NCBI Conserved Domain Search

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: 139.97 E-value: 7.00e-44

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKAcAEGKVEDIMSRNPIVASPDDDLE 98
Cdd:cd09836   1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGID-LDTPVEEIMTKNLVTVSPDESIY 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 5103661   99 IIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd09836  80 EAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 125.36 E-value: 5.19e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   13 LKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLAS-GKACAEGKVEDIMSRNPIVA 91
Cdd:COG0517   1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAeGKDLLDTPVSEVMTRPPVTV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 5103661   92 SPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDLGVSAL 138
Cdd:COG0517  81 SPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPL 127

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 123.79 E-value: 2.18e-37

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   15 AKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINS-LASGKACAEGKVEDIMSRNPIVASP 93
Cdd:COG2905   1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRvLAEGLDPLDTPVSEVMTRPPITVSP 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 5103661   94 DDDLEIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDII 131
Cdd:COG2905  81 DDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLL 117

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: 116.75 E-value: 8.82e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDI-INSLASGKACAEGKVEDIMSRNPIVASPDDDL 97
Cdd:cd04622   1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLV-GMVTDRDIvVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDV 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 5103661   98 EIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04622  80 EEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 119.60 E-value: 9.04e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661    5 KRYMRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLASGKACAEGKVEDIM 84
Cdd:COG2524  78 KELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLV-GIITERDLLKALAEGRDLLDAPVSDIM 156

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 5103661   85 SRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:COG2524 157 TRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204

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: 116.36 E-value: 1.08e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   24 VTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLAS-GKACAEGKVEDIMSRNPIVASPDDDLEIIIE 102
Cdd:cd04623   5 VTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALrGASSLDTPVSEIMTRDVVTCTPDDTVEECMA 84

                        90       100
                ....*....|....*....|....*....
gi 5103661  103 KMRDMNIRHIPVIDeDGRPLGMISVRDII 131
Cdd:cd04623  85 LMTERRIRHLPVVE-DGKLVGIVSIGDVV 112

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 117.27 E-value: 1.25e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   13 LKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGK------ACAEGKVEDIMSR 86
Cdd:COG3448   2 MTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRldeleeRLLDLPVEDVMTR 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 5103661   87 NPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:COG3448  82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLL 126

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

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 114.26 E-value: 7.76e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   20 STPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRNPIVASPDDDLEI 99
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEE 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 5103661  100 IIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd02205  81 ALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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: 106.47 E-value: 1.00e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDI-INSLASGKACAEGKVEDIMSRNPIVASPDDDL 97
Cdd:cd17775   1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIvVEVVAKGLDPKDVTVGDIMSADLITAREDDGL 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5103661   98 EIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:cd17775  81 FEALERMREKGVRRLPVVDDDGELVGIVTLDDILEL 116

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: 100.96 E-value: 1.24e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLASGKACAEGKVEDIMSRNPIVASPDDdl 97
Cdd:cd04587   1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLV-GIVTDRDLRNRVVAEGLDPDTPVSEIMTPPPVTIDADA-- 77

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5103661   98 eIIIEKMRDM---NIRHIPVIDeDGRPLGMISVRDII 131
Cdd:cd04587  78 -LVFEALLLMlerNIHHLPVVD-DGRVVGVVTATDLM 112

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 94.98 E-value: 7.19e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   13 LKAKHVMSTP-PVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINslasgkACAEGKVEDIMSRNPIVA 91
Cdd:COG4109  16 LLVEDIMTLEdVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG------KDDDTPIEDVMTKNPITV 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5103661   92 SPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:COG4109  90 TPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129

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: 93.84 E-value: 9.21e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACaegkVEDIMSRNPIVASPDDDL 97
Cdd:cd04605   5 IMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALKKDS----LEEIMTRNVITARPDEPI 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 5103661   98 EIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04605  81 ELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113

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

Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 94.41 E-value: 9.35e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   16 KHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLAS----------GKACAEGKVEDIMS 85
Cdd:cd04584   3 KDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLV-GIVTDRDLLRASPSkatslsiyelNYLLSKIPVKDIMT 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 5103661   86 RNPIVASPDDDLEIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDIIDL 133
Cdd:cd04584  82 KDVITVSPDDTVEEAALLMLENKIGCLPVVD-GGKLVGIITETDILRA 128

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: 94.42 E-value: 1.06e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASG-----------------------KAC 75
Cdd:cd04586   1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGteprrvwwldallesperlaeeyVKA 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5103661   76 AEGKVEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDII 131
Cdd:cd04586  81 HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLL 135

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: 85.86 E-value: 2.85e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKqGLVKGILTERDIINSLASGK------ACAEG---------KVED 82
Cdd:cd17777   7 IASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDE-NKLEGILSARDLVSYLGGGClfkiveSRHQGdlysalnreVVET 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   83 IMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd17777  86 IMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134

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: 80.17 E-value: 2.12e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGK--ACAEGKVEDIMSRNPIVASPDDD 96
Cdd:cd04629   1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASyhCEPGGTVADYMSTEVLTVSPDTS 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 5103661   97 LEIIIEKMRDMNIRHIPVIdEDGRPLGMISVRDII 131
Cdd:cd04629  81 IVDLAQLFLKNKPRRYPVV-EDGKLVGQISRRDVL 114

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: 78.40 E-value: 1.37e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   22 PPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINS-LASGKACAEGKVEDIMSRNPIVASPDDDLEII 100
Cdd:cd17781   3 PALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRvVASGLDPRSTLVSSVMTPNPLCVTMDTSATDA 82

                        90       100
                ....*....|....*....|....*..
gi 5103661  101 IEKMRDMNIRHIPVIDEDGRPLGMISV 127
Cdd:cd17781  83 LDLMVEGKFRHLPVVDDDGDVVGVLDI 109

