NCBI Conserved Domain Search

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341388 [Multi-domain] Cd Length: 138 Bit Score: 232.06 E-value: 5.92e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 116 KCYDLIPTSSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDTDNQRFTGMLTITDFIKILCKHYDKGdnSERIRALEDQQI 195
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSP--SVQMEELEEHTI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831511673 196 SHWRDQFELDGTlRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMK 256
Cdd:cd04618    79 ETWREIERQIGV-PPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138

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: 217.38 E-value: 1.52e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 283 WGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRSEWFEGVQTCL 362
Cdd:cd04641     2 YENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTCT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 363 ETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 405
Cdd:cd04641    82 LNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 86.84 E-value: 2.36e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHrsewfeGVQTCLET 364
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831511673 365 DSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 405
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 84.92 E-value: 1.14e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVV------DIYAKFDVISLAaESSYDKLDCTVQEALQHRsewfegV 358
Cdd:COG3448    11 DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVgivterDLLRALLPDRLD-ELEERLLDLPVEDVMTRP------V 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1831511673 359 QTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 405
Cdd:COG3448    84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130

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: 78.06 E-value: 1.58e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAEsSYDKLDCTVQEALQhrsewfEGVQTCLET 364
Cdd:cd02205     3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE-GGLALDTPVAEVMT------PDVITVSPD 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1831511673 365 DSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:cd02205    76 TDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 77.56 E-value: 3.42e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRsewfegVQTCLET 364
Cdd:COG2905     8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRP------PITVSPD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1831511673 365 DSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 404
Cdd:COG2905    82 DSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRAL 120

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 77.98 E-value: 3.85e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLS------LYMRDLPRP--SFMSctprelgi 280
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLpdrldeLEERLLDLPveDVMT-------- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831511673 281 gawGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAES 335
Cdd:COG3448    81 ---RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARL 132

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 79.16 E-value: 7.09e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDeNGRVVDIYAKFDVISlAAESSYDKLDCTVQEALQhrsewfEGVQTCLET 364
Cdd:COG2524    95 DVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLK-ALAEGRDLLDAPVSDIMT------RDVVTVSED 166

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1831511673 365 DSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:COG2524   167 DSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204

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: 70.54 E-value: 1.22e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVV------DIYAKFDVISLA---------------AESSYDK-LDC 342
Cdd:cd04586     4 DVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVgivsegDLLRREEPGTEPrrvwwldallesperLAEEYVKaHGR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 343 TVQEALQHRsewfegVQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 402
Cdd:cd04586    84 TVGDVMTRP------VVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLLR 136

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

Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 69.77 E-value: 1.58e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 290 HVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLD-CTVQEALQHrsewfeGVQTCLETDSLF 368
Cdd:cd04629     9 TPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPgGTVADYMST------EVLTVSPDTSIV 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1831511673 369 QVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 402
Cdd:cd04629    83 DLAQLFLKNKPRRYPVVE-DGKLVGQISRRDVLR 115

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 69.89 E-value: 1.69e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLSLYMRDLP-RP--SFMSctprelgigawGD 285
Cdd:COG0517     9 TDVVTVSPDATVREALELMSEKRIGGLPVVD-EDGKLVGIVTDRDLRRALAAEGKDLLdTPvsEVMT-----------RP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1831511673 286 ILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAE 334
Cdd:COG0517    77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 69.91 E-value: 1.05e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMKFLSLYMRDLPRP--SFMSctprelgigawGDI 286
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDAPvsDIMT-----------RDV 160

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1831511673 287 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVV 320
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLV 194

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: 65.73 E-value: 4.34e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLSLYMRDLPRP--SFMSctprelgigawGDI 286
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPvaEVMT-----------PDV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 287 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 329
Cdd:cd02205    70 ITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112

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: 65.19 E-value: 1.25e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 284 GDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQhrsEW--FEGVQTC 361
Cdd:cd17789     3 GKLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADS---TWktFNEVQKL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1831511673 362 L--------------------ETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:cd17789    80 LsktngkvvgdvmtpsplvvrEKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVR 140

