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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 198 LHDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQMKVVGVVTAKDIIDRPHDWAVEKVMTRHPITVGIRTSVTNSAHQMV 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80

                         90       100
                 ....*....|....*....|....*...
gi 557718508 278 WEGIEMLPVIDQYGRLLGIISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 338 LSLEVSPQMTNFMGTASSGVLTTLLVEGATRMLR--HMKKGDLVIENVSIYFIKPVQIESTVTIRANVFDVGRKFGKVDV 415
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAArlGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                         90
                 ....*....|....*.
gi 557718508 416 EMYQGT-QIVAKALVT 430
Cdd:cd03440   83 EVRNEDgKLVATATAT 98

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 198 LHDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQMKVVGVVTAKDIIDRPHDWAVEKVMTRHPITVGIRTSVTNSAHQMV 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80

                         90       100
                 ....*....|....*....|....*...
gi 557718508 278 WEGIEMLPVIDQYGRLLGIISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508   76 EVVNIVDGQVLGGRNGLHKTLTKFVIGAMKLEAMMRYIDVDSLVII-GNREKAHELVLEAG-AAVLITGGFDTTEDAKRL 153
Cdd:pfam07085   1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITpGDREDIQLAALEAGiAGLILTGGFEPSPEVLKL 80

                          90       100
                  ....*....|....*....|....*
gi 557718508  154 ADEMELPIISTSYDTFTVATMINRA 178
Cdd:pfam07085  81 AEELGLPVLSTPYDTFTTASRINRA 105

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508  75 AEVVNIVDGQVLGGRNGLHKTLTKFVIGAMKLEAMMRYIDVDSLVII-GNREKAHELVLEAG-------AAVLITGGFDT 146
Cdd:COG0857  217 RDLAEALGAEVLNGGELLDRRVESVVVGAMSVPNALERLREGALVITpGDRSDILLAALLAAlsgtpsiAGLILTGGLPP 296

                         90       100       110
                 ....*....|....*....|....*....|....
gi 557718508 147 TEDAKRLADEME--LPIISTSYDTFTVATMINRA 178
Cdd:COG0857  297 DPAVLRLAEGLGqtLPILSVELDTYTTAERLERV 330

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 338 LSLEVSPQMTNFMGTASSGVLTTLLVEGATRMLR--HMKKGDLVIENVSIYFIKPVQIESTVTIRANVFDVGRKFGKVDV 415
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAArlGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                         90
                 ....*....|....*.
gi 557718508 416 EMYQGT-QIVAKALVT 430
Cdd:cd03440   83 EVRNEDgKLVATATAT 98

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557718508  350 MGTASSGVLTTLLVEGATRMLRHMKKGD--LVIENVSIYFIKPVQIESTVTIRANVFDVGRKFGKVDVEMYQGTQIVAK 426
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQqvVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 219 QTKHNRYPVIDEQMKVVGVVTAKDIID-----------RPHDWAVEKVMTRHPITVGIRTSVTNSAHQMVWEgiEMLPVI 287
Cdd:NF041630  39 KVGYSKIPVLDKDKKFVGLISLSDITDymlgleriefeKLSELKVADVMNTDVPTITDDYDLEEILHLLVDH--PFLPVV 116

                         90
                 ....*....|....*....
gi 557718508 288 DQYGRLLGIISRQDVLKAL 306
Cdd:NF041630 117 DEDGIFLGIITRREILKAV 135

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557718508   3 TKHEQIIRHIED------LDVGTKI-SVRQIAKDLTVSEGTAYRAIKEAENLGFVSTIERVGT 58
Cdd:COG1167   12 PLYLQLADALREailsgrLPPGDRLpSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGT 74

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 198 LHDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQMKVVGVVTAKDIIDRPHDWAVEKVMTRHPITVGIRTSVTNSAHQMV 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80

                         90       100
                 ....*....|....*....|....*...
gi 557718508 278 WEGIEMLPVIDQYGRLLGIISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508   76 EVVNIVDGQVLGGRNGLHKTLTKFVIGAMKLEAMMRYIDVDSLVII-GNREKAHELVLEAG-AAVLITGGFDTTEDAKRL 153
Cdd:pfam07085   1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITpGDREDIQLAALEAGiAGLILTGGFEPSPEVLKL 80

