPVTK-AGKLVGIISESTVLHTLVKL 130
Cdd:COG4109   84 KNPITVTPDTSLASAAHKMIWEGIELLPVVDdDGRLLGIISRQDVLKALQKI 135
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 8-119 2.24e-17

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: 74.37  E-value: 2.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRD----VRDASPSILDEQVSiDmlqqplelIMKHPVM 83
Cdd:cd04623    1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDyvrkLALRGASSLDTPVS-E--------IMTRDVV 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446557232  84 TCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIIS 119
Cdd:cd04623   72 TCTPDDTVEECMALMTERRIRHLPVVEDGKLVGIVS 107
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 7-119 3.99e-17

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: 73.99  E-value: 3.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRD--VRdaspSILDEQvsiDMLQQPLELIMKHPVMT 84
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCE-GDRLVGMVTDRDivVR----AVAEGK---DPNTTTVREVMTGDVVT 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446557232  85 CHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIIS 119
Cdd:cd04622   73 CSPDDDVEEAARLMAEHQVRRLPVVdDDGRLVGIVS 108
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 3-124 5.24e-17

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: 73.80  E-value: 5.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVdQNNHVVGIISDRDV------RDASPSILDEQVSiDMLQQPLEL 76
Cdd:cd04631    2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDImrylgsGEAFEKLKTGNIH-EVLNVPISS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446557232  77 IMKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVL 124
Cdd:cd04631   80 IMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDIL 127
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 11-124 1.37e-16

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: 72.14  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  11 VVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPSildeqvsiDMLQQPLELIMKHPVMTCHPLDF 90
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLRYGHTGLPVVE-DGKLVGIISRRDVDKAKHH--------GLGHAPVKGYMSTNVITIDPDTS 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446557232  91 VEEIATLFFENKIGCLPVTKAGKLVGIISESTVL 124
Cdd:cd04595   75 LEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVL 108
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 8-124 1.49e-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: 72.75  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDEQVSID-------MLQQPLELIMKH 80
Cdd:cd04632    1 TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRGGDrggekerMLDLPVYDIMSS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446557232  81 PVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLV-GIISESTVL 124
Cdd:cd04632   81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMViGILTKTDVL 125
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 2-119 1.51e-16

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: 72.27  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVrdaSPSILDEQVSIDMlqqplelIMKHP 81
Cdd:cd04605    1 LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDI---SKAVALKKDSLEE-------IMTRN 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446557232  82 VMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIIS 119
Cdd:cd04605   71 VITARPDEPIELAARKMEKHNISALPVVdDDRRVIGIIT 109
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 7-119 9.27e-15

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: 67.55  E-value: 9.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDeqvsidmLQQPLELIMKHPVMTCH 86
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGID-------LDTPVEEIMTKNLVTVS 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446557232  87 PLDFVEEIATLFFENKIGCLPVTKA-GKLVGIIS 119
Cdd:cd09836   74 PDESIYEAAELMREHNIRHLPVVDGgGKLVGVIS 107
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 3-56 4.53e-14

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: 64.16  E-value: 4.53e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446557232    3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDA 56
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 6-118 4.95e-14

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: 65.82  E-value: 4.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   6 IMNQNVVTLHPNDTIETAIRTIRTKG-----IRHIPIVDQNNHVVGIISDRDVRDASPSildeqvsidmlqQPLELIMKH 80
Cdd:cd04606    6 LMTTEFVAVRPDWTVEEALEYLRRLApdpetIYYIYVVDEDRRLLGVVSLRDLLLADPD------------TKVSDIMDT 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446557232  81 PVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGII 118
Cdd:cd04606   74 DVISVSADDDQEEVARLFAKYDLLALPVVdEEGRLVGII 112
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 2-127 1.25e-13

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


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 65.33  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQ-NNHVVGIISDRDVRD-----ASPSILDEQVSIDML---QQ 72
Cdd:cd17779    1 SIMAIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADAgTKRLEGIVTSMDIVDflgggSKYNLVEKKHNGNLLaaiNE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446557232  73 PLELIMKHPVMTCHPLDFVEEIATLFFENKIGCLP-VTKAGKLVGIISESTVLHTL 127
Cdd:cd17779   81 PVREIMTRDVISVKENASIDDAIELMLEKNVGGLPiVDKDGKVIGIVTERDFLKFL 136
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 3-127 1.36e-13

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: 65.05  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV----------RDASPSILDEQVSIdmlqq 72
Cdd:cd17778    2 VKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIvkyfgsheakKRLTTGDIDEAYST----- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446557232  73 PLELIMKHPVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTL 127
Cdd:cd17778   76 PVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVdDEGELKGIITERDVLIAL 131
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 4-118 2.50e-13

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: 67.80  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232    4 EEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPsildeqvsidmLQQPLELIM-KHPV 82
Cdd:pfam00478  83 ESGMITDPVTLSPDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDLRFETD-----------LSQPVSEVMtKENL 150