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: 77.38 E-value: 2.01e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLASgkacaeGKVEDIMSRNPIVASPDDDLE 98
Cdd:cd04599   1 MTRNPITISPLDSVARAAALMERQRIGGLPVVENGKLV-GIITSRDVRRAHPN------RLVADAMSRNVVTISPEASLW 73

                        90       100       110
                ....*....|....*....|....*....|...
gi 5103661   99 IIIEKMRDMNIRHIPVIdEDGRPLGMISVRDII 131
Cdd:cd04599  74 EAKELMEEHGIERLVVV-EEGRLVGIITKSTLY 105

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: 77.57 E-value: 2.07e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   20 STPPVTIEVGRSIAEAARLMAERGVGSLIVVDKqGLVKGILTERDIINSLASGKAcaEGKVEDIMSRNPIVASPDDDLEI 99
Cdd:cd04588   1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDD-GKLVGIVTLTDIAKALAEGKE--NAKVKDIMTKDVITIDKDEKIYD 77

                        90       100       110
                ....*....|....*....|....*....|....
gi 5103661  100 IIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:cd04588  78 AIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111

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: 76.40 E-value: 4.85e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   23 PVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKacaegKVEDIMSRNPIVASPDDDLEIIIE 102
Cdd:cd04583   4 PVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNYRKAK-----KVGEIMERDVFTVKEDSLLRDTVD 78

                        90       100
                ....*....|....*....|...
gi 5103661  103 KMRDMNIRHIPVIDEDGRPLGMI 125
Cdd:cd04583  79 RILKRGLKYVPVVDEQGRLVGLV 101

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: 76.83 E-value: 6.11e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDII---------------NSLASGKACAEGKVEDI 83
Cdd:cd04600   1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLkhadldpprglrgrlRRTLGLRRDRPETVGDI 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 5103661   84 MSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd04600  81 MTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128

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: 74.67 E-value: 5.12e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   14 KAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDkQGLVKGILTERDIINSLASGKACAEG-----------KVED 82
Cdd:cd17778   1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVKYFGSHEAKKRLttgdideaystPVEE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   83 IMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd17778  80 IMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128

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

Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 73.34 E-value: 1.94e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVV------DKQGLV-KGILTERDIINSLASGKACAEGKVEDIMSRNPIV 90
Cdd:cd17774   2 VMTTRVIHAPPTASVLELAQLMAEHRVSCVVIVeedeqqEKNKLIpVGIVTERDIVQFQALGLDLSQTQAQTVMSSPLFS 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5103661   91 ASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd17774  82 LRPDDSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSL 121

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: 71.71 E-value: 3.77e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   24 VTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACaEGKVEDIMSRNPIVASPDDDLEIIIEK 103
Cdd:cd04607   5 VLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGLLKGLSL-DAPVEEVMNKNPITASPSTSREELLAL 83

                        90       100
                ....*....|....*....|....*...
gi 5103661  104 MRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd04607  84 MRAKKILQLPIVDEQGRVVGLETLDDLL 111

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: 72.19 E-value: 4.14e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   23 PVTIEVGRSIAEAARLMA----------------ERGVGSLIVVDKQGLVkGILTERDIINSLASGKACAEGKVEDIMSR 86
Cdd:cd04620   9 PLTVSPDTPVIEAIALMSqtrssccllsedsiitEARSSCVLVVENQQLV-GIFTERDVVRLTASGIDLSGVTIAEVMTQ 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 5103661   87 NPI--VASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMIS 126
Cdd:cd04620  88 PVItlKESEFQDIFTVLSLLRQHQIRHLPIVDDQGQLVGLIT 129

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: 75.50 E-value: 9.14e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661     14 KAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLASGKacaegKVEDIMSR-NPIVAS 92
Cdd:pfam00478  81 RSESGMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLV-GIVTNRDLRFETDLSQ-----PVSEVMTKeNLVTAP 154

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 5103661     93 PDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:pfam00478 155 EGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192

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

Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 70.52 E-value: 1.19e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   23 PVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSlasgkACAEGKVEDIMSRN--PIVASPDDDLEII 100
Cdd:cd04601   4 PVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFE-----TDLSTPVSEVMTPDerLVTAPEGITLEEA 78

                        90       100       110
                ....*....|....*....|....*....|
gi 5103661  101 IEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04601  79 KEILHKHKIEKLPIVDDNGELVGLITRKDI 108

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

Pssm-ID: 341418 [Multi-domain] Cd Length: 118 Bit Score: 69.97 E-value: 1.91e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   20 STPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDII-NSLASGKACAEGKVEDIMSRNPIVASPDDDLE 98
Cdd:cd17782   1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVlRVLAAGLDPATTSVVRVMTPNPETAPPSTTIL 80

                        90       100
                ....*....|....*....|....*....
gi 5103661   99 IIIEKMRDMNIRHIPVIDEDGRPLGMISV 127
Cdd:cd17782  81 DALHKMHEGKFLNLPVVDDEGEIVGLVDV 109

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 69.51 E-value: 5.41e-16

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5103661   79 KVEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:COG3448   3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLR 56

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: 68.52 E-value: 5.61e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQ-GLVKGILTERDIINSLAsgkacaEGKVEDIMSRNPIVASPDDDL 97
Cdd:cd04638   1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKEtGKLVGIVTRKDLLRNPD------EEQIALLMSRDPITISPDDTL 74

                        90       100       110
                ....*....|....*....|....*....|....
gi 5103661   98 EIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDII 131
Cdd:cd04638  75 SEAAELMLEHNIRRVPVVD-DDKLVGIVTVADLV 107

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: 68.53 E-value: 5.66e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   23 PVTIEVgrSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSlasgkacaegkVEDIMSR-NPIVASPDDDLEIII 101
Cdd:cd04597   9 PLSPET--SIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIART-----------VDYIMTKdNLIVFKEDDYLDEVK 75

