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Conserved domains on  [gi|751557642|ref|NP_001291456|]
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5'-AMP-activated protein kinase subunit gamma-2 isoform d [Homo sapiens]

Protein Classification

5'-AMP-activated protein kinase subunit gamma( domain architecture ID 10140186)

5'-AMP-activated protein kinase subunit gamma is the AMP/ATP-binding subunit of AMP-activated protein kinase, an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism; contains CBS (cystathione beta synthase) domains

CATH:  3.10.580.10
Gene Ontology:  GO:0005515|GO:0000166|GO:0019901|GO:0043539|GO:0019887

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 144-281 5.79e-87

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


:

Pssm-ID: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 261.34  E-value: 5.79e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 144 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 223
Cdd:cd04618    1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 751557642 224 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILK 281
Cdd:cd04618   81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 307-430 4.35e-75

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: 230.48  E-value: 4.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 307 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 386
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 387 NKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 144-281 5.79e-87

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


Pssm-ID: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 261.34  E-value: 5.79e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 144 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 223
Cdd:cd04618    1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 751557642 224 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILK 281
Cdd:cd04618   81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 307-430 4.35e-75

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: 230.48  E-value: 4.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 307 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 386
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 387 NKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS COG0517
CBS domain [Signal transduction mechanisms];
310-430 1.82e-20

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 86.84  E-value: 1.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHrsqyfeGVVKCNKL 389
Cdd:COG0517   10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751557642 390 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:COG0517   84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
234-359 6.82e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 82.61  E-value: 6.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILTHKRILKFLQLFMSDMPKPAFMKQNLDELgigTYHNIA 312
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVD--EDGRLVgIVTERDLLRALLPDRLDELEERLLDLPVEDV---MTRPVV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 751557642 313 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 359
Cdd:COG3448   85 TVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 314-358 1.54e-10

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 55.98  E-value: 1.54e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 751557642   314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAA 358
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 309-359 2.01e-09

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: 53.37  E-value: 2.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 751557642  309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 359
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 235-284 1.56e-07

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: 47.51  E-value: 1.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 751557642   235 PLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQ 284
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDE-EGRLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 234-283 8.09e-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: 42.97  E-value: 8.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 751557642  234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 283
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRAL 55
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
310-425 1.98e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 40.59  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDvinLAaeKTYnnLDITVTQALQHRSQYFEGVVKCNKL 389
Cdd:PRK14869  77 KPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSD---LA--RAY--MDILDPEILSKSPTSLENIIRTLDG 149

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557642 390 EILeTIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 425
Cdd:PRK14869 150 EVL-VGAEEDKVEEGKVVVAAMAPESLLERIEEGDI 184
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 144-281 5.79e-87

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


Pssm-ID: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 261.34  E-value: 5.79e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 144 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 223
Cdd:cd04618    1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 751557642 224 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILK 281
Cdd:cd04618   81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 307-430 4.35e-75

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: 230.48  E-value: 4.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 307 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 386
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 387 NKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS COG0517
CBS domain [Signal transduction mechanisms];
310-430 1.82e-20

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 86.84  E-value: 1.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHrsqyfeGVVKCNKL 389
Cdd:COG0517   10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751557642 390 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:COG0517   84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 309-427 2.15e-20

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: 86.14  E-value: 2.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQALQhrsqyfEGVVKCNK 388
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG-GLALDTPVAEVMT------PDVITVSP 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 751557642 389 LEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQ 427
Cdd:cd02205   75 DTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
309-430 1.11e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 84.92  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNL-----DITVTQALQHRsqyfegV 383
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELeerllDLPVEDVMTRP------V 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 751557642 384 VKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:COG3448   84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
234-359 6.82e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 82.61  E-value: 6.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILTHKRILKFLQLFMSDMPKPAFMKQNLDELgigTYHNIA 312
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVD--EDGRLVgIVTERDLLRALLPDRLDELEERLLDLPVEDV---MTRPVV 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 751557642 313 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 359
Cdd:COG3448   85 TVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
309-429 6.34e-17

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 79.16  E-value: 6.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEKTYNnLDITVTQALQhrsqyfEGVVKCNK 388
Cdd:COG2524   94 KDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDL-LDAPVSDIMT------RDVVTVSE 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751557642 389 LEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 429
Cdd:COG2524  166 DDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 309-430 6.43e-16

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 73.71  E-value: 6.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRsqyfegVVKCNK 388
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRP------PITVSP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 751557642 389 LEILETIVDRIVRAEVHRLVVVnEADSIVGIISLSDILQALI 430
Cdd:COG2905   81 DDSLAEALELMEEHRIRHLPVV-DDGKLVGIVSITDLLRALS 121
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
234-355 1.21e-15

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 75.31  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPA--FMKQNLdelgigtyhni 311
Cdd:COG2524   94 KDVITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDLLDAPVsdIMTRDV----------- 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 312 AFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 355
Cdd:COG2524  161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 234-357 1.61e-15