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 446557232   83 MTCHPLDFVEEIATLFFENKIGCLP-VTKAGKLVGII 118
Cdd:pfam00478 151 VTAPEGTTLEEAKEILHKHKIEKLPvVDDNGRLVGLI 187
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 3-53 8.12e-13

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 62.26  E-value: 8.12e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd02205   61 VAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 3-58 8.54e-13

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: 62.54  E-value: 8.54e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASP 58
Cdd:cd09836   61 VEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 10-119 8.87e-13

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: 62.05  E-value: 8.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  10 NVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRdaspsildeqvSIDMLQQPLELIM-KHPVMTCHPL 88
Cdd:cd04601    3 DPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIR-----------FETDLSTPVSEVMtPDERLVTAPE 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446557232  89 DF-VEEIATLFFENKIGCLPVT-KAGKLVGIIS 119
Cdd:cd04601   72 GItLEEAKEILHKHKIEKLPIVdDNGELVGLIT 104
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-127 1.09e-12

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: 62.58  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIIS-----DRDVRDASPSILDEQVSIDMLQQPLEL----I 77
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTladllKHADLDPPRGLRGRLRRTLGLRRDRPEtvgdI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  78 MKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKA-GKLVGIISESTVLHTL 127
Cdd:cd04600   81 MTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDAdGRLVGIVTQSDLIAAL 131
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
6-118 1.16e-12

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 65.86  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   6 IMNQNVVTLHPNDTIETAIRTIRTKG-----IRHIPIVDQNNHVVGIISDRDVRDASPSildeqvsidmlqQPLELIMKH 80
Cdd:COG2239  134 LMTTEFVAVREDWTVGEALRYLRRQAedpetIYYIYVVDDDGRLVGVVSLRDLLLADPD------------TKVSDIMDT 201

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446557232  81 PVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGII 118
Cdd:COG2239  202 DVISVPADDDQEEVARLFERYDLLALPVVdEEGRLVGII 240
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 3-53 1.01e-11

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: 59.48  E-value: 1.01e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd17775   63 VGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 3-49 1.07e-11

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: 59.36  E-value: 1.07e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIIS 49
Cdd:cd04622   62 VREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVS 108
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 ...
 6-121 4.08e-11

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: 57.82  E-value: 4.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   6 IMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDaspSILDEQVSIDmlqQPLELIMKHPVMTC 85
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVD-DGRLVGIVTDRDLRN---RVVAEGLDPD---TPVSEIMTPPPVTI 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446557232  86 HPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISES 121
Cdd:cd04587   74 DADALVFEALLLMLERNIHHLPVVDDGRVVGVVTAT 109
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 5-126 5.57e-11

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: 57.58  E-value: 5.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   5 EIMNQNVVTLHPNDTIETAIRTIRTKgiRHI--PIVDqNNHVVGIISDRDVRDASPSildeqvsiDMLQQPLELIMKHPV 82
Cdd:cd04801    1 DIMTPEVVTVTPEMTVSELLDRMFEE--KHLgyPVVE-NGRLVGIVTLEDIRKVPEV--------EREATRVRDVMTKDV 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446557232  83 MTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLHT 126
Cdd:cd04801   70 ITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRTDLMRA 113
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 3-53 6.59e-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: 57.43  E-value: 6.59e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd04623   62 VSEIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVE-DGKLVGIVSIGDV 111
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 7-126 7.38e-11

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: 56.96  E-value: 7.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPSILdeqvSIDmlqqplelIMKHPVMTCH 86
Cdd:cd04599    1 MTRNPITISPLDSVARAAALMERQRIGGLPVVE-NGKLVGIITSRDVRRAHPNRL----VAD--------AMSRNVVTIS 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446557232  87 PLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLHT 126
Cdd:cd04599   68 PEASLWEAKELMEEHGIERLVVVEEGRLVGIITKSTLYLE 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 10-53 1.28e-10

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: 54.83  E-value: 1.28e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 446557232    10 NVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 3-48 1.55e-10

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: 56.30  E-value: 1.55e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGII 48
Cdd:cd04607   60 VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLE 105
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-53 7.86e-10

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: 55.13  E-value: 7.86e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd04586   85 VGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADL 134
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 7-124 1.29e-09

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: 53.86  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDASPsilDEQVSidmlqqpleLIMKHPVMTCH 86
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVD-DGKVVGYVTAKDLLGKDD---DEKVS---------EIMSRDTVVAD 67

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446557232  87 PLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVL 124
Cdd:cd04610   68 PDMDITDAARVIFRSGISKLPVVdDEGNLVGIITNMDVI 106
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 3-125 1.88e-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: 341393 [Multi-domain]  Cd Length: 120  Bit Score: 53.37  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNH-VVGIISDRDVRDAspsILDEQVSIDMLqqPLELIMKHP 81
Cdd:cd04630    1 VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVEKRHEHdAYGIVTYTDILKK---VIAEDRDPDLV--NVYEIMTKP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446557232  82 VMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLH 125
Cdd:cd04630   76 AISVSPDLDIKYAARLMARFNLKRAPVIENNELIGIVSMTDLVL 119
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 3-53 3.56e-09