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: 62.82 E-value: 4.10e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPlIDENGRVV------DIyakfdVISLAAESSyDKLDCTVQEALQHrsewfeGV 358
Cdd:cd04622     4 DVVTVSPDTTLREAARLMRDLDIGALP-VCEGDRLVgmvtdrDI-----VVRAVAEGK-DPNTTTVREVMTG------DV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1831511673 359 QTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDI 400
Cdd:cd04622    71 VTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112

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: 61.28 E-value: 1.91e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKT--GnityILTHKRIMKFLSlymrdlprPSFMSCTPRELGIGAWG-- 284
Cdd:cd04584     8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKlvG----IVTDRDLLRASP--------SKATSLSIYELNYLLSKip 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1831511673 285 -------DILCCHVDTPIHDALELFLKNRVSALPLIDeNGRVVDI 322
Cdd:cd04584    76 vkdimtkDVITVSPDDTVEEAALLMLENKIGCLPVVD-GGKLVGI 119

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: 58.30 E-value: 1.66e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 286 ILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAEssyDKLDCTVQEALQhrsewFEGVQTCLETD 365
Cdd:cd09836     5 VVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAE---GIDLDTPVEEIM-----TKNLVTVSPDE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1831511673 366 SLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:cd09836    77 SIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 60.28 E-value: 1.80e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 124 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLwdTDNQRFTGMLTITDFIKILckhydkgdnsERIRALEDQQIShwrdqfe 203
Cdd:COG2524    93 TKDVITVSPDTTLEEALELMLEKGISGLPV--VDDGKLVGIITERDLLKAL----------AEGRDLLDAPVS------- 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831511673 204 lDGTLRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL 258
Cdd:COG2524   154 -DIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDD-GKLVGIITRTDILRAL 206

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 57.57 E-value: 5.29e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 124 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDtDNQRFTGMLTITDFIKILckhyDKGDNSERIRALEDQQIShwrdqfe 203
Cdd:COG3448     9 TRDVVTVSPDTTLREALELMREHGIRGLPVVD-EDGRLVGIVTERDLLRAL----LPDRLDELEERLLDLPVE------- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831511673 204 lDGTLRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL 258
Cdd:COG3448    77 -DVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLLRAL 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: 53.29 E-value: 1.97e-09

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1831511673  358 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNL 404
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 51.74 E-value: 5.35e-09

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1831511673  285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAA 333
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49

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: 53.69 E-value: 5.65e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 292 DTPIHDALELFLKNRVSALPLIDeNGRVVDIYAKFDVISLAAEssyDKLDCTVQEALQHRsewfegVQTCLETDSLFQVL 371
Cdd:cd04588    10 DATIKDAAKLLSENNIHGAPVVD-DGKLVGIVTLTDIAKALAE---GKENAKVKDIMTKD------VITIDKDEKIYDAI 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831511673 372 EAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:cd04588    80 RLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 54.15 E-value: 7.20e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 290 HVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVIslaaessyDKLDCTVQEALQHRSewfegVQTCLETDSLFQ 369
Cdd:COG4109    31 SEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL--------GKDDDTPIEDVMTKN-----PITVTPDTSLAS 97

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831511673 370 VLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNL 404
Cdd:COG4109    98 AAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132

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: 53.00 E-value: 1.17e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 286 ILCCHVDTPIHDALELFLKNRVSALpLIDENGRVVDIYAKFDVISLAaESSYDKLDCTVQEALQHRsewfegVQTcleTD 365
Cdd:cd09833     7 LLTCSPDTPLADAAARMAERRCSSI-LIVENGEIVGIWTERDALKLD-FSDPDAFRRPISEVMSSP------VLT---IP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831511673 366 SLFQVLEAIVK---AEVHRLIVTDQDKKVVGVVSLSDILKN 403
Cdd:cd09833    76 QDTTLGEAAVRfrqEGVRHLLVVDDDGRPVGIVSQTDVVLN 116

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: 50.29 E-value: 2.46e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1831511673 358 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 405
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56