                        90       100       110
                ....*....|....*....|....*....|.
gi 5103661  102 EKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd04597  76 EIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106

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: 68.78 E-value: 6.29e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   15 AKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDK-QGLVKGILTERDIINS-LASGKACAEGKVEDIMSRNPIVAS 92
Cdd:cd04630   1 VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVEKRhEHDAYGIVTYTDILKKvIAEDRDPDLVNVYEIMTKPAISVS 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5103661   93 PDDDLEIIIEKMRDMNIRHIPVIdEDGRPLGMISVRDII 131
Cdd:cd04630  81 PDLDIKYAARLMARFNLKRAPVI-ENNELIGIVSMTDLV 118

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: 68.90 E-value: 6.66e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGS-----LIVVDKQGLVKGILTERDIInsLASGKAcaegKVEDIMSRNPIVAS 92
Cdd:cd04606   6 LMTTEFVAVRPDWTVEEALEYLRRLAPDPetiyyIYVVDEDRRLLGVVSLRDLL--LADPDT----KVSDIMDTDVISVS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5103661   93 PDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd04606  80 ADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLD 119

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: 68.18 E-value: 1.26e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   13 LKAKHVMST----PPVTIEVgrSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRNP 88
Cdd:cd04604   3 LRVSDLMHTgdelPLVSPDT--SLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNLPAKDVMTRNP 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 5103661   89 IVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd04604  81 KTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHDLL 123

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 72.02 E-value: 1.37e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERG-----VGSLIVVDKQGLVKGILTERDIInsLASGKAcaegKVEDIMSRNPIVAS 92
Cdd:COG2239 134 LMTTEFVAVREDWTVGEALRYLRRQAedpetIYYIYVVDDDGRLVGVVSLRDLL--LADPDT----KVSDIMDTDVISVP 207

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5103661   93 PDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:COG2239 208 ADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVD 247

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: 68.41 E-value: 1.38e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVdKQGLVKGILTERDIINSLASGKACAEGK-----------VEDIMSRN 87
Cdd:cd04631   6 MTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIMRYLGSGEAFEKLKtgnihevlnvpISSIMKRD 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 5103661   88 PIVASPDDDLEIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDII 131
Cdd:cd04631  85 IITTTPDTDLGEAAELMLEKNIGALPVVD-DGKLVGIITERDIL 127

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: 67.34 E-value: 2.00e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   23 PVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRNPIVASPDDDLEIIIE 102
Cdd:cd17771   6 PVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIDLDAPISEVMTPDPVRLPPSASAFEAAL 85

                        90       100       110
                ....*....|....*....|....*....|.
gi 5103661  103 KMRDMNIRHIPVIDeDGRPLGMISVRDIIDL 133
Cdd:cd17771  86 LMAEHGFRHVCVVD-NGRLVGVVSERDLFSL 115

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: 67.22 E-value: 2.54e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRNPIVASPDDDLE 98
Cdd:cd04613   1 MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEELWDLVVVKDLATTDVITVTPDDDLY 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 5103661   99 IIIEKMRDMNIRHIPVIDED--GRPLGMISVRDII 131
Cdd:cd04613  81 TALLKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVI 115

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: 67.36 E-value: 3.09e-15

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5103661   14 KAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL 69
Cdd:cd17778  76 PVEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131

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: 63.77 E-value: 1.14e-14

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 5103661     80 VEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54

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

Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 65.21 E-value: 1.22e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   20 STPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLASGKACAegKVEDIMSRNPIVASPDDDLEI 99
Cdd:cd04595   1 SSPVKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLV-GIISRRDVDKAKHHGLGHA--PVKGYMSTNVITIDPDTSLEE 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 5103661  100 IIEKMRDMNIRHIPVIdEDGRPLGMISVRDII 131
Cdd:cd04595  78 AQELMVEHDIGRLPVV-EEGKLVGIVTRSDVL 108

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: 65.12 E-value: 1.37e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDkQGLVKGILTERDIINSLASGKAC-AEGKVEDIMSRNPIVASPDDDL 97
Cdd:cd17776   1 MTTDVVTVDADASLEDAAERMLRNRVGSVVVTD-DGTPAGILTETDALHAGYATDDPfSEIPVRAVASRPLVTISPTATL 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 5103661   98 EIIIEKMRDMNIRHIPVIDEDgRPLGMISVRDIID 132
Cdd:cd17776  80 REAAERMVDEGVKKLPVVDGL-DLVGILTATDIIR 113

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 63.35 E-value: 1.41e-13

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5103661    6 RYMRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLA 70
Cdd:COG3448  66 LEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130

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

Pssm-ID: 341403 [Multi-domain] Cd Length: 116 Bit Score: 62.24 E-value: 2.24e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDkQGLVKGILTERDiinSLA---SGKACAEGKVEDIMSRnPIVASP- 93
Cdd:cd09833   2 IVSTSLLTCSPDTPLADAAARMAERRCSSILIVE-NGEIVGIWTERD---ALKldfSDPDAFRRPISEVMSS-PVLTIPq 76

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 5103661   94 DDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd09833  77 DTTLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDVV 114

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

Pssm-ID: 341408 [Multi-domain] Cd Length: 112 Bit Score: 61.81 E-value: 3.16e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   20 STPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQ-GLVKGILTERDIinslasGKACAEG----KVEDIMSRNPIVASPD 94
Cdd:cd17772   1 SSPVISVEPDTTIAEAAELMTRYNINALPVVDGGtGRLVGIITRQVA------EKAIYHGlgdlPVSEYMTTEFATVTPD 74

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5103661   95 DDLEIIIEKMRDMNIRHIPVIdEDGRPLGMISVRDII 131
Cdd:cd17772  75 APLSEIQEIIVEQRQRLVPVV-EDGRLVGVITRTDLL 110

