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Conserved domains on  [gi|663515933|gb|AIF06399|]
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putative signal transduction protein [uncultured marine group II/III euryarchaeote KM3_191_F05]

Protein Classification

CBS domain-containing protein( domain architecture ID 10333812)

CBS (cystathione beta synthase) domain-containing protein may bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet; similar to protein SDS23 involved in DNA replication and cell separation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 121-270 4.47e-71

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


:

Pssm-ID: 341386 [Multi-domain]  Cd Length: 150  Bit Score: 215.22  E-value: 4.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 121 CLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDATDVSERVSVSEMGVAADEDPWSWDGLRDI 200
Cdd:cd04614    1 YAGKGVVPVWDETPLPVALRAMRLANVPAAPVLDSEGKLVGIVTERDLIDVSRIVESEEESGMSIADDEDEWSWEGIRDV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 201 MRVYHSERRLFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKV 270
Cdd:cd04614   81 MSLYYPTSNVELPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDLLKA 150
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 1-106 6.06e-29

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).


The actual alignment was detected with superfamily member cd04638:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 109  Bit Score: 105.89  E-value: 6.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREETMELAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARK 80
Cdd:cd04638    1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKETGKLVGIVTRKDLLRNPDEEQIALLMSRDPITISPDDTLSEAAEL 80

                         90       100
                 ....*....|....*....|....*.
gi 663515933  81 FLELGFNHLPVIEGGVVVGIVTPTNL 106
Cdd:cd04638   81 MLEHNIRRVPVVDDDKLVGIVTVADL 106
 
Name Accession Description Interval E-value
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 121-270 4.47e-71

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


Pssm-ID: 341386 [Multi-domain]  Cd Length: 150  Bit Score: 215.22  E-value: 4.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 121 CLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDATDVSERVSVSEMGVAADEDPWSWDGLRDI 200
Cdd:cd04614    1 YAGKGVVPVWDETPLPVALRAMRLANVPAAPVLDSEGKLVGIVTERDLIDVSRIVESEEESGMSIADDEDEWSWEGIRDV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 201 MRVYHSERRLFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKV 270
Cdd:cd04614   81 MSLYYPTSNVELPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDLLKA 150
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 1-106 6.06e-29

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


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 105.89  E-value: 6.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREETMELAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARK 80
Cdd:cd04638    1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKETGKLVGIVTRKDLLRNPDEEQIALLMSRDPITISPDDTLSEAAEL 80

                         90       100
                 ....*....|....*....|....*.
gi 663515933  81 FLELGFNHLPVIEGGVVVGIVTPTNL 106
Cdd:cd04638   81 MLEHNIRRVPVVDDDKLVGIVTVADL 106
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-107 2.26e-21

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 87.23  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEvPGNR-TDVLHLMIKHHISGVPVVREEtMELAGFVSRNDIFN------------NTGEEQVAMIMTSDVVS 67
Cdd:COG3448    8 MTRDVVTVS-PDTTlREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRallpdrldeleeRLLDLPVEDVMTRPVVT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 663515933  68 VTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:COG3448   86 VTPDTPLEEAAELMLEHGIHRLPVVdDDGRLVGIVTRTDLL 126
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
56-171 1.94e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 81.84  E-value: 1.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  56 QVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL---------PLVAANGDVTVQDCLEGG 125
Cdd:COG3448    3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLrallpdrldELEERLLDLPVEDVMTRP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663515933 126 CVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:COG3448   83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRA 128
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 57-107 4.81e-08

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: 4.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 663515933   57 VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVdEDGKLVGIVTLKDLL 52
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 50-168 3.75e-07

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: 50.85  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   50 NNTGEEQVAMI---------MTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPlvAANGDVTVQD 120
Cdd:pfam00478  66 NMSIEEQAEEVrkvkrsesgMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDLRF--ETDLSQPVSE 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 663515933  121 CL-EGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:pfam00478 144 VMtKENLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 64-107 1.44e-06

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: 44.43  E-value: 1.44e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 663515933    64 DVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLVGIVTRRDII 45
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
59-171 1.59e-04

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 42.81  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  59 MIMTSDVVsVTPNSTVVSAARKFLELGFNHLPVIEG-GVVVGIVTPTNLLPLVAANGDVTVQDCLEGGCVPLHRLTP--- 134
Cdd:PRK01862 452 LIQPAQTV-VPPTASVADMTRVFLEYPVKYLYVVDDdGRFRGAVALKDITSDLLDKRDTTDKTAADYAHTPFPLLTPdmp 530

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663515933 135 LGAALRIMRLSGARAMPVL--GKRGLLCGIVTDRDLFDA 171
Cdd:PRK01862 531 LGDALEHFMAFQGERLPVVesEASPTLAGVVYKTSLLDA 569
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 237-272 5.73e-04

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: 37.11  E-value: 5.73e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 663515933   237 VAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVLL 272
Cdd:smart00116  14 ALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
 
Name Accession Description Interval E-value
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 121-270 4.47e-71

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


Pssm-ID: 341386 [Multi-domain]  Cd Length: 150  Bit Score: 215.22  E-value: 4.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 121 CLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDATDVSERVSVSEMGVAADEDPWSWDGLRDI 200
Cdd:cd04614    1 YAGKGVVPVWDETPLPVALRAMRLANVPAAPVLDSEGKLVGIVTERDLIDVSRIVESEEESGMSIADDEDEWSWEGIRDV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 201 MRVYHSERRLFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKV 270
Cdd:cd04614   81 MSLYYPTSNVELPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGMLRDVDLLKA 150
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 1-106 6.06e-29

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


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 105.89  E-value: 6.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREETMELAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARK 80
Cdd:cd04638    1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKETGKLVGIVTRKDLLRNPDEEQIALLMSRDPITISPDDTLSEAAEL 80

                         90       100
                 ....*....|....*....|....*.
gi 663515933  81 FLELGFNHLPVIEGGVVVGIVTPTNL 106
Cdd:cd04638   81 MLEHNIRRVPVVDDDKLVGIVTVADL 106
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-107 2.26e-21

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 87.23  E-value: 2.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEvPGNR-TDVLHLMIKHHISGVPVVREEtMELAGFVSRNDIFN------------NTGEEQVAMIMTSDVVS 67
Cdd:COG3448    8 MTRDVVTVS-PDTTlREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRallpdrldeleeRLLDLPVEDVMTRPVVT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 663515933  68 VTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:COG3448   86 VTPDTPLEEAAELMLEHGIHRLPVVdDDGRLVGIVTRTDLL 126
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 15-107 1.20e-19

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 81.72  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  15 TDVLHLMIKHHISGVPVVrEETMELAGFVSR--------NDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGF 86
Cdd:cd04629   15 LEAVELLLEHKISGAPVV-DEQGRLVGFLSEqdclkallEASYHCEPGGTVADYMSTEVLTVSPDTSIVDLAQLFLKNKP 93

                         90       100
                 ....*....|....*....|.
gi 663515933  87 NHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04629   94 RRYPVVEDGKLVGQISRRDVL 114
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
56-171 1.94e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 81.84  E-value: 1.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  56 QVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL---------PLVAANGDVTVQDCLEGG 125
Cdd:COG3448    3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVTERDLLrallpdrldELEERLLDLPVEDVMTRP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663515933 126 CVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:COG3448   83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRA 128
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-107 6.09e-19

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 82.62  E-value: 6.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREEtmELAGFVSRNDIFNNTGEE------QVAMIMTSDVVSVTPNSTV 74
Cdd:COG2524   92 MTKDVITVSPDTTLEEALELMLEKGISGLPVVDDG--KLVGIITERDLLKALAEGrdlldaPVSDIMTRDVVTVSEDDSL 169