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: 52.71  E-value: 3.56e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04610   55 VSEIMSRDTVVADPDMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDV 105
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 78-134 4.60e-09

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: 52.82  E-value: 4.60e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446557232  78 MKHPVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTLVKLTGAH 134
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVdDDGKLVGIVSEGDLLRREEPGTEPR 58
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 9-124 8.93e-09

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: 51.32  E-value: 8.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   9 QNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPsildeqvsidmlQQPLELIMKHPVMTCHPL 88
Cdd:cd04596    2 EETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKED------------DTPIEKVMTKNPITVKPK 69

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446557232  89 DFVEEIA-TLFFENkIGCLPVTKAG-KLVGIISESTVL 124
Cdd:cd04596   70 TSVASAAhMMIWEG-IELLPVVDENrKLLGVISRQDVL 106
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 7-127 9.19e-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: 51.77  E-value: 9.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDvrdaspsILDEQVS--IDMLQQPLELIMKHPVMT 84
Cdd:cd17775    1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRD-------IVVEVVAkgLDPKDVTVGDIMSADLIT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446557232  85 CHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTL 127
Cdd:cd17775   74 AREDDGLFEALERMREKGVRRLPVVdDDGELVGIVTLDDILELL 117
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-124 1.08e-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: 51.38  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDvrdaspsILDeQVSIDMLQQ--PLELIM 78
Cdd:cd04608    2 LIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGN-------LLS-SLLAGRAQPsdPVSKAM 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446557232  79 KHPVMTCHPLDFVEEIATlFFENKIGCLPVTKAGKLVGIISESTVL 124
Cdd:cd04608   74 YKQFKQVDLDTPLGALSR-ILERDHFALVVDGQGKVLGIVTRIDLL 118
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 8-125 1.29e-08

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 50.99  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDAspsildeqVSIDMLQQPLELIMKHPVMTCHP 87
Cdd:cd04588    1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVD-DGKLVGIVTLTDIAKA--------LAEGKENAKVKDIMTKDVITIDK 71

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446557232  88 LDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLH 125
Cdd:cd04588   72 DEKIYDAIRLMNKHNIGRLIVVdDNGKPVGIITRTDILK 110
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 3-48 1.90e-08

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: 50.80  E-value: 1.90e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGII 48
Cdd:cd04606   67 VSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGII 112
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 ...
 6-120 2.11e-08

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: 50.78  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   6 IMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDaspSILDEQVSidmLQQPLELIM-KHPVMT 84
Cdd:cd17771    1 LIRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLS---RVALPQID---LDAPISEVMtPDPVRL 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446557232  85 cHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIISE 120
Cdd:cd17771   75 -PPSASAFEAALLMAEHGFRHVCVVDNGRLVGVVSE 109
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-129 2.92e-08

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: 50.46  E-value: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIM--NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDAspsiLDEQVSIdmLQQPLELIM-K 79
Cdd:cd04604    5 VSDLMhtGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRA----LEKGLDI--LNLPAKDVMtR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  80 HPVmTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISestvLHTLVK 129
Cdd:cd04604   79 NPK-TISPDALAAEALELMEEHKITVLPVVdEDGKPVGILH----LHDLLR 124
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 1-53 7.12e-08

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: 49.65  E-value: 7.12e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd17777   81 EVVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDL 133
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 12-118 9.05e-08

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: 48.60  E-value: 9.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  12 VTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDAspsILdEQVSidmLQQPLELIMKHPVMTCHPLDFV 91
Cdd:cd04607    5 VLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRG---LL-KGLS---LDAPVEEVMNKNPITASPSTSR 77

                         90       100
                 ....*....|....*....|....*...
gi 446557232  92 EEIATLFFENKIGCLPVTKA-GKLVGII 118
Cdd:cd04607   78 EELLALMRAKKILQLPIVDEqGRVVGLE 105
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
3-70 1.07e-07

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 51.22  E-value: 1.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDaspsILDEQVSIDML 70
Cdd:COG2239  195 VSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVD----VIEEEATEDIL 258
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 2-53 1.24e-07

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: 48.73  E-value: 1.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNH--VVGIISDRDV 53
Cdd:cd04613   61 VVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDDDDPgkVLGMLSRRDV 114
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 9-124 1.54e-07

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: 49.01  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   9 QNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV----------RDASPSILDEQvSIDMLQQPLELIM 78
Cdd:cd17789    3 GKLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLlaldsisgrsQTDNNFPPADS-TWKTFNEVQKLLS 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446557232  79 KH------PVMTCHPLDF-----VEEIATLFFENKIGCLPVTKA-GKLVGIISESTVL 124
Cdd:cd17789   82 KTngkvvgDVMTPSPLVVrektnLEDAARILLETKFRRLPVVDSdGKLVGIITRGNVV 139
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 4-130 1.70e-07