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: 61.25 E-value: 4.57e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIinslasgkACAEGKVEDIMSRNPIVASPDDDL 97
Cdd:cd04582   2 DAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDA--------RGASGTCGDFAHPFKATVPVDENL 73

                        90       100       110
                ....*....|....*....|....*....|....*
gi 5103661   98 EIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd04582  74 RVVLSRMYEHNTSWLPVVDEDGRYAGEVTQDSIAD 108

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: 61.58 E-value: 4.70e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   12 RLK-AKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIV-VDKQGLvkGILTERDIINSLASGKACAegKVEDIMSRNPI 89
Cdd:cd04611   3 RLReVGSAMNRSPLVLPGDASLAEAARRMRSHRADAAVIeCPDGGL--GILTERDLVRFIARHPGNT--PVGELASRPLL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 5103661   90 VASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd04611  79 TVGAEDSLIHARDLLIDHRIRHLAVVDEDGQVTGLLGFADLLA 121

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: 61.48 E-value: 6.19e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   16 KHVMSTPPVTievgrSIAEAARLMAERGVGSLIVVDK-QGLVKGILTERDIINSLASGK--------------ACAEGKV 80
Cdd:cd17779   8 KDVITIPPTT-----TIIGAIKTMTEKGFRRLPVADAgTKRLEGIVTSMDIVDFLGGGSkynlvekkhngnllAAINEPV 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 5103661   81 EDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:cd17779  83 REIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKF 135

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 60.65 E-value: 1.04e-12

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5103661    3 VFKRYMRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKA 74
Cdd:COG0517  57 LAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128

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: 59.64 E-value: 1.51e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKqGLVKGILTERDIInslasgKACAEGKVEDIMSRNPIVASPDDDLE 98
Cdd:cd04610   1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDD-GKVVGYVTAKDLL------GKDDDEKVSEIMSRDTVVADPDMDIT 73

                        90       100       110
                ....*....|....*....|....*....|...
gi 5103661   99 IIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd04610  74 DAARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 57.92 E-value: 1.00e-11

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5103661    3 VFKRYMRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLAS 71
Cdd:COG2905  55 VLAEGLDPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDGKLV-GIVSITDLLRALSE 122

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: 57.93 E-value: 1.01e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   22 PPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRNPIVASPDDDLEIII 101
Cdd:cd04608  11 APVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQVDLDTPLGALS 90

                        90       100       110
                ....*....|....*....|....*....|.
gi 5103661  102 EKMrDMNIRHIpVIDEDGRPLGMISVRDIID 132
Cdd:cd04608  91 RIL-ERDHFAL-VVDGQGKVLGIVTRIDLLN 119

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: 57.58 E-value: 1.06e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   31 SIAEAARLMAERGVGSLIVVDkQGLVKGILTERDIINSLASgkacaEGKVEDIM-SRNPIVASPDDDLEIIIEKMRDMNI 109
Cdd:cd17783  12 SVEKALDWMEEFRVSQLPVVD-NGQYLGLISEDDLLELNDP-----EAPLSNLPlSLKDVFVYEDQHFYDVIRLASEYKL 85

                        90       100
                ....*....|....*....|..
gi 5103661  110 RHIPVIDEDGRPLGMISVRDII 131
Cdd:cd17783  86 EVVPVLDEENEYLGVITVNDLL 107

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: 57.82 E-value: 1.38e-11

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5103661   79 KVEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDIID 132
Cdd:cd04584   1 LVKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLR 53

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: 57.82 E-value: 1.49e-11

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5103661   12 RLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSL 69
Cdd:cd04584  73 KIPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLV-GIITETDILRAF 129

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: 55.60 E-value: 1.56e-11

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 5103661      87 NPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 59.13 E-value: 1.59e-11

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5103661   13 LKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL 69
Cdd:COG2524 150 APVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206

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

Pssm-ID: 341368 [Multi-domain] Cd Length: 128 Bit Score: 57.76 E-value: 1.61e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGK----VEDIMSRN------P 88
Cdd:cd04592   1 MSTRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIQRFLKRAKADNEDPktilVSSICTRNggycrgL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   89 IVASPDDDLEIIIEKMRDMNIRHIPVIDED-----GRPLGMISvRDIID 132
Cdd:cd04592  81 WTCTPDMDLLTAKMLMEARGINQLPVVKRGgeerrRRVVGLLD-RDSID 128

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: 56.71 E-value: 2.53e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   22 PPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINslasgkACAEGKVEDIMSRNPIVASPDDDLEIII 101
Cdd:cd04596   3 ETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIG------KEDDTPIEKVMTKNPITVKPKTSVASAA 76

                        90       100       110
                ....*....|....*....|....*....|
gi 5103661  102 EKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd04596  77 HMMIWEGIELLPVVDENRKLLGVISRQDVL 106

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: 54.91 E-value: 3.18e-11

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 5103661     15 AKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLAS 71
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

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: 56.42 E-value: 3.41e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLM-AERGVGsLIVVDKQGLVkGILTERDIINslASGKACAEGKVEDIMSRNPIVASPDDD 96
Cdd:cd04801   2 IMTPEVVTVTPEMTVSELLDRMfEEKHLG-YPVVENGRLV-GIVTLEDIRK--VPEVEREATRVRDVMTKDVITVSPDAD 77

                        90       100       110
                ....*....|....*....|....*....|....*
gi 5103661   97 LEIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDII 131
Cdd:cd04801  78 AMEALKLMSQNNIGRLPVVE-DGELVGIISRTDLM 111

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 59.46 E-value: 3.71e-11

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5103661    79 KVEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:PRK14869  69 QVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDL 120

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

Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 56.19 E-value: 4.77e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   23 PVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEG-------------KVEDIMSRNPI 89
Cdd:cd04632   4 VITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRGgdrggekermldlPVYDIMSSPVV 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 5103661   90 VASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd04632  84 TVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126