                         90       100       110
                 ....*....|....*....|....*....|....
gi 663515933  75 VSAARKFLELGFNHLPVIE-GGVVVGIVTPTNLL 107
Cdd:COG2524  170 EEALRLMLEHGIGRLPVVDdDGKLVGIITRTDIL 203
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 1-107 1.75e-18

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 79.10  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICaeVPGNRT--DVLHLMIKHHISGVPVVrEETMELAGFVSRNDIFN-------NTGEEQVAMIMTSDVVSVTPN 71
Cdd:COG2905    5 MSRDVVT--VSPDATvrEAARLMTEKGVGSLVVV-DDDGRLVGIITDRDLRRrvlaeglDPLDTPVSEVMTRPPITVSPD 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 663515933  72 STVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:COG2905   82 DSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLL 117
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
56-171 1.84e-18

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 81.08  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  56 QVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPLVAANG---DVTVQDCLEGGCVPLHRL 132
Cdd:COG2524   87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGRdllDAPVSDIMTRDVVTVSED 166

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:COG2524  167 DSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRA 205
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-107 3.55e-18

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: 78.63  E-value: 3.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVV-----------------REETMELAGFVSRNDIFNNTGEE-------- 55
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVdddgklvgivsegdllrREEPGTEPRRVWWLDALLESPERlaeeyvka 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663515933  56 ---QVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04586   81 hgrTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLL 135
CBS COG0517
CBS domain [Signal transduction mechanisms];
1-107 4.22e-18

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 77.98  E-value: 4.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREEtMELAGFVSRNDI-------FNNTGEEQVAMIMTSDVVSVTPNST 73
Cdd:COG0517    7 MTTDVVTVSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLrralaaeGKDLLDTPVSEVMTRPPVTVSPDTS 85

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 663515933  74 VVSAARKFLELGFNHLPVIEG-GVVVGIVTPTNLL 107
Cdd:COG0517   86 LEEAAELMEEHKIRRLPVVDDdGRLVGIITIKDLL 120
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-107 5.82e-18

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: 77.85  E-value: 5.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEvPGNR-TDVLHLMIKHHISGVPVVREEtmELAGFVSRNDIFNN------TGEEQ----------VAMIMTS 63
Cdd:cd04584    6 MTKNVVTVT-PDTSlAEARELMKEHKIRHLPVVDDG--KLVGIVTDRDLLRAspskatSLSIYelnyllskipVKDIMTK 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 663515933  64 DVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04584   83 DVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDIL 126
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
117-272 1.13e-17

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 77.21  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 117 TVQDCLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLfdatdvservsvsemgvaadedpwswdg 196
Cdd:COG3448    3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDL---------------------------- 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933 197 LRDIMRVYHSERRLFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVLL 272
Cdd:COG3448   55 LRALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS COG0517
CBS domain [Signal transduction mechanisms];
56-171 4.66e-17

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 75.29  E-value: 4.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  56 QVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAANG----DVTVQDCLEGGCVPLH 130
Cdd:COG0517    2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVdEDGKLVGIVTDRDLRRALAAEGkdllDTPVSEVMTRPPVTVS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 663515933 131 RLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:COG0517   82 PDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKA 122
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 57-171 1.42e-16

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: 73.99  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  57 VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVT--------PTNLLPLVAANGD-----VTVQDCLE 123
Cdd:cd04584    2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTdrdllrasPSKATSLSIYELNyllskIPVKDIMT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 663515933 124 GGCVPLHRLTPLGAALRIMRLSGARAMPVLGKrGLLCGIVTDRDLFDA 171
Cdd:cd04584   82 KDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRA 128
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 16-107 1.65e-16

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: 73.43  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREETmELAGFVSRNDIFNNTGEEQ------VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHL 89
Cdd:cd02205   15 EALELMAENGIGALPVVDDDG-KLVGIVTERDILRALVEGGlaldtpVAEVMTPDVITVSPDTDLEEALELMLEHGIRRL 93

                         90
                 ....*....|....*....
gi 663515933  90 PVIEG-GVVVGIVTPTNLL 107
Cdd:cd02205   94 PVVDDdGKLVGIVTRRDIL 112
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
16-107 1.91e-16

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 73.79  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREEtMELAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEG- 94
Cdd:COG4109   38 DALELLEKTGHSRFPVVDEN-GRLVGIVTSKDILGKDDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDd 116

                         90
                 ....*....|...
gi 663515933  95 GVVVGIVTPTNLL 107
Cdd:COG4109  117 GRLLGIISRQDVL 129
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 62-170 4.68e-16

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: 72.28  E-value: 4.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  62 TSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAANG---DVTVQDCLEGGCVPLHRLTPLGA 137
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVdDDGKLVGIVTERDILRALVEGGlalDTPVAEVMTPDVITVSPDTDLEE 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 663515933 138 ALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFD 170
Cdd:cd02205   81 ALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 60-171 1.09e-15

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 71.87  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  60 IMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPLVAAN--------------GDVTVQDCLEGG 125
Cdd:cd04631    5 YMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMRYLGSGeafeklktgnihevLNVPISSIMKRD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 663515933 126 CVPLHRLTPLGAALRIMRLSGARAMPVLgKRGLLCGIVTDRDLFDA 171
Cdd:cd04631   85 IITTTPDTDLGEAAELMLEKNIGALPVV-DDGKLVGIITERDILRA 129
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 16-107 1.78e-15

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 70.60  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREEtmELAGFVSRNDI----FNNTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPV 91
Cdd:cd04595   15 EARKIMLRYGHTGLPVVEDG--KLVGIISRRDVdkakHHGLGHAPVKGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPV 92

                         90
                 ....*....|....*.
gi 663515933  92 IEGGVVVGIVTPTNLL 107
Cdd:cd04595   93 VEEGKLVGIVTRSDVL 108
CBS COG0517
CBS domain [Signal transduction mechanisms];
116-272 2.38e-15

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 70.66  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 116 VTVQDCLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLfdatdvservsvsemgvaadedpwswd 195
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDL--------------------------- 53

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663515933 196 glrdimRVYHSERRLFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVLL 272
Cdd:COG0517   54 ------RRALAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
57-271 1.42e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 70.68  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  57 VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPLVAANGDVTVQDCLEGGCVPLHRLTPLG 136
Cdd:COG2524   27 AALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 137 AALRIMRLSGARAMPVLgKRGLLCGIVTDRDLFDATDvservsvsemgvaadedpwswdglrdimrvyhseRRLFLPDVP 216
Cdd:COG2524  107 EALELMLEKGISGLPVV-DDGKLVGIITERDLLKALA----------------------------------EGRDLLDAP 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663515933 217 VEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVL 271
Cdd:COG2524  152 VSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 2-107 6.43e-14

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


Pssm-ID: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 66.44  E-value: 6.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   2 TSPVIcaEVPGNRT--DVLHLMIKHHISGVPVVREETMELAGFVSRND----IFNNTGEEQVAMIMTSDVVSVTPNSTVV 75
Cdd:cd17772    1 SSPVI--SVEPDTTiaEAAELMTRYNINALPVVDGGTGRLVGIITRQVaekaIYHGLGDLPVSEYMTTEFATVTPDAPLS 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 663515933  76 SAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd17772   79 EIQEIIVEQRQRLVPVVEDGRLVGVITRTDLL 110
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 57-171 8.52e-14

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 66.39  E-value: 8.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  57 VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEG-GVVVGIVTPTNLLPLVAANG----DVTVQDCLEGGCVPLHR 131
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDdGRLVGIITDRDLRRRVLAEGldplDTPVSEVMTRPPITVSP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 663515933 132 LTPLGAALRIMRLSGARAMPVLgKRGLLCGIVTDRDLFDA 171
Cdd:COG2905   81 DDSLAEALELMEEHRIRHLPVV-DDGKLVGIVSITDLLRA 119
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 56-171 2.10e-13