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: 48.49  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   4 EEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNhVVGIISDRDVRD----ASPSILDEQVSIDML-----QQPL 74
Cdd:cd17777    5 MIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDENK-LEGILSARDLVSylggGCLFKIVESRHQGDLysalnREVV 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446557232  75 ELIMKHPVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISEstvlHTLVKL 130
Cdd:cd17777   84 ETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVdRDGRPVGIVTE----RDLVLY 136
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 7-119 2.40e-07

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: 47.72  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNH-VVGIISDRDVRDASPsilDEQVSidmlqqpleLIMKHPVMTC 85
Cdd:cd04638    1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKETGkLVGIVTRKDLLRNPD---EEQIA---------LLMSRDPITI 68

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446557232  86 HPLDFVEEIATLFFENKIGCLPVTKAGKLVGIIS 119
Cdd:cd04638   69 SPDDTLSEAAELMLEHNIRRVPVVDDDKLVGIVT 102
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 3-48 2.92e-07

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: 47.13  E-value: 2.92e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGII 48
Cdd:cd04583   56 VGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLV 101
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 3-124 3.27e-07

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 46.94  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTK-GIRHIPIVDqnnhVVGiISDRDVRDASPSilDEQVSIDMLqqplelimkhp 81
Cdd:COG3620    1 VRDLMSRDVVTVSPDDTLGEALRLMRKElGLSQLPVAE----LVG-VSQSDILRIESG--KRDPTVSTL----------- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446557232  82 vmtchpldfvEEIATLfFENKIGCLPVTKAGKLVGIISESTVL 124
Cdd:COG3620   63 ----------EKIAEA-LGKELSAVLVVDDGKLVGIITRRDLL 94
ACT pfam01842
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ...
 138-199 3.27e-07

ACT domain; This family of domains generally have a regulatory role. ACT domains are 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 ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5


Pssm-ID: 426468 [Multi-domain]  Cd Length: 66  Bit Score: 46.15  E-value: 3.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446557232  138 SQIEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQ-TMNPLKVIDALEA 199
Cdd:pfam01842   1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVdEEDLEEVLEALKK 63
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 3-53 3.69e-07

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: 47.05  E-value: 3.69e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd04629   64 VADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVE-DGKLVGQISRRDV 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 77-128 5.88e-07

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 46.75  E-value: 5.88e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446557232  77 IMKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKA-GKLVGIISESTVLHTLV 128
Cdd:COG2905    4 IMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDdGRLVGIITDRDLRRRVL 56
ACT_Bt0572_2 cd04882
C-terminal ACT domain of a novel protein composed of just two ACT domains; Included in this CD ...
 142-205 8.57e-07

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: 44.90  E-value: 8.57e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557232 142 IQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQTMNplKVIDALEAEGYRVL 205
Cdd:cd04882    4 VEVPDKPGGLHEILQILSEEGINIEYMYAFVEKKGGKALLIFRTEDIE--KAIEVLQERGVELV 65
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
3-52 9.86e-07

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 48.67  E-value: 9.86e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRD 52
Cdd:PRK14869  70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSD 119
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 6-124 1.07e-06

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: 46.50  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   6 IMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASpSILDEQVSIDML--------------- 70
Cdd:cd04614    1 YAGKGVVPVWDETPLPVALRAMRLANVPAAPVLDSEGKLVGIVTERDLIDVS-RIVESEEESGMSiaddedewswegird 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446557232  71 --------------QQPLELIMKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKA-GKLVGIISESTVL 124
Cdd:cd04614   80 vmslyyptsnvelpDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGeGDLAGMLRDVDLL 148
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 3-56 1.24e-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: 46.17  E-value: 1.24e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDA 56
Cdd:cd04632   74 VYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 12-121 1.42e-06

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 48.04  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  12 VTLHPNDTIETAIRTIRTKGIRHIPIVDQNNH---VVGIISDRDVRDASPSildeqvsidmlQQPLELIM---KHPVMTC 85
Cdd:PTZ00314 107 YVLSPNHTVADVLEIKEKKGFSSILITVDGKVggkLLGIVTSRDIDFVKDK-----------STPVSEVMtprEKLVVGN 175

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446557232  86 HPLDfVEEIATLFFENKIGCLP-VTKAGKLVGIISES 121
Cdd:PTZ00314 176 TPIS-LEEANEVLRESRKGKLPiVNDNGELVALVSRS 211
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 3-49 1.43e-06

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: 45.99  E-value: 1.43e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446557232   3 VEEIMNQNVVTLHPND--TIETAIRTIRTKGIRHIPIVDQNNHVVGIIS 49
Cdd:cd04620   81 IAEVMTQPVITLKESEfqDIFTVLSLLRQHQIRHLPIVDDQGQLVGLIT 129
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 8-127 1.71e-06