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: 55.57 E-value: 1.03e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   18 VMStPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRNP--IVASPDD 95
Cdd:cd04617   2 IMS-VPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPniVTVTPDD 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 5103661   96 DLEIIIEKMRDMNIRHIPVIDEDGRPL---GMISVRDIidlgvsaLKLFVE 143
Cdd:cd04617  81 SVLEAARKLIEHEIDSLPVVEKEDGKLkvvGRITKTNI-------TRLFVE 124

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: 54.94 E-value: 1.11e-10

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5103661   13 LKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIIN 67
Cdd:cd02205  59 TPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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

Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 54.45 E-value: 2.33e-10

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5103661    9 RSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLA 70
Cdd:cd09836  55 IDLDTPVEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116

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: 53.16 E-value: 5.19e-10

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   82 DIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04582   1 EDAATPTPTVRPSTPLSDALGIMDDADSRYLVVVDADGRPLGYVTRRDA 49

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: 52.95 E-value: 1.13e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   21 TPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIIN------SLASGKACAEGKVEDIM-SRNPIVASP 93
Cdd:cd04640   5 VPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGekplkiVQERGIPREELLVADVMtPRDKLEALD 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 5103661   94 DDDLEI-----IIEKMRDMNIRHIPVIDEDGRP----LGMISVRDI 130
Cdd:cd04640  85 YEDVAHarvgdVVETLKASGRQHALVVDRDEDGrqevRGIFSASQI 130

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 52.61 E-value: 1.38e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5103661   11 PRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL 69
Cdd:COG4109  74 DDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132

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: 52.04 E-value: 1.72e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   23 PVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRNPIVASPDDDLEIIIE 102
Cdd:cd17784   4 VITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKYELGTTVEEVMVKDVATVHPDETLLEAIK 83

                        90       100       110
                ....*....|....*....|....*....|....
gi 5103661  103 KMRDMN-----IRHIPVIDeDGRPLGMISVRDII 131
Cdd:cd17784  84 KMDSNApdeeiINQLPVVD-DGKLVGIISDGDII 116

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: 49.82 E-value: 2.72e-09

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 5103661      22 PPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLA 70
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49

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: 51.19 E-value: 5.18e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL 69
Cdd:cd17777  86 IMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL 137

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: 50.89 E-value: 5.98e-09

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5103661    3 VFKRYMRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDkQGLVKGILTERDII 66
Cdd:cd04586  73 LAEEYVKAHGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLL 135

GuaB1 family IMP dehydrogenase-related protein;

Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 52.60 E-value: 8.94e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661    12 RLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDiinslasgkaCAE----GKVEDIMSRN 87
Cdd:PRK07807  88 WVKSRDLVFDTPVTLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEAD----------CAGvdrfTQVRDVMSTD 157

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 5103661    88 PIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMIS 126
Cdd:PRK07807 158 LVTLPAGTDPREAFDLLEAARVKLAPVVDADGRLVGVLT 196

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: 49.84 E-value: 9.74e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5103661   11 PRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINS 68
Cdd:cd04588  54 ENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111

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: 49.85 E-value: 9.94e-09

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5103661   13 LKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL 69
Cdd:cd17775  61 VTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117

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

Pssm-ID: 341394 [Multi-domain] Cd Length: 130 Bit Score: 49.92 E-value: 1.23e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSL 69
Cdd:cd04631  80 IMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLV-GIITERDILRAI 130

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: 48.72 E-value: 2.57e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   22 PPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINSLASGKACAEGKVEDIMSRNPIVASPDDDLEIII 101
Cdd:cd04589   4 PPLFVDAETSIREATRLMKENGADSLLVRDGDGRV-GIVTRTDLRDAVVLDGQPVDTPVGEIATFPLISVEPDDFLFNAL 82

                        90       100
                ....*....|....*....|....*....
gi 5103661  102 EKMRDMNIRHIPVIdEDGRPLGMISVRDI 130
Cdd:cd04589  83 LLMTRHRVKRVVVR-EGEEIVGVLEQTDL 110

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: 48.78 E-value: 2.58e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5103661   85 SRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDLGVSALKL 140
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLA 56

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 49.14 E-value: 3.01e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5103661   79 KVEDIM-SRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:COG4109  17 LVEDIMtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG 71

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: 48.77 E-value: 3.78e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5103661   16 KHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL 69
Cdd:cd17779  83 REIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136

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: 49.20 E-value: 4.14e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   35 AARLMAERGVGSLIVVDKQGLVKGILTERDIIN---------SLASGKACAEGK-------------------------V 80
Cdd:cd04614  18 ALRAMRLANVPAAPVLDSEGKLVGIVTERDLIDvsriveseeESGMSIADDEDEwswegirdvmslyyptsnvelpdkpV 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 5103661   81 EDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd04614  98 KDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDLL 148

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: 48.30 E-value: 4.61e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 5103661   79 KVEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd04608   3 IVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLS 56

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: 48.48 E-value: 4.62e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 5103661   16 KHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDI 65
Cdd:cd04632  75 YDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDV 124

voltage-gated chloride channel ClcB;

Pssm-ID: 234987 [Multi-domain] Cd Length: 574 Bit Score: 50.51 E-value: 5.05e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661     8 MRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGKVEDIMSRN 87
Cdd:PRK01862 442 ERLRTTQMRELIQPAQTVVPPTASVADMTRVFLEYPVKYLYVVDDDGRFRGAVALKDITSDLLDKRDTTDKTAADYAHTP 521

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 5103661    88 PIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRP--LGMISVRDIID 132
Cdd:PRK01862 522 FPLLTPDMPLGDALEHFMAFQGERLPVVESEASPtlAGVVYKTSLLD 568