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 65.43  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  56 QVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPLV---AANGDVTVQDCLEGGCVPLHRL 132
Cdd:cd17778    1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYFgshEAKKRLTTGDIDEAYSTPVEEI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 -----------TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:cd17778   81 mskevvtiepdADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIA 130
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 61-168 2.82e-13

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: 64.75  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  61 MTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNL-LPLVAANGD---VTVQDCLEGGCVPLHRLTPLG 136
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIvVRAVAEGKDpntTTVREVMTGDVVTCSPDDDVE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 663515933 137 AALRIMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:cd04622   81 EAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 133-273 3.32e-13

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: 64.89  E-value: 3.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDAtdvservsvsemgvAADEDPWSWDGlrdimRVYHSERRLFL 212
Cdd:cd04600   12 TSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKH--------------ADLDPPRGLRG-----RLRRTLGLRRD 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663515933 213 PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVLLT 273
Cdd:cd04600   73 RPETVGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLIAALYR 133
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 61-168 1.48e-12

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: 62.94  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  61 MTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVV-VGIVTPTNLLPLVAANG----DVTVQDCLEGGCVPLHRLTPL 135
Cdd:cd17775    1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKpVGIVTDRDIVVEVVAKGldpkDVTVGDIMSADLITAREDDGL 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 663515933 136 GAALRIMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:cd17775   81 FEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 127-269 1.57e-12

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 62.65  E-value: 1.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 127 VPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDAtdvservsvsemgvaadedpwswdglrdimrvyhS 206
Cdd:cd02205    5 VTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRA----------------------------------L 50

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663515933 207 ERRLFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:cd02205   51 VEGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-107 2.13e-12

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


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 62.44  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICaeVPGNRT--DVLHLMIKHHISGVPVVREEtmELAGFVSRNDIFN------NTGEEQVAMIMTSDVVSVTPNS 72
Cdd:cd04587    2 MSRPPVT--VPPDATiqEAAQLMSEERVSSLLVVDDG--RLVGIVTDRDLRNrvvaegLDPDTPVSEIMTPPPVTIDADA 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 663515933  73 TVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04587   78 LVFEALLLMLERNIHHLPVVDDGRVVGVVTATDLM 112
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 1-107 4.69e-12

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


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 61.43  E-value: 4.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREEtmELAGFVSRNDIFNNTGEEQVAM----IMTSDVVSVTPNSTVVS 76
Cdd:cd04801    3 MTPEVVTVTPEMTVSELLDRMFEEKHLGYPVVENG--RLVGIVTLEDIRKVPEVEREATrvrdVMTKDVITVSPDADAME 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663515933  77 AARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04801   81 ALKLMSQNNIGRLPVVEDGELVGIISRTDLM 111
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 1-107 7.63e-12

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: 61.00  E-value: 7.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREETmELAGFVSRNDIFN-----NTGEEQVAMIMTSDVVSVTPNSTVV 75
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDG-KPVGIVTERDIVRavaegIDLDTPVEEIMTKNLVTVSPDESIY 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 663515933  76 SAARKFLELGFNHLPVIEGGV-VVGIVTPTNLL 107
Cdd:cd09836   80 EAAELMREHNIRHLPVVDGGGkLVGVISIRDLA 112
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 16-101 8.05e-12

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: 60.51  E-value: 8.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREETmELAGFVSRNDIFN-------NTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNH 88
Cdd:cd04623   15 EALRLLAEKNIGALVVVDDGG-RLVGILSERDYVRklalrgaSSLDTPVSEIMTRDVVTCTPDDTVEECMALMTERRIRH 93

                         90
                 ....*....|...
gi 663515933  89 LPVIEGGVVVGIV 101
Cdd:cd04623   94 LPVVEDGKLVGIV 106
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-112 8.67e-12

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 61.04  E-value: 8.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEvPGNR-TDVLHLMIKHHISGVPVVREETmELAGFVSRNDIFNNTG---------------------EEQVA 58
Cdd:cd04600    1 MSRDVVTVT-PDTSlEEAWRLLRRHRIKALPVVDRAR-RLVGIVTLADLLKHADldpprglrgrlrrtlglrrdrPETVG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663515933  59 MIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNllpLVAA 112
Cdd:cd04600   79 DIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVdADGRLVGIVTQSD---LIAA 130
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 61-167 2.33e-11

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 59.26  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  61 MTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLplvAANGDVTVQDCLEGGCVPLHRLTPLGAALR 140
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLL---GKDDDEKVSEIMSRDTVVADPDMDITDAAR 77

                         90       100
                 ....*....|....*....|....*..
gi 663515933 141 IMRLSGARAMPVLGKRGLLCGIVTDRD 167
Cdd:cd04610   78 VIFRSGISKLPVVDDEGNLVGIITNMD 104
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 118-273 2.72e-11

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 59.46  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 118 VQDCLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLfdatdvservsvsemgvaadedpwswdgl 197
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDL----------------------------- 51

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933 198 rdimRVYHSERRLFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDaEGKLTGMIYCQDLLKVLLT 273
Cdd:COG2905   52 ----RRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRALSE 122
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-107 3.39e-11

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 58.89  E-value: 3.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREETmeLAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARK 80
Cdd:cd04599    1 MTRNPITISPLDSVARAAALMERQRIGGLPVVENGK--LVGIITSRDVRRAHPNRLVADAMSRNVVTISPEASLWEAKEL 78

                         90       100
                 ....*....|....*....|....*..
gi 663515933  81 FLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04599   79 MEEHGIERLVVVEEGRLVGIITKSTLY 105
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
133-269 3.92e-11

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 59.54  E-value: 3.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDAtdvservsvsemgvaadedpwswdglrdimrvyhserrlfL 212
Cdd:COG4109   34 DTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK----------------------------------------D 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663515933 213 PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:COG4109   74 DDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 57-168 1.79e-10

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: 57.25  E-value: 1.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  57 VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAANGDvTVQDCLEGGCVPLHRLTPL 135
Cdd:cd04605    2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVsEDGKLIGIVTSWDISKAVALKKD-SLEEIMTRNVITARPDEPI 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 663515933 136 GAALRIMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:cd04605   81 ELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 16-102 2.68e-10

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 56.32  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREEtMELAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EG 94
Cdd:cd04596   15 DYKQLSEETGHSRFPVVDEE-NRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVdEN 93


                 ....*...
gi 663515933  95 GVVVGIVT 102
Cdd:cd04596   94 RKLLGVIS 101
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
60-171 3.70e-10

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 56.84  E-value: 3.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  60 IMTS-DVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLplvAANGDVTVQDCLEGGCVPLHRLTPLGA 137
Cdd:COG4109   21 IMTLeDVATLSEDDTVEDALELLEKTGHSRFPVVdENGRLVGIVTSKDIL---GKDDDTPIEDVMTKNPITVTPDTSLAS 97

                         90       100       110
                 ....*....|....*....|....*....|....
gi 663515933 138 ALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:COG4109   98 AAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKA 131
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 1-102 4.97e-10

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: 55.79  E-value: 4.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVIcaEVPGNRT--DVLHLMIKHHISGVPVVREETMElaGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAA 78
Cdd:cd04610    1 MTRDVI--TVSPDDTvkDVIKLIKETGHDGFPVVDDGKVV--GYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITDAA 76

                         90       100
                 ....*....|....*....|....*
gi 663515933  79 RKFLELGFNHLPVI-EGGVVVGIVT 102
Cdd:cd04610   77 RVIFRSGISKLPVVdDEGNLVGIIT 101
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 17-107 1.19e-09