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: 45.20  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSildeqvsidmlQQPLELIMKHPVMTCHP 87
Cdd:cd04583    1 ITNPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNYRK-----------AKKVGEIMERDVFTVKE 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446557232  88 LDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTL 127
Cdd:cd04583   70 DSLLRDTVDRILKRGLKYVPVVdEQGRLVGLVTRASLVDIV 110
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
77-145 2.00e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 45.63  E-value: 2.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  77 IMKHPVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTLVKLTGAHQPSSQIEIQVK 145
Cdd:COG3448    7 IMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVE 76
ACT cd02116
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ...
 140-198 2.59e-06

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: 43.43  E-value: 2.59e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232 140 IEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQTMNPL-KVIDALE 198
Cdd:cd02116    1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLeKLLEALE 60
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-56 2.64e-06

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: 44.77  E-value: 2.64e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDA 56
Cdd:cd04596   53 TPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDENRKLLGVISRQDVLKA 108
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 77-129 2.69e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 43.36  E-value: 2.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446557232   77 IMKHPVMTCHPLDFVEEIATLFFENKIGCLPV-TKAGKLVGIISESTVLHTLVK 129
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVvDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_Thermoplasmatales cd17786
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 8-119 3.73e-06

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: 44.45  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV------RDASPSILdeqvsidmlqqPLELIMKHP 81
Cdd:cd17786    1 NKNFKTINWNATVFDAVKIMNENHLYGLVVKDDDGNYVGLISERSIikrfipRNVKPDEV-----------PVKLVMRKP 69

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446557232  82 VMTCHPLDFVEEIATLFFENKIG-CLPVTKAGKLVGIIS 119
Cdd:cd17786   70 IPKVKSDYDVKDVAAFLSENGLErCAVVDDNGRVVGIVT 108
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
3-124 4.47e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 46.36  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   3 VEEIMN-QNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPS--IL-D-----------EQVSI 67
Cdd:PRK14869 248 VSYIMTtEDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHLLSPVRKkvILvDhneksqavegiEEAEI 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446557232  68 dmlqqpLELIMKH---PVMTCHPLDFVEE--------IATLFFENKI-------GCLpvtkagkLVGIISEsTVL 124
Cdd:PRK14869 328 ------LEIIDHHrlgDIQTSNPIFFRNEpvgststiVARMYRENGIepspeiaGLL-------LAAILSD-TLL 388
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 5-123 4.85e-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: 4.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   5 EIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRD---ASPSILdeqvsidmlQQPLELIMKHP 81
Cdd:cd09833    1 RIVSTSLLTCSPDTPLADAAARMAERRCSSILIVE-NGEIVGIWTERDALKldfSDPDAF---------RRPISEVMSSP 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446557232  82 VMTCHPLDFVEEIATLFFENKIGCLPVTK-AGKLVGIISESTV 123
Cdd:cd09833   71 VLTIPQDTTLGEAAVRFRQEGVRHLLVVDdDGRPVGIVSQTDV 113
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 80-120 5.03e-06

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: 43.94  E-value: 5.03e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446557232  80 HPVMTCHPLDFVEEIATLFFENKIGCLPVTKA-GKLVGIISE 120
Cdd:cd04623    2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSE 43
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-53 9.81e-06

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: 43.70  E-value: 9.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04600   77 VGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDL 127
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 1-53 1.07e-05

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 43.37  E-value: 1.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd04631   75 VPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVD-DGKLVGIITERDI 126
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 1-53 1.48e-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: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 42.56  E-value: 1.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd04801   59 TRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVE-DGELVGIISRTDL 110
CBS_pair_ACT cd17787
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga ...
 8-128 1.75e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga in combination with an ACT 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: 341423 [Multi-domain]  Cd Length: 111  Bit Score: 42.40  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSildeqvsidmlqQPLELIMKHPVMTCHP 87
Cdd:cd17787    1 NRDFPTFEESATVGEVLHEMRKYETDYCIVVDEEGKFAGMVRKSKIMDEDLD------------KKVKEYVVEPDFYCHE 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446557232  88 LDFVEEIATLFFENKIGCLPVTKAG-KLVGIISESTVLHTLV 128
Cdd:cd17787   69 EDYIEDAALLLIESHEFVLPVVNSDmKVKGVLTVFEILEALM 110
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 3-53 2.16e-05

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: 42.41  E-value: 2.16e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKG-----IRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd17784   61 VEEVMVKDVATVHPDETLLEAIKKMDSNApdeeiINQLPVVD-DGKLVGIISDGDI 115
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 3-53 2.58e-05

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: 42.65  E-value: 2.58e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04614   97 VKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDL 147
CBS_pair_bac cd17783
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 8-124 3.07e-05

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: 41.79  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   8 NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVRDaspsILDEQVSIDMLqqPLELIMKHPVMTCHP 87
Cdd:cd17783    1 NPMIPPLKPTDSVEKALDWMEEFRVSQLPVVD-NGQYLGLISEDDLLE----LNDPEAPLSNL--PLSLKDVFVYEDQHF 73