                          90       100
                  ....*....|....*....|....*
gi 557718508  154 ADEMELPIISTSYDTFTVATMINRA 178
Cdd:pfam07085  81 AEELGLPVLSTPYDTFTTASRINRA 105

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 189 LLVSDILIPlhDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQMKVVGVVTAKDIID------------RPHDWAVEKVM 256
Cdd:COG3448    2 MTVRDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRallpdrldeleeRLLDLPVEDVM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 557718508 257 TRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQYGRLLGIISRQDVLKAL 306
Cdd:COG3448   80 TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRAL 129

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 199 HDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQMKVVGVVTAKDIIDRPHDW------AVEKVMTRHPITVGIRTSVTNS 272
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGglaldtPVAEVMTPDVITVSPDTDLEEA 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 557718508 273 AHQMVWEGIEMLPVIDQYGRLLGIISRQDVLK 304
Cdd:cd02205   82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 199 HDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQmKVVGVVTAKDIIDRPHDWAVEKVMTRHPITVGIRTSVTNSAHQMVW 278
Cdd:cd04610    3 RDVITVSPDDTVKDVIKLIKETGHDGFPVVDDG-KVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITDAARVIFR 81

                         90       100
                 ....*....|....*....|....*.
gi 557718508 279 EGIEMLPVIDQYGRLLGIISRQDVLK 304
Cdd:cd04610   82 SGISKLPVVDDEGNLVGIITNMDVIR 107

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 226 PVIDEQMKVVGVVTAKDIIDRP-----------------------------HDWAVEKVMTRHPITVGIRTSVTNSAHQM 276
Cdd:cd04586   30 PVVDDDGKLVGIVSEGDLLRREepgteprrvwwldallesperlaeeyvkaHGRTVGDVMTRPVVTVSPDTPLEEAARLM 109

                         90       100
                 ....*....|....*....|....*....
gi 557718508 277 VWEGIEMLPVIDQyGRLLGIISRQDVLKA 305
Cdd:cd04586  110 ERHRIKRLPVVDD-GKLVGIVSRADLLRA 137

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 226 PVIDEQMKVVGVVTAKDII-----DRPH-DWA--VEKVMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQyGRLLGII 297
Cdd:cd04629   30 PVVDEQGRLVGFLSEQDCLkalleASYHcEPGgtVADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQI 108

                 ....*...
gi 557718508 298 SRQDVLKA 305
Cdd:cd04629  109 SRRDVLRA 116

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 227 VIDEQMKVVGVVTAKDIIDR-------PHDWAVEKVMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQYGRLLGIISR 299
Cdd:cd17775   31 VVEEDGKPVGIVTDRDIVVEvvakgldPKDVTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTL 110

                 ....*..
gi 557718508 300 QDVLKAL 306
Cdd:cd17775  111 DDILELL 117

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 191 VSDILIPLHDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQM-KVVGVVTAKDIIDRPHDWAVEKVMTRH---PITVGIR 266
Cdd:cd04590    2 VREVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDLdNIIGVLHVKDLLAALLEGREKLDLRALlrpPLFVPET 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 557718508 267 TSVTNSAHQMVWEGIEMLPVIDQYGRLLGIISRQDVL 303
Cdd:cd04590   82 TPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508  200 DTFYLQTTDPISRWHELNEQTKHNRYPVIDEQmKVVGVVTAKDI-IDRPHDWAVEKVMTRHP-ITVGIRTSVtNSAHQMV 277
Cdd:pfam00478  89 DPVTLSPDATVADALALMERYGISGVPVVDDG-KLVGIVTNRDLrFETDLSQPVSEVMTKENlVTAPEGTTL-EEAKEIL 166

                          90       100       110
                  ....*....|....*....|....*....|.
gi 557718508  278 WE-GIEMLPVIDQYGRLLGIISRQDVLKALQ 307
Cdd:pfam00478 167 HKhKIEKLPVVDDNGRLVGLITIKDIEKAKE 197