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: 55.03  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  17 VLHLMIKHHISGVPVVREETmELAGFVSRNDIFNNT-------------GEEQ------VAMIMTSDVVSVTPNSTVVSA 77
Cdd:cd04632   16 AINLLREHGISRLPVVDDNG-KLVGIVTTYDIVDFVvrpgtktrggdrgGEKErmldlpVYDIMSSPVVTVTRDATVADA 94

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663515933  78 ARKFLELGFNHLPVIEG-GVVVGIVTPTNLL 107
Cdd:cd04632   95 VERMLENDISGLVVTPDdNMVIGILTKTDVL 125
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 61-168 1.34e-09

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 55.13  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  61 MTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAANGDVTVQDCLEGGCVPLHRL------- 132
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVdDDGKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLaeeyvka 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663515933 133 -------------------TPLGAALRIMRLSGARAMPVLgKRGLLCGIVTDRDL 168
Cdd:cd04586   81 hgrtvgdvmtrpvvtvspdTPLEEAARLMERHRIKRLPVV-DDGKLVGIVSRADL 134
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 16-107 3.21e-09

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: 53.31  E-value: 3.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREEtmELAGFVSRNDI----FNNTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPV 91
Cdd:cd04588   15 DAAKLLSENNIHGAPVVDDG--KLVGIVTLTDIakalAEGKENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIV 92

                         90
                 ....*....|....*..
gi 663515933  92 IEG-GVVVGIVTPTNLL 107
Cdd:cd04588   93 VDDnGKPVGIITRTDIL 109
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 20-102 9.41e-09

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


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 52.42  E-value: 9.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  20 LMIKHHISGVPVVREETmELAGFVSRNDIFNN------TGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELG-----FNH 88
Cdd:cd17784   19 KMLKHKISALPVVDDEG-KLIGIVTATDLGHNlildkyELGTTVEEVMVKDVATVHPDETLLEAIKKMDSNApdeeiINQ 97

                         90
                 ....*....|....
gi 663515933  89 LPVIEGGVVVGIVT 102
Cdd:cd17784   98 LPVVDDGKLVGIIS 111
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 133-270 1.03e-08

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 52.82  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFdatdvsERVSVSEMGVAADEDPWSWDGLRDIMRVYHSERrlfl 212
Cdd:cd04586   12 TSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLL------RREEPGTEPRRVWWLDALLESPERLAEEYVKAH---- 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663515933 213 pDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDaEGKLTGMIYCQDLLKV 270
Cdd:cd04586   82 -GRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLLRA 137
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 1-107 1.58e-08

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 51.84  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEvPGNR-TDVLHLMIKHHISGVPVVREETmeLAGFVSRNDI---------FNN--TG------EEQVAMIMT 62
Cdd:cd04631    6 MTKNVITAT-PGTPiEDVAKIMVRNGFRRLPVVSDGK--LVGIVTSTDImrylgsgeaFEKlkTGnihevlNVPISSIMK 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 663515933  63 SDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04631   83 RDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDIL 127
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 1-107 4.04e-08

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


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 50.48  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREETMelAGFVSRNDIFNNT-------GEEQVAMIMTSDVVSVTPNST 73
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERMLRNRVGSVVVTDDGTP--AGILTETDALHAGyatddpfSEIPVRAVASRPLVTISPTAT 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 663515933  74 VVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd17776   79 LREAAERMVDEGVKKLPVVDGLDLVGILTATDII 112
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 20-102 4.28e-08

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: 50.31  E-value: 4.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  20 LMIKHHISGVPVVREETmELAGFVSRNDIFNN--TGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEG-GV 96
Cdd:cd04605   25 IMIDKNVTHLPVVSEDG-KLIGIVTSWDISKAvaLKKDSLEEIMTRNVITARPDEPIELAARKMEKHNISALPVVDDdRR 103


                 ....*.
gi 663515933  97 VVGIVT 102
Cdd:cd04605  104 VIGIIT 109
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 57-107 4.81e-08

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: 4.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 663515933   57 VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVdEDGKLVGIVTLKDLL 52
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 65-168 8.95e-08

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


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 50.03  E-value: 8.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  65 VVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLplvaangdvtvqDCLEGGC------------------ 126
Cdd:cd17777   12 VLSISPSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARDLV------------SYLGGGClfkivesrhqgdlysaln 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663515933 127 ----VPLHRLTPLGA--------ALRIMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:cd17777   80 revvETIMTPNPVYVyedsdlieALTIMVTRGIGSLPVVDRDGRPVGIVTERDL 133
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 61-171 8.97e-08

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: 49.44  E-value: 8.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  61 MTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAANGD--VTVQDCLEGGCVPLHRLTPLGA 137
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVdDDGKPVGIVTERDIVRAVAEGIDldTPVEEIMTKNLVTVSPDESIYE 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 663515933 138 ALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:cd09836   81 AAELMREHNIRHLPVVDGGGKLVGVISIRDLARE 114
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 32-111 9.81e-08

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 49.79  E-value: 9.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  32 VREETMELAGFVSRNDIF----NNTGEEQ--VAMIMT--SDVVSVTPNSTVVSAARKFLELGFNHLPVIE----GGVVVG 99
Cdd:cd04617   32 VVDEEGYLVGVVSRKDLLkatlGGQDLEKtpVSMIMTrmPNIVTVTPDDSVLEAARKLIEHEIDSLPVVEkedgKLKVVG 111

                         90
                 ....*....|..
gi 663515933 100 IVTPTNLLPLVA 111
Cdd:cd04617  112 RITKTNITRLFV 123
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 16-102 1.46e-07

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: 49.54  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREETMELAGFVSRNDIFNNTG--------------------EEQVAMIMTSDVVSVTPNSTVV 75
Cdd:cd17779   21 GAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLGggskynlvekkhngnllaaiNEPVREIMTRDVISVKENASID 100

                         90       100
                 ....*....|....*....|....*...
gi 663515933  76 SAARKFLELGFNHLPVI-EGGVVVGIVT 102
Cdd:cd17779  101 DAIELMLEKNVGGLPIVdKDGKVIGIVT 128
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 16-102 1.51e-07

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: 52.01  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   16 DVLHLMIKHHISGVPVVreETMELAGFVSRNDI-FNNTGEEQVAMIMTSD-VVSVTPNSTVVSAARKFLELGFNHLPVI- 92
Cdd:pfam00478 101 DALALMERYGISGVPVV--DDGKLVGIVTNRDLrFETDLSQPVSEVMTKEnLVTAPEGTTLEEAKEILHKHKIEKLPVVd 178

                          90
                  ....*....|
gi 663515933   93 EGGVVVGIVT 102
Cdd:pfam00478 179 DNGRLVGLIT 188
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 50-168 3.75e-07

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: 50.85  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   50 NNTGEEQVAMI---------MTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPlvAANGDVTVQD 120
Cdd:pfam00478  66 NMSIEEQAEEVrkvkrsesgMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDLRF--ETDLSQPVSE 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 663515933  121 CL-EGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:pfam00478 144 VMtKENLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDI 192
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 22-102 4.34e-07

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


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 47.57  E-value: 4.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  22 IKHHISGV-----PVVREETmELAGFVSRNDI----FNNTGEEQVAM--IMTSDVVSVTPNSTVVSAARKFLELGFNHLP 90
Cdd:cd04613   17 FTEFIAGTrqhyfPVVDEQG-RLTGILSIQDVrgvlFEEELWDLVVVkdLATTDVITVTPDDDLYTALLKFTSTNLDQLP 95

                         90
                 ....*....|....*
gi 663515933  91 VIEG---GVVVGIVT 102
Cdd:cd04613   96 VVDDddpGKVLGMLS 110
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 60-168 5.67e-07