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446557232  88 LDFVEeiatLFFENKIGCLPV-TKAGKLVGIISESTVL 124
Cdd:cd17783   74 YDVIR----LASEYKLEVVPVlDEENEYLGVITVNDLL 107
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
 3-51 3.74e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase; This CD contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase NeuB. NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). 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: 341409 [Multi-domain]  Cd Length: 118  Bit Score: 41.85  E-value: 3.74e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446557232   3 VEEIMNQNVVTLHPNDTIETaIRTIRTKGIRHIPIVDQNNHVVGIISDR 51
Cdd:cd17773   66 VSHVANTNFVSAPEGESPEK-IEALFSSRISYIPLVDERGRLVAVARKR 113
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 36-125 4.20e-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: 41.41  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  36 PIVDQNNHVVGIISDRDVRdaspSILDEQVSIDMLqqPLELIMKHPVMTCHPLDFVEEIATLFFENKIGCLPVTKA---G 112
Cdd:cd04613   30 PVVDEQGRLTGILSIQDVR----GVLFEEELWDLV--VVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDDddpG 103

                         90
                 ....*....|...
gi 446557232 113 KLVGIISESTVLH 125
Cdd:cd04613  104 KVLGMLSRRDVIA 116
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 2-119 4.29e-05

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: 41.35  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQN--NHVVGIISDRDVRDAspsildeqvsidmLQQPLelimk 79
Cdd:cd04591    1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTesQTLVGFILRSQLILL-------------LEADL----- 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446557232  80 HPVMTCHPLDFVEE-----IATLFfeNKIGC--LPVTKAGKLVGIIS 119
Cdd:cd04591   63 RPIMDPSPFTVTEEtslekVHDLF--RLLGLrhLLVTNNGRLVGIVT 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 81-127 4.51e-05

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: 39.80  E-value: 4.51e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 446557232    81 PVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTL 127
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLVGIVTRRDIIKAL 48
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 1-48 4.77e-05

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: 41.72  E-value: 4.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRtirtKGIRH--IPIVDQNNHVVGII 48
Cdd:cd04643   69 LKVEEVMNTDVPTVSPDDDLEEVLH----LLVDHpfLCVVDEDGYFLGII 114
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 10-119 5.35e-05

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: 40.79  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  10 NVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDEQVsidmlqqPLELIMKhpvmtchplD 89
Cdd:cd04597    6 KVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIARTVDYIMTKDN-------LIVFKED---------D 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446557232  90 FVEEIATLFFENKIGCLPVT-KAGKLVGIIS 119
Cdd:cd04597   70 YLDEVKEIMLNTNFRNYPVVdENNKFLGTIS 100
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 3-53 5.57e-05

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: 40.94  E-value: 5.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd04595   58 VKGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVE-EGKLVGIVTRSDV 107
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 79-128 5.63e-05

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: 41.08  E-value: 5.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  79 KHPVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTLV 128
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVdDDGKLVGIVTERDILRALV 51
ACTx2 COG4747
ACT domain-containing protein [General function prediction only];
96-202 7.51e-05

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


Pssm-ID: 443781 [Multi-domain]  Cd Length: 129  Bit Score: 40.89  E-value: 7.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  96 TLFFENKIGCLpvTKAGKL-----VGII-------SESTVLHTLV--------KLTGAHQPSSQIE---IQVKNEPGILG 152
Cdd:COG4747    4 SVFLENKPGRL--AEVTRLlgdagINIRalsiadtSDFGILRLIVddpekareVLKEAGFTVSETDvlaVELPDRPGGLA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557232 153 KVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQtmNPLKVIDALEAEGY 202
Cdd:COG4747   82 EILKALAEAGINIEYMYAFVGRPGGKAVLILRVD--DLEKAIEVLKENGI 129
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 ...
 3-53 7.58e-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: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 40.87  E-value: 7.58e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNhVVGIISDRDV 53
Cdd:cd04587   62 VSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDDGR-VVGVVTATDL 111
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 11-53 7.99e-05

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: 40.96  E-value: 7.99e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446557232  11 VVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04641   77 VHTCTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDI 119
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 10-127 8.68e-05