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

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 50.88 E-value: 6.48e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 284 GDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRsewfegVQTCLE 363
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRD------VVTCTP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1831511673 364 TDSLFQVLEAIVKaevHR---LIVTDqDKKVVGVVSLSDILK 402
Cdd:cd04623    76 DDTVEECMALMTE---RRirhLPVVE-DGKLVGIVSIGDVVK 113

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: 48.75 E-value: 7.43e-08

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAE 334
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

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: 50.64 E-value: 1.24e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRSEWFEG------- 357
Cdd:cd04600     4 DVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRDRPETvgdimtr 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 358 -VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSD 399
Cdd:cd04600    84 pVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSD 126

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 49.48 E-value: 3.23e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831511673 358 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLVLD 407
Cdd:COG3448    12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPD 61

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: 48.30 E-value: 4.60e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMKFLSLYMRDLPRPSFMSctprelgigawGDILC 288
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD--GKLVGIVTLTDIAKALAEGKENAKVKDIMT-----------KDVIT 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 289 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISL 331
Cdd:cd04588    69 IDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111

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: 46.05 E-value: 7.37e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLS 259
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRALL 56

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: 47.92 E-value: 7.41e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFD-VISLAAESSyDKLDCTVQEALQhrsewfEGVQTCLE 363
Cdd:cd17775     4 EVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDiVVEVVAKGL-DPKDVTVGDIMS------ADLITARE 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1831511673 364 TDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:cd17775    77 DDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILE 115

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: 48.38 E-value: 7.91e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 212 VYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKFL-----SLYMRDLPRPSFMSCTPRELGIGAWGDI 286
Cdd:cd17779    11 ITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskYNLVEKKHNGNLLAAINEPVREIMTRDV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 287 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 329
Cdd:cd17779    91 ISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133

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: 47.42 E-value: 1.04e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 297 DALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYdKLDCTVQEALQhrsewfEGVQTCLETDSLfqvLEAIVK 376
Cdd:cd17784    15 EAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKY-ELGTTVEEVMV------KDVATVHPDETL---LEAIKK 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1831511673 377 AE--------VHRLIVTDqDKKVVGVVSLSDILKNL 404
Cdd:cd17784    85 MDsnapdeeiINQLPVVD-DGKLVGIISDGDIIRAI 119

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

Pssm-ID: 341395 [Multi-domain] Cd Length: 127 Bit Score: 46.94 E-value: 2.04e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 292 DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLA---------AESSYDK---LDCTVqealqhRSEWFEGVQ 359
Cdd:cd04632    10 DDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVvrpgtktrgGDRGGEKermLDLPV------YDIMSSPVV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 360 TCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:cd04632    84 TVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126

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

Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 45.89 E-value: 3.24e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFL--SLYMRDLPRP--SFMSctprelgigawG 284
Cdd:cd04629     3 RNPVTLTPDTSILEAVELLLEHKISGAPVVD-EQGRLVGFLSEQDCLKALleASYHCEPGGTvaDYMS-----------T 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIdENGRVV 320
Cdd:cd04629    71 EVLTVSPDTSIVDLAQLFLKNKPRRYPVV-EDGKLV 105

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: 43.66 E-value: 4.15e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1831511673  127 LVVFDTHLPVRKAFYALVYNGVRAAPLWDtDNQRFTGMLTITDFIKIL 174
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVD-EEGRLVGIVTRRDIIKAL 48

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 45.98 E-value: 4.23e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 124 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDtDNQRFTGMLTITDfikILCKHYDKGDNSERIRAledQQISHwrdqfe 203
Cdd:COG2905     6 SRDVVTVSPDATVREAARLMTEKGVGSLVVVD-DDGRLVGIITDRD---LRRRVLAEGLDPLDTPV---SEVMT------ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1831511673 204 ldgtlRPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMKFLS 259
Cdd:COG2905    73 -----RPPITVSPDDSLAEALELMEEHRIRHLPVVDD--GKLVGIVSITDLLRALS 121