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: 47.61  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  60 IMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGV--VVGIVTPTNLLP-------------------LVAANGDVTv 118
Cdd:cd17779    5 IATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTkrLEGIVTSMDIVDflgggskynlvekkhngnlLAAINEPVR- 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 663515933 119 qDCLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:cd17779   84 -EIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDF 132
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
33-190 5.73e-07

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 50.07  E-value: 5.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  33 REETMELAGFvsrndifnntGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELG-----FNHLPVI-EGGVVVGIVTPTNL 106
Cdd:COG2239  117 REEIRELLSY----------PEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAedpetIYYIYVVdDDGRLVGVVSLRDL 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 107 LplvAANGDVTVQDCLEGGCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVT-DrdlfDATDVSERVSVSEM-- 183
Cdd:COG2239  187 L---LADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITvD----DVVDVIEEEATEDIlk 259


                 ....*....
gi 663515933 184 --GVAADED 190
Cdd:COG2239  260 laGVSEDED 268
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 133-269 6.43e-07

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 47.33  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDAtdVSERVSVSEMGVAADEdpwswdglrdimrvyhSERRLfl 212
Cdd:cd04632   11 DTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDF--VVRPGTKTRGGDRGGE----------------KERML-- 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663515933 213 pDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:cd04632   71 -DLPVYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 54-107 6.83e-07

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


Pssm-ID: 341386 [Multi-domain]  Cd Length: 150  Bit Score: 47.66  E-value: 6.83e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663515933  54 EEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEG-GVVVGIVTPTNLL 107
Cdd:cd04614   94 DKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGeGDLAGMLRDVDLL 148
CBS_pair_voltage-gated_CLC_euk_bac cd04591
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 1-107 7.80e-07

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


Pssm-ID: 341367 [Multi-domain]  Cd Length: 114  Bit Score: 46.74  E-value: 7.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICaeVPGNRT--DVLHLMIKHHISGVPVVRE-ETMELAGFVSRNDIfnntgeeQVA------MIMTSDVVSVTPN 71
Cdd:cd04591    6 MRPPLTV--LARDETvgDIVSVLKTTDHNGFPVVDStESQTLVGFILRSQL-------ILLleadlrPIMDPSPFTVTEE 76

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 663515933  72 STVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd04591   77 TSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLL 112
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 133-271 9.29e-07

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: 46.75  E-value: 9.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDAtdvservsvsemgVAADEDPwswdglrdimrvyhserrlfl 212
Cdd:cd09836   12 TTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRA-------------VAEGIDL--------------------- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663515933 213 pDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVL 271
Cdd:cd09836   58 -DTPVEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 1-110 1.00e-06

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: 46.77  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVpVVREETMELAGFVSRNDIF-------NNTGEEQVAMIMTSDVVSVTPNST 73
Cdd:cd17775    1 CRREVVTASPDTSVLEAARLMRDHHVGSV-VVVEEDGKPVGIVTDRDIVvevvakgLDPKDVTVGDIMSADLITAREDDG 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 663515933  74 VVSAARKFLELGFNHLPVIEG-GVVVGIVTPTNLLPLV 110
Cdd:cd17775   80 LFEALERMREKGVRRLPVVDDdGELVGIVTLDDILELL 117
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 64-107 1.44e-06

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: 44.43  E-value: 1.44e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 663515933    64 DVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLVGIVTRRDII 45
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 1-102 1.52e-06

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 45.87  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREEtmELAGFVSRNDIF-------NNTGEEQVAMIMTSDVVSVTPNST 73
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGD--RLVGMVTDRDIVvravaegKDPNTTTVREVMTGDVVTCSPDDD 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 663515933  74 VVSAARKFLELGFNHLPVIEG-GVVVGIVT 102
Cdd:cd04622   79 VEEAARLMAEHQVRRLPVVDDdGRLVGIVS 108
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 217-272 1.53e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.51  E-value: 1.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933  217 VEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVLL 272
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 1-107 1.78e-06

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


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 46.38  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAevPGNRT--DVLHLMIKHHISGVPVVREETMELA------GFVSRNDI---------FNNTgeeQVAMIMTS 63
Cdd:cd17774    3 MTTRVIHA--PPTASvlELAQLMAEHRVSCVVIVEEDEQQEKnklipvGIVTERDIvqfqalgldLSQT---QAQTVMSS 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 663515933  64 DVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:cd17774   78 PLFSLRPDDSLWTAHQLMQQRRIRRLVVVgEQGELLGIVTQTSLL 122
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 1-110 2.55e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 45.20  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVicaEVPGNRT--DVLHLMIKHHISGVPVVREETMeLAGFVSRNDI-FNNTGEEQVAMIMTSDVVSVTPNSTVVSA 77
Cdd:cd04583    1 ITNPV---TITPERTlaQAIEIMREKRVDSLLVVDKDNV-LLGIVDIEDInRNYRKAKKVGEIMERDVFTVKEDSLLRDT 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 663515933  78 ARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLV 110
Cdd:cd04583   77 VDRILKRGLKYVPVVdEQGRLVGLVTRASLVDIV 110
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 133-270 2.61e-06

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 45.18  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLgKRGLLCGIVTdrdlfdatdvservsvsemgvaadedpwswdgLRDIMRVYHSErrlfL 212
Cdd:cd04595   11 TTIEEARKIMLRYGHTGLPVV-EDGKLVGIIS--------------------------------RRDVDKAKHHG----L 53

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 663515933 213 PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDaEGKLTGMIYCQDLLKV 270
Cdd:cd04595   54 GHAPVKGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVE-EGKLVGIVTRSDVLRY 110
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 57-168 3.53e-06

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: 45.22  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  57 VAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAANG---DVTVQDCLEGGCVPLHRL 132
Cdd:cd04608    4 VRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVdEDGRVVGMVTEGNLLSSLLAGRaqpSDPVSKAMYKQFKQVDLD 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 663515933 133 TPLGAALRIMRlSGARAMPVLGKRGLLcGIVTDRDL 168
Cdd:cd04608   84 TPLGALSRILE-RDHFALVVDGQGKVL-GIVTRIDL 117
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 133-262 3.82e-06

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: 44.72  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVlGKRGLLCGIVTDRDLfdatdvservSVSemGVAADEDPwswdglrdimrvyhserrlfl 212
Cdd:cd04622   12 TTLREAARLMRDLDIGALPV-CEGDRLVGMVTDRDI----------VVR--AVAEGKDP--------------------- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663515933 213 PDVPVEEIMIEDVMTAFYRSPASGVAQIMldGDYgQV---PLVDAEGKLTGMI 262
Cdd:cd04622   58 NTTTVREVMTGDVVTCSPDDDVEEAARLM--AEH-QVrrlPVVDDDGRLVGIV 107
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 16-102 5.38e-06

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 44.33  E-value: 5.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVrEETMELAGFVSRNDIFNNTGEEQ-VAMIMTSDVVSVT-PNSTVVSAARKFLElgfNH----L 89
Cdd:cd04601   15 DVLELKAEYGISGVPVT-EDGGKLVGIVTSRDIRFETDLSTpVSEVMTPDERLVTaPEGITLEEAKEILH---KHkiekL 90

                         90
                 ....*....|....
gi 663515933  90 PVI-EGGVVVGIVT 102
Cdd:cd04601   91 PIVdDNGELVGLIT 104
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 23-102 6.21e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 44.25  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  23 KHHISGVPVVREEtMELAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIV 101
Cdd:cd04606   34 PETIYYIYVVDED-RRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVdEEGRLVGII 112


                 .
gi 663515933 102 T 102
Cdd:cd04606  113 T 113
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 60-171 7.30e-06