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: 40.87  E-value: 8.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  10 NVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDAspSILDEQVsidmLQQPLELIMKHPVMTCHPLD 89
Cdd:cd17784    3 NVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHN--LILDKYE----LGTTVEEVMVKDVATVHPDE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446557232  90 FV-EEIATL----FFENKIGCLPVTKAGKLVGIISESTVLHTL 127
Cdd:cd17784   77 TLlEAIKKMdsnaPDEEIINQLPVVDDGKLVGIISDGDIIRAI 119
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 5-130 1.36e-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: 40.16  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   5 EIMNQnVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDvrdaspsILdeQVSI---DMLQQPLELIM-KH 80
Cdd:cd04617    1 DIMSV-PVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKD-------LL--KATLggqDLEKTPVSMIMtRM 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446557232  81 P-VMTCHPLDFVEEIATLFFENKIGCLPVTKAG----KLVGIISESTVLHTLVKL 130
Cdd:cd04617   71 PnIVTVTPDDSVLEAARKLIEHEIDSLPVVEKEdgklKVVGRITKTNITRLFVEL 125
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 10-128 1.50e-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: 40.19  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  10 NVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV----RDASPSILDEQVsidmlQQPLELIMKHP--VM 83
Cdd:cd04641    4 NIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVinlaAEKTYNNLDLTV-----GEALQHRSEDFegVH 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446557232  84 TCHPLDFVEEIATLFFENKIGCLPVTKA-GKLVGIISESTVLHTLV 128
Cdd:cd04641   79 TCTLNDTLETIIDRIVKAEVHRLVVVDEeDRLEGIVSLSDILKYLV 124
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 3-49 1.66e-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: 1.66e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIIS 49
Cdd:cd17781   62 VSSVMTPNPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVLD 108
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 78-127 1.89e-04

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: 39.81  E-value: 1.89e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232  78 MKHPVMTCHPLDFVEEIATLFFENKIGCLPVT-KAGKLVGIISESTVLHTL 127
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVdDDGKPVGIVTERDIVRAV 51
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 3-53 1.91e-04

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: 39.51  E-value: 1.91e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd09833   63 ISEVMSSPVLTIPQDTTLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDV 113
CBS_pair_ABC_OpuCA_assoc cd04582
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 5-127 2.74e-04

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: 39.29  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   5 EIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDeqvsidmlqqpleliMKHPVMT 84
Cdd:cd04582    1 EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDARGASGTCGD---------------FAHPFKA 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446557232  85 CHPLDFVEEIA-TLFFENKIGCLPVTKA-GKLVGIISESTVLHTL 127
Cdd:cd04582   66 TVPVDENLRVVlSRMYEHNTSWLPVVDEdGRYAGEVTQDSIADYL 110
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 12-118 3.47e-04

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


Pssm-ID: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 38.86  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  12 VTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDEQVS--------IDMLQQPLELIMKhpvm 83
Cdd:cd04594    5 IKVSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDIENKSPGKVGKYVVrgspyvtpTSSLEEAWEIMMR---- 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446557232  84 tchpldfveeiatlffeNKIGCLPVTKAGKLVGII 118
Cdd:cd04594   81 -----------------NKSRWVAVVEKGKFLGII 98
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 6-53 5.60e-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: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 38.09  E-value: 5.60e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446557232   6 IMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNhVVGIISDRDV 53
Cdd:cd04638   60 LMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDK-LVGIVTVADL 106
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 80-119 6.76e-04

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: 37.86  E-value: 6.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446557232  80 HPVMTCHPLDFVEEIATLFFENKIGCLPVTKAGKLVGIIS 119
Cdd:cd04595    2 SPVKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIIS 41
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 ...
 3-53 7.23e-04

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: 38.07  E-value: 7.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDV 53
Cdd:cd17771   63 ISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVD-NGRLVGVVSERDL 112
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 5-54 7.26e-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: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 37.88  E-value: 7.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446557232   5 EIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDqNNHVVGIISDRDVR 54
Cdd:cd04591   64 PIMDPSPFTVTEETSLEKVHDLFRLLGLRHLLVTN-NGRLVGIVTRKDLL 112
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 ...
 12-124 7.66e-04

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: 37.94  E-value: 7.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  12 VTLHPNDTIETAIRTIRTKGIRHIpIVDQNNHVVGIISDRDVRDAspSILDEQvSIDMlqqPLELIMKHPVMTCHPLDFV 91
Cdd:cd04589    6 LFVDAETSIREATRLMKENGADSL-LVRDGDGRVGIVTRTDLRDA--VVLDGQ-PVDT---PVGEIATFPLISVEPDDFL 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446557232  92 EEIATLFFENKIGCLPVTKAGKLVGIISESTVL 124
Cdd:cd04589   79 FNALLLMTRHRVKRVVVREGEEIVGVLEQTDLL 111
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 3-53 7.88e-04

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: 39.68  E-value: 7.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446557232    3 VEEIM-NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:pfam00478 141 VSEVMtKENLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 3-53 1.18e-03

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: 37.39  E-value: 1.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446557232   3 VEEIM--NQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04601   56 VSEVMtpDERLVTAPEGITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDI 108
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 7-125 1.21e-03

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: 37.38  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232   7 MNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVvGIISDRDVRDASPSILDEQVSIdmlqqPLELIMKHPVMTCH 86
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERMLRNRVGSVVVTDDGTPA-GILTETDALHAGYATDDPFSEI-----PVRAVASRPLVTIS 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446557232  87 PLDFVEEIATLFFENKIGCLPVTKAGKLVGIISESTVLH 125
Cdd:cd17776   75 PTATLREAAERMVDEGVKKLPVVDGLDLVGILTATDIIR 113
ACT_Bt0572_1 cd04908
N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; ...
 139-204 1.48e-03