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: 48.27 E-value: 5.21e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   49 VVDKQGLVKGILTERDIINSLA-----SGKACAEGKVEDIMSRNPIVASPDDDLEIIIEKMRDMNIrhIPVIDEDGRPLG 123
Cdd:cd04643  35 VLDKDYKLVGLISLSMILDAILgleriEFEKLSELKVEEVMNTDVPTVSPDDDLEEVLHLLVDHPF--LCVVDEDGYFLG 112


                ....*...
gi 5103661  124 MISVRDII 131
Cdd:cd04643 113 IITRREIL 120

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

Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 47.92 E-value: 8.07e-08

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5103661   12 RLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL 69
Cdd:cd17774  68 QTQAQTVMSSPLFSLRPDDSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSLLQAL 125

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: 47.38 E-value: 9.39e-08

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   12 RLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGIL 60
Cdd:cd04604  69 NLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGIL 117

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: 47.04 E-value: 1.22e-07

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5103661    9 RSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDII 66
Cdd:cd04587  56 LDPDTPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDDGRVV-GVVTATDLM 112

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: 45.49 E-value: 4.16e-07

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 5103661   14 KAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDI 65
Cdd:cd04622  61 TVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 47.52 E-value: 5.00e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 5103661    79 KVEDIM-SRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:PRK14869 247 PVSYIMtTEDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHLLS 301

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: 45.58 E-value: 5.26e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPpvtievgrsIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINsLASGKACAEGKV---EDIMSRNPIVA---- 91
Cdd:cd04641  10 MDTP---------VIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVIN-LAAEKTYNNLDLtvgEALQHRSEDFEgvht 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 5103661   92 -SPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04641  80 cTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDI 119

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

Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 45.18 E-value: 5.28e-07

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5103661   16 KHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIINS 68
Cdd:cd04595  59 KGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLV-GIVTRSDVLRY 110

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: 45.93 E-value: 5.51e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   31 SIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIInSLASG-----------------KACAE---------GK-VEDI 83
Cdd:cd17789  13 TVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLL-ALDSIsgrsqtdnnfppadstwKTFNEvqkllsktnGKvVGDV 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 5103661   84 MSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd17789  92 MTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVV 139

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

Pssm-ID: 341407 [Multi-domain] Cd Length: 115 Bit Score: 45.39 E-value: 6.45e-07

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 5103661   83 IMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:cd17771   1 LIRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSR 51

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: 45.01 E-value: 8.06e-07

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5103661   85 SRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDLGVSA 137
Cdd:cd04632   1 TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRP 53

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

Pssm-ID: 341421 [Multi-domain] Cd Length: 136 Bit Score: 45.34 E-value: 8.68e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   19 MSTPPVTIEVGRSIAEAARLMAERGVG-SLIVVDKQGLVKGILTERDIINSLASGKACAE---------------GKVED 82
Cdd:cd17785   8 ITKKPSVVHENTSIRDVIDKMIEDPKTrSVYVVDDDEKLLGIITLMELLKYIGYRFGVTIykgvsfglllrislkEKAKD 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   83 IMsRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd17785  88 IM-LSPIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIGDLNSLELL 135

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: 44.83 E-value: 9.57e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   25 TIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINS-LASGKACAEGKVEDIMsRNPI-VASPDDDLEIIIE 102
Cdd:cd17786   6 TINWNATVFDAVKIMNENHLYGLVVKDDDGNYVGLISERSIIKRfIPRNVKPDEVPVKLVM-RKPIpKVKSDYDVKDVAA 84

                        90       100
                ....*....|....*....|....*...
gi 5103661  103 KMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd17786  85 FLSENGLERCAVVDDNGRVVGIVTITDL 112

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

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 44.48 E-value: 1.73e-06

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5103661    9 RSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDII 66
Cdd:cd04600  71 RDRPETVGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128

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: 43.87 E-value: 1.81e-06

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   82 DIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04597   1 DLEYDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDI 49

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: 1.86e-06

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINS 68
Cdd:cd09833  66 VMSSPVLTIPQDTTLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDVVLN 116

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 44.82 E-value: 3.71e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661     6 RYMRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDI 65
Cdd:PRK14869  61 ELIEDVKPQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDL 120

arabinose-5-phosphate isomerase GutQ;

Pssm-ID: 183186 [Multi-domain] Cd Length: 321 Bit Score: 44.76 E-value: 3.81e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661    14 KAKHVMST----PPVTIEVgrSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKACAEGkVEDIMSRNPI 89
Cdd:PRK11543 198 KVHHLMRRddaiPQVALTA--SVMDAMLELSRTGLGLVAVCDAQQQVQGVFTDGDLRRWLVGGGALTTP-VNEAMTRGGT 274

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 5103661    90 VASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDLGVS 136
Cdd:PRK11543 275 TLQAQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGII 321

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: 42.21 E-value: 1.06e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5103661   79 KVEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIdEDGRPLGMISVRDII 131
Cdd:cd04631   1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIM 52

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: 1.74e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   15 AKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVD--KQGLVKGILTERDIINSLasgkacaEGKVEDIMSRNPIVAS 92
Cdd:cd04591   2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDstESQTLVGFILRSQLILLL-------EADLRPIMDPSPFTVT 74

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 5103661   93 PDDDLEIIIEKMRDMNIRHIPVIDeDGRPLGMISVRDI 130
Cdd:cd04591  75 EETSLEKVHDLFRLLGLRHLLVTN-NGRLVGIVTRKDL 111

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: 42.76 E-value: 2.05e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5103661      6 RYMRSPRLKAKHVM-STPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDI 65
Cdd:pfam00478 132 RFETDLSQPVSEVMtKENLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192

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

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 41.07 E-value: 2.66e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 5103661   80 VEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04605   2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDI 52

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: 40.00 E-value: 4.01e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   15 AKHVMSTPPVTIEVGRSIAEAARLM-AERGVGSLIVVDKQGlvkgiLTERDIINSLASGkacaegkvedimsRNPIVasp 93
Cdd:COG3620   1 VRDLMSRDVVTVSPDDTLGEALRLMrKELGLSQLPVAELVG-----VSQSDILRIESGK-------------RDPTV--- 59