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: 44.10  E-value: 7.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  60 IMTSDVVSVTPNSTVvsaaRKFLELGFN--HL--PVIEGGVVVGIVTPTNLLPLVAANGDVT-VQDCLEGGCVPLHRLTP 134
Cdd:cd04801    2 IMTPEVVTVTPEMTV----SELLDRMFEekHLgyPVVENGRLVGIVTLEDIRKVPEVEREATrVRDVMTKDVITVSPDAD 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 663515933 135 LGAALRIMRLSGARAMPVLgKRGLLCGIVTDRDLFDA 171
Cdd:cd04801   78 AMEALKLMSQNNIGRLPVV-EDGELVGIISRTDLMRA 113
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 133-271 9.66e-06

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: 44.14  E-value: 9.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLG---KRglLCGIVTDRDLFDATDVSERvsvsemgvaadedpwswdglRDIMRVYHSERR 209
Cdd:cd17779   17 TTIIGAIKTMTEKGFRRLPVADagtKR--LEGIVTSMDIVDFLGGGSK--------------------YNLVEKKHNGNL 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663515933 210 LFLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVL 271
Cdd:cd17779   75 LAAINEPVREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-50 9.67e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 44.09  E-value: 9.67e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREEtMELAGFVSRNDIFN 50
Cdd:COG3448   79 MTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLLR 127
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 127-270 1.02e-05

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 43.58  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 127 VPLHRLTPLGAALRIM---RLSGAramPVLGKRGLLCGIVtdrdlfdatdvSERvsvsemgvaadedpwswDGLRDIMR- 202
Cdd:cd04629    6 VTLTPDTSILEAVELLlehKISGA---PVVDEQGRLVGFL-----------SEQ-----------------DCLKALLEa 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663515933 203 VYHSErrlflPDVPVEEIMIEDVMTAfyrSPASG---VAQIMLDGDYGQVPLVDaEGKLTGMIYCQDLLKV 270
Cdd:cd04629   55 SYHCE-----PGGTVADYMSTEVLTV---SPDTSivdLAQLFLKNKPRRYPVVE-DGKLVGQISRRDVLRA 116
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 133-269 1.04e-05

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: 46.23  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  133 TPLGAALRIMRLSGARAMPVLGKrGLLCGIVTDRDLFDATDvservsvsemgvaadedpwswdglrdimrvyhserrlfl 212
Cdd:pfam00478  97 ATVADALALMERYGISGVPVVDD-GKLVGIVTNRDLRFETD--------------------------------------- 136

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 663515933  213 PDVPVEEIM-IEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:pfam00478 137 LSQPVSEVMtKENLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIEK 194
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 16-107 1.16e-05

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: 43.87  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREETME-----------LAGFV--------SRNDIFNNTGEEQVAMIMTSDVVSVTPNSTVVS 76
Cdd:cd17777   23 SAFEKMNRRGIRRLVVVDENKLEgilsardlvsyLGGGClfkivesrHQGDLYSALNREVVETIMTPNPVYVYEDSDLIE 102

                         90       100       110
                 ....*....|....*....|....*....|..
gi 663515933  77 AARKFLELGFNHLPVI-EGGVVVGIVTPTNLL 107
Cdd:cd17777  103 ALTIMVTRGIGSLPVVdRDGRPVGIVTERDLV 134
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 60-164 1.22e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 43.48  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  60 IMTSDVVSVTPNSTVVSAARKFLELG-----FNHLPVI-EGGVVVGIVTPTNLLplvAANGDVTVQDCLEGGCVPLHRLT 133
Cdd:cd04606    6 LMTTEFVAVRPDWTVEEALEYLRRLApdpetIYYIYVVdEDRRLLGVVSLRDLL---LADPDTKVSDIMDTDVISVSADD 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 663515933 134 PLGAALRIMRLSGARAMPVLGKRGLLCGIVT 164
Cdd:cd04606   83 DQEEVARLFAKYDLLALPVVDEEGRLVGIIT 113
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 57-169 1.30e-05

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: 43.64  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  57 VAMIMT--SDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGV--VVGIVTPTNLLPLVAANGDVT-----VQDCLEggcV 127
Cdd:cd04590    2 VREVMTprTDVVALDADATLEELLELILESGYSRFPVYEGDLdnIIGVLHVKDLLAALLEGREKLdlralLRPPLF---V 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 663515933 128 PLHrlTPLGAALRIMRLSGAR-AMpVLGKRGLLCGIVTDRDLF 169
Cdd:cd04590   79 PET--TPLDDLLEEFRKERSHmAI-VVDEYGGTAGIVTLEDIL 118
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 62-170 1.32e-05

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: 43.29  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  62 TSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPLVAA-NGDVTVQDCLEGGCVPLHRLTPLGAALR 140
Cdd:cd04588    1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLTDIAKALAEgKENAKVKDIMTKDVITIDKDEKIYDAIR 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 663515933 141 IMRLSGARAMPVLGKRGLLCGIVTDRDLFD 170
Cdd:cd04588   81 LMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 47-168 1.42e-05

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 45.88  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  47 DIFNNT---GEEQVAMIMT--SDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGV--VVGIVTPTNLLPLVAANGDVTVQ 119
Cdd:COG1253  203 EMIENVfefGDRTVREVMTprTDVVALDLDDTLEEALELILESGHSRIPVYEGDLddIVGVVHVKDLLRALLEGEPFDLR 282

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663515933 120 DCLEggcvPLHRL---TPLGAALRIMRLSGAR-AMpVLGKRGLLCGIVTDRDL 168
Cdd:COG1253  283 DLLR----PPLFVpetKPLDDLLEEFRRERVHmAI-VVDEYGGTAGLVTLEDI 330
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 133-271 1.73e-05

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: 42.91  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLfdATDVservsvsemgVAADEDPwswdglrdimrvyhserrlfl 212
Cdd:cd17775   12 TSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDI--VVEV----------VAKGLDP--------------------- 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663515933 213 PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVL 271
Cdd:cd17775   59 KDVTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 133-269 2.07e-05

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: 42.79  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDATDVSERVSvsemgvaadedpwswdglrDIMrvyhserrlfL 212
Cdd:cd04601   11 ATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFETDLSTPVS-------------------EVM----------T 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663515933 213 PD----VPVEEIMIEDVMtafyrspasgvaQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:cd04601   62 PDerlvTAPEGITLEEAK------------EILHKHKIEKLPIVDDNGELVGLITRKDIEK 110
CBS COG0517
CBS domain [Signal transduction mechanisms];
1-56 2.33e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 42.93  E-value: 2.33e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVrEETMELAGFVSRNDIFNNTGEEQ 56
Cdd:COG0517   73 MTRPPVTVSPDTSLEEAAELMEEHKIRRLPVV-DDDGRLVGIITIKDLLKALLEPL 127
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 16-107 2.39e-05

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


Pssm-ID: 341393 [Multi-domain]  Cd Length: 120  Bit Score: 42.58  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREETMELAGFVSRNDIFN-------NTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNH 88
Cdd:cd04630   20 EALQLMKEHNVKSLIVEKRHEHDAYGIVTYTDILKkviaedrDPDLVNVYEIMTKPAISVSPDLDIKYAARLMARFNLKR 99

                         90
                 ....*....|....*....
gi 663515933  89 LPVIEGGVVVGIVTPTNLL 107
Cdd:cd04630  100 APVIENNELIGIVSMTDLV 118
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 208-271 3.16e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 42.32  E-value: 3.16e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933 208 RRLFL--PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVL 271
Cdd:cd04606   56 RDLLLadPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 133-268 3.25e-05