N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains; Included in this CD is the N-terminal ACT domain of a novel protein composed almost entirely of two tandem ACT domains as seen in the uncharacterized structure (pdb 2F06) of the Bt0572 protein from Bacteroides thetaiotaomicron and related ACT domains. These tandem ACT domain proteins belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153180  Cd Length: 66  Bit Score: 36.02  E-value: 1.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446557232 139 QIEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENdkvlVFRIQTMNPLKVIDALEAEGYRV 204
Cdd:cd04908    3 QLSVFLENKPGRLAAVTEILSEAGINIRALSIADTSEFG----ILRLIVSDPDKAKEALKEAGFAV 64
PRK07107 PRK07107
IMP dehydrogenase;
13-118 1.61e-03

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 38.91  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  13 TLHPNDTIETAIRTIRTKGIRHIPIVDQ---NNHVVGIISDRDVRDASPSiLDEQVSIDMlqQPLELIMKHPVMTChpld 89
Cdd:PRK07107 109 NLTPDNTLADVLDLKEKTGHSTVAVTEDgtaHGKLLGIVTSRDYRISRMS-LDTKVKDFM--TPFEKLVTANEGTT---- 181

                         90       100       110
                 ....*....|....*....|....*....|
gi 446557232  90 fVEEIATLFFENKIGCLP-VTKAGKLVGII 118
Cdd:PRK07107 182 -LKEANDIIWDHKLNTLPiVDKNGNLVYLV 210
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 3-53 2.24e-03

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: 36.36  E-value: 2.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04588   58 VKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDI 108
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 2-53 3.29e-03

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: 36.68  E-value: 3.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446557232   2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd17789   87 VVGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNV 138
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 1-53 3.41e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 2; 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: 341384 [Multi-domain]  Cd Length: 131  Bit Score: 36.55  E-value: 3.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446557232   1 MIVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04611   67 TPVGELASRPLLTVGAEDSLIHARDLLIDHRIRHLAVVDEDGQVTGLLGFADL 119
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 2-63 5.98e-03

Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 129495 [Multi-domain]  Cd Length: 449  Bit Score: 37.11  E-value: 5.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446557232    2 IVEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDVRDASPSILDE 63
Cdd:TIGR00400 196 ILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSEATE 257
GcvR COG2716
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
124-200 6.32e-03

Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];


Pssm-ID: 442029 [Multi-domain]  Cd Length: 174  Bit Score: 35.97  E-value: 6.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232 124 LHTLVKLTGAHQPSSQ-----IEIQVKNEPGILGKVVAIFSDLQINIV--SVLVYPAKDENDKVLVFRIQTMNPLKV-ID 195
Cdd:COG2716   72 LLVTVKRTEPHEAPPAglpyvVEVVGNDRPGIVAEVTQFLAERGINIEdlSTKTYPAPMSGTPLFSAQITVHVPAGLdID 151


                 ....*
gi 446557232 196 ALEAE 200
Cdd:COG2716  152 ALRDA 156
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 12-53 6.57e-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: 35.62  E-value: 6.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446557232  12 VTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:cd04640    8 VTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDI 49
ACT_HSDH-Hom cd04881
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ...
 140-210 6.67e-03

ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains.


Pssm-ID: 153153 [Multi-domain]  Cd Length: 79  Bit Score: 34.41  E-value: 6.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446557232 140 IEIQVKNEPGILGKVVAIFSDLQINIVSVLVYPAKDENDKVLVFRIQTMNP---LKVIDALEAEGYRVLWPNIM 210
Cdd:cd04881    3 LRLTVKDKPGVLAKITGILAEHGISIESVIQKEADGGETAPVVIVTHETSEaalNAALAEIEALDAVQGVPSVI 76
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 37-125 6.75e-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: 35.59  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446557232  37 IVDQNNHVVGIISDRD-VRDASPSILDEQVSIdmlqqplELIMKHPVMTCHPLDF--VEEIATLFFENKIGCLP-VTKAG 112
Cdd:cd04620   50 LVVENQQLVGIFTERDvVRLTASGIDLSGVTI-------AEVMTQPVITLKESEFqdIFTVLSLLRQHQIRHLPiVDDQG 122

                         90
                 ....*....|...
gi 446557232 113 KLVGIISESTVLH 125
Cdd:cd04620  123 QLVGLITPESLRQ 135
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 3-56 8.29e-03

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


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 35.07  E-value: 8.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446557232   3 VEEIMNQNVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNhVVGIISDRDVRDA 56
Cdd:cd17776   62 VRAVASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLD-LVGILTATDIIRA 114
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 3-53 9.62e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 36.49  E-value: 9.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446557232   3 VEEIMNQ--NVVTLHPNDTIETAIRTIRTKGIRHIPIVDQNNHVVGIISDRDV 53
Cdd:PTZ00314 161 VSEVMTPreKLVVGNTPISLEEANEVLRESRKGKLPIVNDNGELVALVSRSDL 213
 
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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