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5103661   94 dDDLEIIIEKMrDMNIRHIPVIDeDGRPLGMISVRDIID 132
Cdd:COG3620  60 -STLEKIAEAL-GKELSAVLVVD-DGKLVGIITRRDLLK 95

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: 40.09 E-value: 4.24e-05

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 5103661   86 RNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04601   2 TDPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDI 46

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: 40.24 E-value: 5.51e-05

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   84 MSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd04600   1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLK 49

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 41.59 E-value: 5.61e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5103661   10 SPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDII 66
Cdd:COG2239 190 DPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVV 246

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: 39.63 E-value: 6.65e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   31 SIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLAsgkacaeGKVEDIMSRNPIVASPDDDLEIIIEKMRDMNIR 110
Cdd:cd04594  12 TVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDIENKSP-------GKVGKYVVRGSPYVTPTSSLEEAWEIMMRNKSR 84

                        90       100
                ....*....|....*....|..
gi 5103661  111 HIPVIDEdGRPLGMISVRDIID 132
Cdd:cd04594  85 WVAVVEK-GKFLGIITLDDLLE 105

inosine-5'-monophosphate dehydrogenase; Provisional

Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 41.11 E-value: 8.02e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661    23 PVTIEVGRSIAEAARLMAERGVGS-LIVVDKQ--GLVKGILTERDIINSLASgkacaEGKVEDIMSR--NPIVASPDDDL 97
Cdd:PTZ00314 106 PYVLSPNHTVADVLEIKEKKGFSSiLITVDGKvgGKLLGIVTSRDIDFVKDK-----STPVSEVMTPreKLVVGNTPISL 180

                         90       100       110
                 ....*....|....*....|....*....|...
gi 5103661    98 EIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:PTZ00314 181 EEANEVLRESRKGKLPIVNDNGELVALVSRSDL 213

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: 38.84 E-value: 1.16e-04

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5103661   14 KAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINS 68
Cdd:cd04610  54 KVSEIMSRDTVVADPDMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVIRS 108

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: 39.24 E-value: 1.19e-04

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5103661   10 SPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDII 66
Cdd:cd04606  62 DPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVL 118

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: 38.84 E-value: 1.44e-04

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDkQGLVKGILTERDI 65
Cdd:cd17771  66 VMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVD-NGRLVGVVSERDL 112

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: 38.55 E-value: 1.56e-04

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5103661   85 SRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI----IDLGVSALKLFVE 143
Cdd:cd04623   1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYvrklALRGASSLDTPVS 63

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: 38.71 E-value: 1.66e-04

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5103661   13 LKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVD--KQGLVKGILTERDII 66
Cdd:cd04613  60 VVVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDddDPGKVLGMLSRRDVI 115

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: 38.48 E-value: 1.96e-04

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 5103661   89 IVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDI 130
Cdd:cd04594   5 IKVSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDI 46

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: 38.38 E-value: 2.11e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   31 SIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLAS-GKACAEGKVEDIMSRNPIVASPDDDLEIIIEKMRDmNI 109
Cdd:cd17773  16 SILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLEnPNADLSQPVSHVANTNFVSAPEGESPEKIEALFSS-RI 94

                        90
                ....*....|.
gi 5103661  110 RHIPVIDEDGR 120
Cdd:cd17773  95 SYIPLVDERGR 105

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; 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: 341402 [Multi-domain] Cd Length: 116 Bit Score: 38.31 E-value: 2.11e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   17 HVMSTPPVTI--EVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSLASGKAcaegKVEDIMSRNPIVASPD 94
Cdd:cd09831   1 DIARKTQVTVieKTGDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRAALKENAQ----SLEDAFLTDVETVPAD 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 5103661   95 DDLEIIIEKMRDMNIRhIPVIDEDGRPLGMIS 126
Cdd:cd09831  77 TSLSDILGLVASAPCP-LPVVDEDGRYLGVIS 107

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

Pssm-ID: 341412 [Multi-domain] Cd Length: 115 Bit Score: 38.16 E-value: 2.46e-04

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDII 66
Cdd:cd17776  65 VASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLDLV-GILTATDII 112

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

Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 38.48 E-value: 3.27e-04

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5103661   77 EGKVEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVIDEDgRPLGMISVRDIID-LGVSALKLFVE 143
Cdd:cd17777   1 EKELMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDEN-KLEGILSARDLVSyLGGGCLFKIVE 67

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: 38.41 E-value: 3.94e-04

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5103661    3 VFKRYMRSPRLKA-----KHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDII 66
Cdd:cd04614  80 VMSLYYPTSNVELpdkpvKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDLL 148

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: 39.04 E-value: 4.45e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661     30 RSIAEAARlmaerGVGSLIVVDKQGLVKGILTERDIInslasgKACAEGKVEDIMSRNPIVASPDDDLEIIIEKMRDMNI 109
Cdd:TIGR00400 158 RRVAKTKE-----DIYTLYVTNESKHLKGVLSIRDLI------LAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDF 226

                          90       100
                  ....*....|....*....|....
gi 5103661    110 RHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:TIGR00400 227 LAVPVVDNEGRLVGIVTVDDIIDV 250

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

Pssm-ID: 341421 [Multi-domain] Cd Length: 136 Bit Score: 37.64 E-value: 6.20e-04

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5103661   78 GKVEDIMSRNPIVASPDDDLEIIIEKM-RDMNIRHIPVIDEDGRPLGMISVRDIIDL 133
Cdd:cd17785   2 GDIYNLITKKPSVVHENTSIRDVIDKMiEDPKTRSVYVVDDDEKLLGIITLMELLKY 58