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


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 42.03  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKrGLLCGIVTDRDLfdatdvSERVsvsemgVAADEDpwswdglrdimrvyhserrlfl 212
Cdd:cd04587   13 ATIQEAAQLMSEERVSSLLVVDD-GRLVGIVTDRDL------RNRV------VAEGLD---------------------- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933 213 PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDaEGKLTGMIYCQDLL 268
Cdd:cd04587   58 PDTPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVD-DGRVVGVVTATDLM 112
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
208-271 4.09e-05

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 44.29  E-value: 4.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933 208 RRLFL--PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVL 271
Cdd:COG2239  184 RDLLLadPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVDVI 249
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
1-102 4.64e-05

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 44.29  E-value: 4.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVIcaEVPGNRT--DVLHLMIKH-----HISGVPVVrEETMELAGFVSRNDIFNNTGEEQVAMIMTSDVVSVTPNST 73
Cdd:COG2239  135 MTTEFV--AVREDWTvgEALRYLRRQaedpeTIYYIYVV-DDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDD 211

                         90       100       110
                 ....*....|....*....|....*....|
gi 663515933  74 VVSAARKFLELGFNHLPVI-EGGVVVGIVT 102
Cdd:COG2239  212 QEEVARLFERYDLLALPVVdEEGRLVGIIT 241
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 133-171 5.20e-05

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: 40.27  E-value: 5.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 663515933  133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:pfam00571  16 TTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 62-171 5.85e-05

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: 41.93  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  62 TSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAANGDVT----------------VQDCLEG 124
Cdd:cd04632    1 TEEVITVNEDDTIGKAINLLREHGISRLPVVdDNGKLVGIVTTYDIVDFVVRPGTKTrggdrggekermldlpVYDIMSS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 663515933 125 GCVPLHRLTPLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDA 171
Cdd:cd04632   81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 138-262 6.68e-05

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


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 41.42  E-value: 6.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 138 ALRIMRLSGARAMPVLGKRGLLCGIVTDrdlfdaTDVSERVsvsemgVAADEDPWSwdglrdimrvyhserrlflpdVPV 217
Cdd:cd17781   16 AAQLMAAKRTDAVLVVDDDGGLSGIFTD------KDLARRV------VASGLDPRS---------------------TLV 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 663515933 218 EEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMI 262
Cdd:cd17781   63 SSVMTPNPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVL 107
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 16-102 1.42e-04

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


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 40.69  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVpVVREETMELAGFVSRNDIFN-------NTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNH 88
Cdd:cd17782   15 EAARLMKENRTTAV-LVMDNSGKVIGIFTSKDVVLrvlaaglDPATTSVVRVMTPNPETAPPSTTILDALHKMHEGKFLN 93

                         90
                 ....*....|....*
gi 663515933  89 LPVI-EGGVVVGIVT 102
Cdd:cd17782   94 LPVVdDEGEIVGLVD 108
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 1-56 1.50e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 40.58  E-value: 1.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREEtmELAGFVSRNDIFNNTGEEQ 56
Cdd:COG2905   71 MTRPPITVSPDDSLAEALELMEEHRIRHLPVVDDG--KLVGIVSITDLLRALSEEL 124
PRK01862 PRK01862
voltage-gated chloride channel ClcB;
59-171 1.59e-04

voltage-gated chloride channel ClcB;


Pssm-ID: 234987 [Multi-domain]  Cd Length: 574  Bit Score: 42.81  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  59 MIMTSDVVsVTPNSTVVSAARKFLELGFNHLPVIEG-GVVVGIVTPTNLLPLVAANGDVTVQDCLEGGCVPLHRLTP--- 134
Cdd:PRK01862 452 LIQPAQTV-VPPTASVADMTRVFLEYPVKYLYVVDDdGRFRGAVALKDITSDLLDKRDTTDKTAADYAHTPFPLLTPdmp 530

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663515933 135 LGAALRIMRLSGARAMPVL--GKRGLLCGIVTDRDLFDA 171
Cdd:PRK01862 531 LGDALEHFMAFQGERLPVVesEASPTLAGVVYKTSLLDA 569
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 20-100 1.62e-04

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


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 40.26  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  20 LMIKHHISGVpVVREETMELAGFVSRNDIFN-------NTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI 92
Cdd:cd17781   19 LMAAKRTDAV-LVVDDDGGLSGIFTDKDLARrvvasglDPRSTLVSSVMTPNPLCVTMDTSATDALDLMVEGKFRHLPVV 97


                 ....*....
gi 663515933  93 E-GGVVVGI 100
Cdd:cd17781   98 DdDGDVVGV 106
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
1-50 2.18e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 40.28  E-value: 2.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREETmELAGFVSRNDIFN 50
Cdd:COG4109   82 MTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDG-RLLGIISRQDVLK 130
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 62-171 2.43e-04

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


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 40.10  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  62 TSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNL---LPLVAANGDVTVQDCLEGGCVPLHRLTPLGA 137
Cdd:cd17784    1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVdDEGKLIGIVTATDLghnLILDKYELGTTVEEVMVKDVATVHPDETLLE 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 663515933 138 ALRIMRLSGARA-----MPVLGKrGLLCGIVTDRDLFDA 171
Cdd:cd17784   81 AIKKMDSNAPDEeiinqLPVVDD-GKLVGIISDGDIIRA 118
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 1-49 3.16e-04

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: 37.96  E-value: 3.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 663515933    1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVREEtMELAGFVSRNDIF 49
Cdd:pfam00571   5 MTKDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLL 52
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 197-262 3.35e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 39.42  E-value: 3.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933 197 LRDIMRVYHSERRlflpdvpVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMI 262
Cdd:cd04583   43 IEDINRNYRKAKK-------VGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLV 101
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 217-271 3.51e-04

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 39.52  E-value: 3.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663515933 217 VEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVdAEGKLTGMIYCQDLLKVL 271
Cdd:cd04631    2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIMRYL 55
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
56-272 3.59e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.74  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  56 QVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLL--------PLVAANGDVTVQ---DCLE 123
Cdd:PRK14869  69 QVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVdEEGKLLGLVSLSDLAraymdildPEILSKSPTSLEniiRTLD 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 124 GGCV---PLHRLTPLGAALRIMRLSGARA------MPVLGKR----------GLLCGIVTdrdlfDATDVSERV--SVSE 182
Cdd:PRK14869 149 GEVLvgaEEDKVEEGKVVVAAMAPESLLErieegdIVIVGDRediqlaaieaGVRLLIIT-----GGAPVSEDVleLAKE 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 183 MGVAadedpwswdglrdIMRVYH---SERRLFLPDVPVEEIMIEDVMTAFYRS-PASGVAQIMLDGDYGQVPLVDAEGKL 258
Cdd:PRK14869 224 NGVT-------------VISTPYdtfTTARLINQSIPVSYIMTTEDLVTFSKDdYLEDVKEVMLKSRYRSYPVVDEDGKV 290

                        250
                 ....*....|....*....
gi 663515933 259 TGMIYCQDLL-----KVLL 272
Cdd:PRK14869 291 VGVISRYHLLspvrkKVIL 309
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 60-102 3.88e-04

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


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 39.33  E-value: 3.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 663515933  60 IMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVT 102
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVT 43
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 213-269 5.64e-04

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


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 38.60  E-value: 5.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 663515933 213 PDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:cd04596   51 DDTPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDENRKLLGVISRQDVLK 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 237-272 5.73e-04

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: 37.11  E-value: 5.73e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 663515933   237 VAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVLL 272
Cdd:smart00116  14 ALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 1-107 7.32e-04

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


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 38.08  E-value: 7.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKH-HISGVPVVreetmELAGfVSRNDIfnntgeeqvAMIMTSDVvsvTPNSTVVSAAR 79
Cdd:COG3620    5 MSRDVVTVSPDDTLGEALRLMRKElGLSQLPVA-----ELVG-VSQSDI---------LRIESGKR---DPTVSTLEKIA 66