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: 46.11 E-value: 4.52e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 205 DGTLRPFVyIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKflSLYMRDLPRPS--FMSCTPRELGIGA 282
Cdd:cd17785     7 LITKKPSV-VHENTSIRDVIDKMIEDPKTRSVYVVDDDEKLLGIITLMELLK--YIGYRFGVTIYkgVSFGLLLRISLKE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 283 -WGDIL----CCHVDTPIHDALELFLKNRVSALPLIDENGRVV 320
Cdd:cd17785    84 kAKDIMlspiYVKKEDTLEEALELMVKNRLQELPVVDENGKVI 126

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: 44.92 E-value: 8.12e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLSLYMRDLPRpsFMSCtprelgigawgDILC 288
Cdd:cd04605     8 KDVATIREDISIEEAAKIMIDKNVTHLPVVS-EDGKLIGIVTSWDISKAVALKKDSLEE--IMTR-----------NVIT 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1831511673 289 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDI 322
Cdd:cd04605    74 ARPDEPIELAARKMEKHNISALPVVDDDRRVIGI 107

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: 44.33 E-value: 9.28e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 212 VYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILThKRIMKFLSlyMRDLPRPSFMscTPRELGIGAwgdilccHV 291
Cdd:cd04601     5 VTLSPDATVADVLELKAEYGISGVPVTEDG-GKLVGIVT-SRDIRFET--DLSTPVSEVM--TPDERLVTA-------PE 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831511673 292 DTPIHDALELFLKNRVSALPLIDENGRVVDI 322
Cdd:cd04601    72 GITLEEAKEILHKHKIEKLPIVDDNGELVGL 102

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

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 44.24 E-value: 1.97e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrkTGNITYILTHKRIMKFLSlYMRDLPRPS------FMSCTPRELgigA 282
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFG-SHEAKKRLTtgdideAYSTPVEEI---M 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1831511673 283 WGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 329
Cdd:cd17778    82 SKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128

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: 41.73 E-value: 2.32e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1831511673  210 PFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL 258
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKAL 48

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: 43.32 E-value: 2.68e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKFLSLYMRDLPRPSFMSCTPRELGigawgdilc 288
Cdd:cd17772     2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIYHGLGDLPVSEYMTTEFATVT--------- 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1831511673 289 chVDTPIHDALELFLKNRVSALPLIdENGRVV 320
Cdd:cd17772    73 --PDAPLSEIQEIIVEQRQRLVPVV-EDGRLV 101

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: 42.87 E-value: 3.28e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 289 CHVDTPIHDALELFLKNRVSALPLIdENGRVVDIYAKFDVislaaessyDKldcTVQEALQH---RSEWFEGVQTCLETD 365
Cdd:cd04595     7 VSPDTTIEEARKIMLRYGHTGLPVV-EDGKLVGIISRRDV---------DK---AKHHGLGHapvKGYMSTNVITIDPDT 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1831511673 366 SLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 402
Cdd:cd04595    74 SLEEAQELMVEHDIGRLPVVE-EGKLVGIVTRSDVLR 109

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 43.36 E-value: 3.70e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 207 TLRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKflslYMRDLPRPSFMSctprelgigawGDI 286
Cdd:COG4109    23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDEN-GRLVGIVTSKDILG----KDDDTPIEDVMT-----------KNP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 287 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 329
Cdd:COG4109    87 ITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 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).

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 42.62 E-value: 4.10e-05

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1831511673 360 TCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 405
Cdd:cd02205     6 TVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51

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: 42.69 E-value: 4.18e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 289 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDkLDCTVQEALQHRSEWFEgvqtclETDSLF 368
Cdd:cd17771     9 CSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQID-LDAPISEVMTPDPVRLP------PSASAF 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1831511673 369 QVLEAIVKAEVHRLIVTDQDkKVVGVVSLSDIL 401
Cdd:cd17771    82 EAALLMAEHGFRHVCVVDNG-RLVGVVSERDLF 113

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

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 43.09 E-value: 4.41e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 124 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLwdTDNQRFTGMLTITDFIKILCKHYDKGDNSERiraledqQISHWRDQFE 203
Cdd:cd17778     7 TTPVVTIYPDDTLKEAMELMVTRGFRRLPV--VSGGKLVGIVTAMDIVKYFGSHEAKKRLTTG-------DIDEAYSTPV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1831511673 204 LDGTLRPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIM 255
Cdd:cd17778    78 EEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVD-DEGELKGIITERDVL 128