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

Pssm-ID: 341406 [Multi-domain] Cd Length: 111 Bit Score: 36.96 E-value: 7.89e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   27 EVGRSIAEAARLMAERGVGSLIVVDKqGLVKGILTERDIINSLASGKACAEGKVEDIMSRNPIVAsPDDDLEIIIEKMRD 106
Cdd:cd09837   8 TDDAPAAEVLAFMQAKELSCAPVLHD-GRYVAMVTLADLLPARQGTPTAGLKLGELSLEEVGSIG-PHEHLFDLFSRLAL 85

                        90       100
                ....*....|....*....|....*
gi 5103661  107 MNIRHIPVIDEDGRPLGMISVRDII 131
Cdd:cd09837  86 FPCSIIPVSDEDGRYIGVVSKKRVL 110

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: 36.65 E-value: 9.09e-04

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5103661    7 YMRSPRLKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDIIN 67
Cdd:cd04629  56 YHCEPGGTVADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLV-GQISRRDVLR 115

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: 341424 [Multi-domain] Cd Length: 137 Bit Score: 36.84 E-value: 9.69e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   21 TPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINSL-----------------ASGKACAEG----K 79
Cdd:cd17788   2 EPYPTVSLDDDALDAARLLAEERLPGLVVVDDDGRPYAVLPGSQVLRFLvpryvrddpalarvideRHADQLCARlagrT 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5103661   80 VEDIMSRNPI---VASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd17788  82 VADLLPAERVrlpVVGPDATLLEIAALMARLRSPLVAVVDRKGRLLGVVTASRLLE 137

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

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 36.45 E-value: 1.07e-03

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 5103661   16 KHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDI 65
Cdd:cd04605  64 EEIMTRNVITARPDEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113

GuaB1 family IMP dehydrogenase-related protein;

Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 37.58 E-value: 1.19e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 5103661    17 HVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINS 68
Cdd:PRK07807 152 DVMSTDLVTLPAGTDPREAFDLLEAARVKLAPVVDADGRLVGVLTRTGALRA 203

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

Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 37.41 E-value: 1.25e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   13 LKAKHVMsTPP---VTIEVGRSIAEAARLMAERGVgSLIVVDKQGL--VKGILTERDIINSLASGKacaEGKVEDIMsRN 87
Cdd:COG1253 214 RTVREVM-TPRtdvVALDLDDTLEEALELILESGH-SRIPVYEGDLddIVGVVHVKDLLRALLEGE---PFDLRDLL-RP 287

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 5103661   88 PIVAsPD----DDLeiiiekMRDMNIRHIP---VIDEDGRPLGMISVRDII 131
Cdd:COG1253 288 PLFV-PEtkplDDL------LEEFRRERVHmaiVVDEYGGTAGLVTLEDIL 331

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: 36.27 E-value: 1.43e-03

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5103661   14 KAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDII 66
Cdd:cd04607  59 PVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLETLDDLL 111

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: 35.57 E-value: 2.08e-03

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   13 LKAKHVMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILT 61
Cdd:cd04583  54 KKVGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVT 102

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: 35.47 E-value: 2.83e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   25 TIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIINsLASGKacaegKVEDIMSRNPIVASPDDDLEIIIEKM 104
Cdd:cd17787   6 TFEESATVGEVLHEMRKYETDYCIVVDEEGKFAGMVRKSKIMD-EDLDK-----KVKEYVVEPDFYCHEEDYIEDAALLL 79

                        90       100
                ....*....|....*....|....*...
gi 5103661  105 RDMNIRHIPVIDEDGRPLGMISVRDIID 132
Cdd:cd17787  80 IESHEFVLPVVNSDMKVKGVLTVFEILE 107

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341366 [Multi-domain] Cd Length: 119 Bit Score: 35.16 E-value: 3.32e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5103661   14 KAKHVMsTPP---VTIEVGRSIAEAARLMAERGVGSLIVVDKQ-GLVKGILTERDIINSLASGKAcaEGKVEDIMsRNPI 89
Cdd:cd04590   1 TVREVM-TPRtdvVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVLHVKDLLAALLEGRE--KLDLRALL-RPPL 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 5103661   90 VASPDDDLEIIIEKMRdmnIRHIP---VIDEDGRPLGMISVRDII 131
Cdd:cd04590  77 FVPETTPLDDLLEEFR---KERSHmaiVVDEYGGTAGIVTLEDIL 118

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: 34.80 E-value: 3.89e-03

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5103661   80 VEDIMSRNPIVASPDDDLEIIIEKMRDMNIRHIPVID--EDGRPLGMISVRDIIDL 133
Cdd:cd04591   2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDstESQTLVGFILRSQLILL 57

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: 34.62 E-value: 4.13e-03

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 5103661   18 VMSTPPVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVkGILTERDII 66
Cdd:cd04599  58 AMSRNVVTISPEASLWEAKELMEEHGIERLVVVEEGRLV-GIITKSTLY 105

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

Pssm-ID: 341377 [Multi-domain] Cd Length: 112 Bit Score: 34.36 E-value: 5.76e-03

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 5103661   88 PIVASPDDDLEIIIEKMRDMNIRHIPVIDEDGRPLGMISVRDIIDLGVSALK 139
Cdd:cd04603   4 LVFVNKNEPLREIIKKITELNARAIVIVNNNMSVLGQITVSDLLEIGPSQYE 55

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: 34.37 E-value: 6.31e-03

                        10        20
                ....*....|....*....|
gi 5103661  113 PVIDEDGRPLGMISVRDIID 132
Cdd:cd04596  29 PVVDEENRVVGIVTAKDVIG 48

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 35.58 E-value: 6.95e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 5103661    13 LKAKHVMSTP-PVTIEVGRSIAEAARLMAERGVGSLIVVDKQGLVKGILTERDIIN 67
Cdd:PRK14869 246 IPVSYIMTTEdLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHLLS 301