                         90       100
                 ....*....|....*....|....*...
gi 663515933  80 KFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:COG3620   67 EALGKELSAVLVVDDGKLVGIITRRDLL 94
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-50 9.63e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 39.48  E-value: 9.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 663515933   1 MTSPVICAEVPGNRTDVLHLMIKHHISGVPVVrEETMELAGFVSRNDIFN 50
Cdd:COG2524  156 MTRDVVTVSEDDSLEEALRLMLEHGIGRLPVV-DDDGKLVGIITRTDILR 204
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 133-262 9.84e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 38.61  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIM---RLSGaraMPVLGKRGLLCGIVTDRDLFDATDVSERVSVSEMGVAADEdpwSWDGLRDIMR-VYHSER 208
Cdd:cd17789   12 TTVDEALELLvenRITG---LPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADS---TWKTFNEVQKlLSKTNG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663515933 209 RLflpdvpVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMI 262
Cdd:cd17789   86 KV------VGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGII 133
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 217-269 1.09e-03

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: 37.99  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 663515933 217 VEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:cd04605    2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISK 54
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 63-123 1.26e-03

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: 37.88  E-value: 1.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663515933  63 SDVVSVTPNSTVVSAARKFLELGFNHLPVI-EGGVVVGIVTPTNLLPLVAA----NGDVTVQDCLE 123
Cdd:cd04641    3 ENIATASMDTPVIDALNLFVERRVSALPIVdEDGRVVDIYAKFDVINLAAEktynNLDLTVGEALQ 68
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 61-171 2.17e-03

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


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 37.00  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  61 MTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPLVAANGD----VTVQDCLEGGCVPLHRLTPLG 136
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALHAGYATDDpfseIPVRAVASRPLVTISPTATLR 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 663515933 137 AALRIMRLSGARAMPVLgkRGL-LCGIVTDRDLFDA 171
Cdd:cd17776   81 EAAERMVDEGVKKLPVV--DGLdLVGILTATDIIRA 114
CBS_pair_arch1_repeat1 cd17780
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 31-107 2.63e-03

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


Pssm-ID: 341416 [Multi-domain]  Cd Length: 106  Bit Score: 36.56  E-value: 2.63e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663515933  31 VVREETMELAGFVSRNDIF-NNTGEEQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLL 107
Cdd:cd17780   28 VVVTDDGEYEGVVTERQLLqSHVEDDAKVGALVRAAPKVDRTEDVREVARLLVEGGTKVAPVFEGGSLWGVVTADAIL 105
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 18-107 2.69e-03

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


Pssm-ID: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 36.55  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  18 LHLMIKHHISGVPVVREETmELAGFVSRNDIFNNTGEeQVAMIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVV 97
Cdd:cd04594   17 LKIMRENNLLSLPVVDNDS-NFLGAVYLRDIENKSPG-KVGKYVVRGSPYVTPTSSLEEAWEIMMRNKSRWVAVVEKGKF 94

                         90
                 ....*....|
gi 663515933  98 VGIVTPTNLL 107
Cdd:cd04594   95 LGIITLDDLL 104
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 50-173 3.78e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 38.41  E-value: 3.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  50 NNTGEEQVAMI---------MTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVV----VGIVTPTNLLPLVAANGDV 116
Cdd:PTZ00314  82 NCSIEEQVEEVrkvkrfengFIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVggklLGIVTSRDIDFVKDKSTPV 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663515933 117 ----TVQDCLEGGCVPLHrltpLGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDATD 173
Cdd:PTZ00314 162 sevmTPREKLVVGNTPIS----LEEANEVLRESRKGKLPIVNDNGELVALVSRSDLKKNRG 218
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
135-272 4.47e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 37.56  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 135 LGAALRIMRLSGARAMPVLGKRGLLCGIVTDRDLFDATDVSERVSVSEMGVAADEDPWSWDGL----RDIMRVYHSERRL 210
Cdd:COG2524    2 LVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLivlqAAAVRVVAEKELG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663515933 211 FLPDVPVEEIMIEDVMTAFYRSPASGVAQIMLDGDYGQVPLVDaEGKLTGMIYCQDLLKVLL 272
Cdd:COG2524   82 LVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALA 142
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 16-107 5.62e-03

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 35.79  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  16 DVLHLMIKHHISGVPVVREETmELAGFVSRNDIFNNtgeeqVAMIMTSDVVSVTPNSTVVSAARK-FLELGFNHLPVI-E 93
Cdd:cd04597   18 DAWNLMDENNLKTLPVTDDNG-KLIGLLSISDIART-----VDYIMTKDNLIVFKEDDYLDEVKEiMLNTNFRNYPVVdE 91

                         90
                 ....*....|....
gi 663515933  94 GGVVVGIVTPTNLL 107
Cdd:cd04597   92 NNKFLGTISRKHLI 105
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 133-269 5.67e-03

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


Pssm-ID: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 35.82  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIM---RLsGARAmpVLGKRGLLCGIVTDRDLfdatdvservsvsemgvaadedpwswdglrdimrvyhseRR 209
Cdd:cd04604   22 TSLKEALLEMtrkGL-GCTA--VVDEDGRLVGIITDGDL---------------------------------------RR 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663515933 210 LFLPDVPVEEIMIEDVMTafyRSP--------ASGVAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLK 269
Cdd:cd04604   60 ALEKGLDILNLPAKDVMT---RNPktispdalAAEALELMEEHKITVLPVVDEDGKPVGILHLHDLLR 124
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 151-268 6.30e-03

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: 35.63  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 151 PVLGKRGLLCGIVTDRDLfdatdvservsvseMGVAADEdpwswdGLRDImrvyhserrlflpdVPVEEIMIEDVMTAFY 230
Cdd:cd04613   30 PVVDEQGRLTGILSIQDV--------------RGVLFEE------ELWDL--------------VVVKDLATTDVITVTP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 663515933 231 RSPASGVAQIMLDGDYGQVPLVDAE--GKLTGMIYCQDLL 268
Cdd:cd04613   76 DDDLYTALLKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVI 115
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 133-269 8.78e-03

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: 35.08  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 133 TPLGAALRIMRLSGARAMPVLGKRGLLCGIvtdrdlfdatdVSErvsvsemgvaadedpwswdglRDIMRVYHSERRLFL 212
Cdd:cd04623   11 ATVAEALRLLAEKNIGALVVVDDGGRLVGI-----------LSE---------------------RDYVRKLALRGASSL 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933 213 pDVPVEEIMIEDVMTAfyrSPASGVA---QIMLDGDYGQVPLVDaEGKLTGMIYCQDLLK 269
Cdd:cd04623   59 -DTPVSEIMTRDVVTC---TPDDTVEecmALMTERRIRHLPVVE-DGKLVGIVSIGDVVK 113
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 237-272 9.74e-03

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: 35.30  E-value: 9.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 663515933 237 VAQIMLDGDYGQVPLVDAEGKLTGMIYCQDLLKVLL 272
Cdd:cd02205   16 ALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 59-168 9.98e-03

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: 35.28  E-value: 9.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515933  59 MIMTSDVVSVTPNSTVVSAARKFLELGFNHLPVIEGGVVVGIVTPTNLLPLVAANGDVTVQDCLEGGCVP---LHRLTPL 135
Cdd:cd09833    1 RIVSTSLLTCSPDTPLADAAARMAERRCSSILIVENGEIVGIWTERDALKLDFSDPDAFRRPISEVMSSPvltIPQDTTL 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 663515933 136 G-AALRiMRLSGARAMPVLGKRGLLCGIVTDRDL 168
Cdd:cd09833   81 GeAAVR-FRQEGVRHLLVVDDDGRPVGIVSQTDV 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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