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 42.89 E-value: 4.91e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1831511673 356 EGVQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLVLD 407
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAE 58

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: 42.48 E-value: 6.42e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 274 TPRElgigawgDILCCHVDTPIHDALELFLKNRVSALPLIDEN-GRVVDI-YAKfDVISLAAEssyDKLDCTVQEALqhR 351
Cdd:cd04590     7 TPRT-------DVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVlHVK-DLLAALLE---GREKLDLRALL--R 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831511673 352 SEWFegVQtclETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDIL 401
Cdd:cd04590    74 PPLF--VP---ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118

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: 42.39 E-value: 6.71e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDEnGRVVDIYAKFDVisLAAESSYDKL--DCTVQEALQHRSEWFEGVQTcl 362
Cdd:cd17776     4 DVVTVDADASLEDAAERMLRNRVGSVVVTDD-GTPAGILTETDA--LHAGYATDDPfsEIPVRAVASRPLVTISPTAT-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831511673 363 etdsLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKN 403
Cdd:cd17776    79 ----LREAAERMVDEGVKKLPVVD-GLDLVGILTATDIIRA 114

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: 42.23 E-value: 7.11e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 290 HVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDvISLAAESSYDKLdctvqEALQHRSewfegVQTCLETDSLFQ 369
Cdd:cd04605    14 REDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWD-ISKAVALKKDSL-----EEIMTRN-----VITARPDEPIEL 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831511673 370 VLEAIVKAEVHRLIVTDQDKKVVGVVSLSDI 400
Cdd:cd04605    83 AARKMEKHNISALPVVDDDRRVIGIITSDDI 113

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 42.17 E-value: 7.58e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 290 HVDTPIHDALELFLKNRVSALPLIdENGRVVDIYAKFDVISLAAEssyDKLDCTVQEALQhrsewfEGVQTCLETDSLFQ 369
Cdd:cd04801    11 TPEMTVSELLDRMFEEKHLGYPVV-ENGRLVGIVTLEDIRKVPEV---EREATRVRDVMT------KDVITVSPDADAME 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1831511673 370 VLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 402
Cdd:cd04801    81 ALKLMSQNNIGRLPVVE-DGELVGIISRTDLMR 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: 41.64 E-value: 9.65e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 212 VYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHkrimkflslymRDL----------PRpsfmSCTPRELgig 281
Cdd:cd04622     6 VTVSPDTTLREAARLMRDLDIGALPVCEG--DRLVGMVTD-----------RDIvvravaegkdPN----TTTVREV--- 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831511673 282 AWGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIyakfdvISLA 332
Cdd:cd04622    66 MTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGI------VSLG 110

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: 42.33 E-value: 1.00e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 275 PRELGIGAWGDILCCHVDTPIHDALELFLKNRVSALPLIDENgRVVDIYAKFDVISLAAESSYDKL--DCT---VQEALq 349
Cdd:cd17777     1 EKELMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDEN-KLEGILSARDLVSYLGGGCLFKIveSRHqgdLYSAL- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 350 hRSEWFEGVQT-----CLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNL 404
Cdd:cd17777    79 -NREVVETIMTpnpvyVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL 137

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: 43.53 E-value: 2.25e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 212 VYIDPNESLHRAVELLCESKVHRLPVLDRKT--GnityILThKRIMKFLSLYmrDLPRPSFMscTPRELgIGAwgdilcc 289
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVDDGKlvG----IVT-NRDLRFETDL--SQPVSEVM--TKENL-VTA------- 153

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1831511673 290 HVDTPIHDALELFLKNRVSALPLIDENGRVV 320
Cdd:pfam00478 154 PEGTTLEEAKEILHKHKIEKLPVVDDNGRLV 184