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 204 LQTTDPISRWHELNEQTKHNRYPVIDEQmKVVGVVTAKDIID-RPHDWA---------------VEKVMTRHPITVGIRT 267
Cdd:cd04584   13 VTPDTSLAEARELMKEHKIRHLPVVDDG-KLVGIVTDRDLLRaSPSKATslsiyelnyllskipVKDIMTKDVITVSPDD 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 557718508 268 SVTNSAHQMVWEGIEMLPVIDQyGRLLGIISRQDVLKAL 306
Cdd:cd04584   92 TVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 557718508  252 VEKVMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQYGRLLGIISRQDVLKAL 306
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRAL 55

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 208 DPISRWHELNEQTKHNRYPVIDEQmKVVGVVTAKDIIDRPHDWAVEKVMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVI 287
Cdd:cd04599   12 DSVARAAALMERQRIGGLPVVENG-KLVGIITSRDVRRAHPNRLVADAMSRNVVTISPEASLWEAKELMEEHGIERLVVV 90

                         90
                 ....*....|....*.
gi 557718508 288 DQyGRLLGIISRQDVL 303
Cdd:cd04599   91 EE-GRLVGIITKSTLY 105

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 227 VIDEQMKVVGVVTAKDIIDR-------PHDWAVEKVMTRHPITVGIRTSVTNSAHQMvWEGIEM-LPVIDQYGRLLGIIs 298
Cdd:cd17782   30 VMDNSGKVIGIFTSKDVVLRvlaagldPATTSVVRVMTPNPETAPPSTTILDALHKM-HEGKFLnLPVVDDEGEIVGLV- 107

                 ....*.
gi 557718508 299 rqDVLK 304
Cdd:cd17782  108 --DVLQ 111

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 197 PLHDTFYLQTTDPISRWHELNEQTKHNRYPVIDEQMKVVGVVT-----AKDIIDR-----------PHDW----AVEK-- 254
Cdd:cd17789    1 PKGKLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSdydllALDSISGrsqtdnnfppaDSTWktfnEVQKll 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 557718508 255 ----------VMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQYGRLLGIISRQDVLKA 305
Cdd:cd17789   81 sktngkvvgdVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVRA 141

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 226 PVIDEQMKVVGVVTAKDIIDRPH---------------------DWAVEKVMTRHPITVGIRTSVTNSAHQMVWEGIEML 284
Cdd:cd04600   30 PVVDRARRLVGIVTLADLLKHADldpprglrgrlrrtlglrrdrPETVGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHI 109

                         90       100
                 ....*....|....*....|..
gi 557718508 285 PVIDQYGRLLGIISRQDVLKAL 306
Cdd:cd04600  110 PVVDADGRLVGIVTQSDLIAAL 131

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 224 RYPVIDEQmKVVGVVTAKDIID-----RPHDW----------------AVEKVMTRHPITVGIRTSVTNSAHQMVWEGIE 282
Cdd:cd17777   35 RLVVVDEN-KLEGILSARDLVSylgggCLFKIvesrhqgdlysalnreVVETIMTPNPVYVYEDSDLIEALTIMVTRGIG 113

                         90       100
                 ....*....|....*....|....
gi 557718508 283 MLPVIDQYGRLLGIISRQDVLKAL 306
Cdd:cd17777  114 SLPVVDRDGRPVGIVTERDLVLYL 137

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).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557718508 227 VIDEQMKVVGVVTAKDIiDRPHDWA--VEKVMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQYGRLLGIISR 299
Cdd:cd04583   30 VVDKDNVLLGIVDIEDI-NRNYRKAkkVGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTR 103

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 338 LSLEVSPQMTNFMGTASSGVLTTLLVEGATRMLR--HMKKGDLVIENVSIYFIKPVQIESTVTIRANVFDVGRKFGKVDV 415
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAArlGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                         90
                 ....*....|....*.
gi 557718508 416 EMYQGT-QIVAKALVT 430
Cdd:cd03440   83 EVRNEDgKLVATATAT 98

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).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557718508 226 PVIDEQMKVVGVVTAKDIIDRPHDWAVEKVMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQYGRLLGIISRQDVL 303
Cdd:cd04606   41 YVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVL 118

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557718508 226 PVIDEQMKVVGVVTAKDIIDR-------PHDWAVEKVMTRHPITVGIRTSVTNSAHQMVWEGIEMLPVIDQyGRLLGIIS 298
Cdd:cd04623   29 VVVDDGGRLVGILSERDYVRKlalrgasSLDTPVSEIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVED-GKLVGIVS 107