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 41.05 E-value: 2.43e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831511673 328 VISlaaeSSYD--KLDCTVQEALQHRSewfegVQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDIL 401
Cdd:COG4109     4 IIS----TSYDtfKEILLVEDIMTLED-----VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL 70

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: 40.26 E-value: 3.30e-04

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDI 322
Cdd:cd17781    69 NPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGV 106

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: 40.39 E-value: 3.47e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 212 VYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLSLYMRDLPRPSFMSCTPRELGIGAWgDILCCHV 291
Cdd:cd04632     5 ITVNEDDTIGKAINLLREHGISRLPVVD-DNGKLVGIVTTYDIVDFVVRPGTKTRGGDRGGEKERMLDLPVY-DIMSSPV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1831511673 292 -----DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVIS 330
Cdd:cd04632    83 vtvtrDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126

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

Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 39.32 E-value: 6.64e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLSLYMRD-LPRP--SFMSCtprelgigawgD 285
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDG-GRLVGILSERDYVRKLALRGASsLDTPvsEIMTR-----------D 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1831511673 286 ILCCHVDTPIHDALELFLKNRVSALPLIDeNGRVVDI 322
Cdd:cd04623    70 VVTCTPDDTVEECMALMTERRIRHLPVVE-DGKLVGI 105

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: 38.86 E-value: 9.27e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1831511673 212 VYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIM 255
Cdd:cd04599    64 VTISPEASLWEAKELMEEHGIERLVVVEE--GRLVGIITKSTLY 105

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 40.25 E-value: 1.04e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1831511673 358 VQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 404
Cdd:COG2524    96 VITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKAL 141

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: 38.70 E-value: 1.37e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1831511673 366 SLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLVL 406
Cdd:cd04640    15 SADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPL 55

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: 38.63 E-value: 1.39e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 212 VYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKFLSLYMRDLPRPSFMsctpRElgigawgdILCCHV 291
Cdd:cd04590    13 VALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALL----RP--------PLFVPE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1831511673 292 DTPIHDALELFLKNRVS-ALpLIDENGRVV 320
Cdd:cd04590    81 TTPLDDLLEEFRKERSHmAI-VVDEYGGTA 109

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

Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 38.19 E-value: 1.71e-03

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1831511673 290 HVDTPIHDALELFLKNRVSALPLIDENGRVVDI 322
Cdd:cd04607    72 SPSTSREELLALMRAKKILQLPIVDEQGRVVGL 104

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: 38.33 E-value: 1.77e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL-------SLYMRDLPRPSFMSCTPrelgig 281
Cdd:cd04613     3 RKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQ-GRLTGILSIQDVRGVLfeeelwdLVVVKDLATTDVITVTP------ 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831511673 282 awgdilcchvDTPIHDALELFLKNRVSALPLIDEN--GRVVDIYAKFDVIS 330
Cdd:cd04613    76 ----------DDDLYTALLKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVIA 116

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: 38.27 E-value: 1.87e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 135 PVRKAFYALVYNGVRAAPLWDTDNqRFTGMLTITDFIKILCkhyDKGDNSERIRaledqqishwrdqfelDGTLRPFVYI 214
Cdd:cd09836    13 TIREAAKLMAENNIGSVVVVDDDG-KPVGIVTERDIVRAVA---EGIDLDTPVE----------------EIMTKNLVTV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1831511673 215 DPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLS 259
Cdd:cd09836    73 SPDESIYEAAELMREHNIRHLPVVD-GGGKLVGVISIRDLARELS 116

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: 36.04 E-value: 2.52e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831511673 124 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDTDNqRFTGMLTITDFIKIL 174
Cdd:pfam00571   6 TKDVVTVSPDTTLEEALELMREHGISRLPVVDEDG-KLVGIVTLKDLLRAL 55

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

Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 36.92 E-value: 3.62e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMkflsLYMRDLPRPSFMSctprelgigawGDILC 288
Cdd:cd04610     3 RDVITVSPDDTVKDVIKLIKETGHDGFPVVDD--GKVVGYVTAKDLL----GKDDDEKVSEIMS-----------RDTVV 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1831511673 289 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 329
Cdd:cd04610    66 ADPDMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106

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: 37.54 E-value: 3.97e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRK---TGNITYI--LTHKRIMKFLSLYMRDLPRPSFMSCTPRELGigaw 283
Cdd:cd04600     3 RDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRArrlVGIVTLAdlLKHADLDPPRGLRGRLRRTLGLRRDRPETVG---- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1831511673 284 gDILCCHV-----DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 329
Cdd:cd04600    79 -DIMTRPVvtvrpDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128

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: 37.13 E-value: 4.05e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 284 GDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVIS--LAAESsydKLDCTVQEALQHRsewFE--GVQ 359
Cdd:cd04608    10 GAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSslLAGRA---QPSDPVSKAMYKQ---FKqvDLD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 360 TCLETdsLFQVLEaivkaEVHRLIVTDQDKKVVGVVSLSDILK 402
Cdd:cd04608    84 TPLGA--LSRILE-----RDHFALVVDGQGKVLGIVTRIDLLN 119

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: 37.17 E-value: 4.06e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 292 DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLdCTVQEALQhrsewfEGVQTCLETDSLFQVL 371
Cdd:cd04613    11 GMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEELWDL-VVVKDLAT------TDVITVTPDDDLYTAL 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1831511673 372 EAIVKAEVHRLIVTDQD--KKVVGVVSLSDIL 401
Cdd:cd04613    84 LKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVI 115

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: 37.40 E-value: 4.50e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1831511673 358 VQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 404
Cdd:cd04584    10 VVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRAS 55

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: 37.31 E-value: 4.56e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1831511673 356 EGVQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 404
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVKYF 55

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: 36.73 E-value: 5.47e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 292 DTPIHDALELFLKNRVSALPLIDENGRVVDIyakFDVISLaaESSYDKlDCTVQEALQHRsewfegVQTCLETDSLFQVL 371
Cdd:cd04583    10 ERTLAQAIEIMREKRVDSLLVVDKDNVLLGI---VDIEDI--NRNYRK-AKKVGEIMERD------VFTVKEDSLLRDTV 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1831511673 372 EAIVKAEVHRLIVTDQDKKVVGVV---SLSDIL 401
Cdd:cd04583    78 DRILKRGLKYVPVVDEQGRLVGLVtraSLVDIV 110

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

Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 38.95 E-value: 5.70e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 274 TPRElgigawgDILCCHVDTPIHDALELFLKNRVSALPLIDENgrvVD-----IYAKfDVISLAAESSYDKLDCTVQEAL 348
Cdd:COG1253   221 TPRT-------DVVALDLDDTLEEALELILESGHSRIPVYEGD---LDdivgvVHVK-DLLRALLEGEPFDLRDLLRPPL 289

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1831511673 349 qhrsewfegvqTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 405
Cdd:COG1253   290 -----------FVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIV 335

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: 36.58 E-value: 8.05e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 210 PFVYIDPNESLHRAVELLCESKVHRLPVLDrkTGNITY-ILTHKRIMKFLSLYMRDLPRP--SFMS--CTpreLGIGAWG 284
Cdd:cd04592     4 RYITVLMSTTLKEAVLLMLEEKQSCALIVD--SDDFLIgILTLGDIQRFLKRAKADNEDPktILVSsiCT---RNGGYCR 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1831511673 285 DILCCHVDTPIHDALELFLKNRVSALPLIDENG 317
Cdd:cd04592    79 GLWTCTPDMDLLTAKMLMEARGINQLPVVKRGG 111

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: 35.78 E-value: 8.90e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831511673 209 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHkrimkflslymRDLPRpsfmsCTPRELGIGAWG-DIL 287
Cdd:cd04599     3 RNPITISPLDSVARAAALMERQRIGGLPVVEN--GKLVGIITS-----------RDVRR-----AHPNRLVADAMSrNVV 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1831511673 288 CCHVDTPIHDALELFLKNRVSALPLIdENGRVVDIYAKFDVIS 330
Cdd:cd04599    65 TISPEASLWEAKELMEEHGIERLVVV-EEGRLVGIITKSTLYL 106