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: 72.84  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpisGNALY-ILTHKRILKFLqlfMSDMPKPAFMKQNLDELGIgTYHNI- 311
Cdd:cd04584    8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVD---DGKLVgIVTDRDLLRAS---PSKATSLSIYELNYLLSKI-PVKDIm 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 751557642 312 ----AFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLA 357
Cdd:cd04584   81 tkdvITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 314-428 1.74e-15

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: 72.85  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCNKL---E 390
Cdd:cd04586    8 VTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLAEEYVKAHGRtvgD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 751557642 391 I-------------LETIVDRIVRAEVHRLVVVNEaDSIVGIISLSDILQA 428
Cdd:cd04586   88 VmtrpvvtvspdtpLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLLRA 137
CBS COG0517
CBS domain [Signal transduction mechanisms];
234-359 6.23e-15

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 71.05  E-value: 6.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILTHKRILKFLqlfmsdmpkpAFMKQNLDELGIGTY--HN 310
Cdd:COG0517    9 TDVVTVSPDATVREALELMSEKRIGGLPVVD--EDGKLVgIVTDRDLRRAL----------AAEGKDLLDTPVSEVmtRP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 751557642 311 IAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 359
Cdd:COG0517   77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 309-428 2.78e-14

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 69.00  E-value: 2.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLD-ITVtqalqhrSQYFEGVVKCN 387
Cdd:cd04629    3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPgGTV-------ADYMSTEVLTV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 388 KLEilETIVD---RIVRAEVHRLVVVnEADSIVGIISLSDILQA 428
Cdd:cd04629   76 SPD--TSIVDlaqLFLKNKPRRYPVV-EDGKLVGQISRRDVLRA 116
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 152-281 2.04e-13

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 66.50  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 152 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETwrelylqe 231
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK-LVGIVTERDILRALVEGGLALDTPVAEVMTPDVIT-------- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 751557642 232 tfkplvnISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILK 281
Cdd:cd02205   72 -------VSPDTDLEEALELMLEHGIRRLPVVDD-DGKLVGIVTRRDILR 113
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 314-428 6.39e-12

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: 62.35  E-value: 6.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNN------------LDITVtqalqhRSQYFE 381
Cdd:cd04632    7 VNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTrggdrggekermLDLPV------YDIMSS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 751557642 382 GVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQA 428
Cdd:cd04632   81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 234-356 1.62e-11

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: 61.01  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPAFMKQNldelgigtyhnIAF 313
Cdd:cd04588    2 KDLITLKPDATIKDAAKLLSENNIHGAPVVD--DGKLVGIVTLTDIAKALAEGKENAKVKDIMTKD-----------VIT 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINL 356
Cdd:cd04588   69 IDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 310-429 3.48e-11

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: 60.23  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTynNLDITVTQALqhrsqyFEGVVKCNKL 389
Cdd:cd09836    4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGI--DLDTPVEEIM------TKNLVTVSPD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 751557642 390 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 429
Cdd:cd09836   76 ESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
307-429 3.63e-11

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 60.70  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 307 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLditVTQALQhrsqyfegVVKC 386
Cdd:COG4109   23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTPIEDV---MTKNPI--------TVTP 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 751557642 387 NklEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 429
Cdd:COG4109   92 D--TSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 314-429 1.17e-10

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: 59.11  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQyFEGVVKcnklEILE 393
Cdd:cd04600    8 VTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRD-RPETVG----DIMT 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 751557642 394 TIVdRIVRAEVH--RLV------------VVNEADSIVGIISLSDILQAL 429
Cdd:cd04600   83 RPV-VTVRPDTPiaELVplfsdgglhhipVVDADGRLVGIVTQSDLIAAL 131
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 314-358 1.54e-10

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 55.98  E-value: 1.54e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 751557642   314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAA 358
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 234-359 1.72e-10

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 58.30  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLfmsdmpkpafMKQNLDELGIGTY--HNI 311
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDD-DGRLVGIITDRDLRRRVLA----------EGLDPLDTPVSEVmtRPP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 751557642 312 AFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAE 359
Cdd:COG2905   76 ITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSE 122
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 234-354 4.13e-10

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: 57.63  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFL-----QLFMSDMPKPAFMKQNLDELGIGTY 308
Cdd:cd17779    8 KDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskYNLVEKKHNGNLLAAINEPVREIMT 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 354
Cdd:cd17779   88 RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 309-425 5.50e-10

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: 56.66  E-value: 5.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRsqyfegVVKCNK 388
Cdd:cd04623    2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRD------VVTCTP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751557642 389 ----LEILETIVDRIVRaevHRLVVvnEADSIVGIISLSDI 425
Cdd:cd04623   76 ddtvEECMALMTERRIR---HLPVV--EDGKLVGIVSIGDV 111
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
152-283 1.88e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 57.20  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 152 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKqsFVGMLTITDFINILHRYYKSPMVQIyeleehkietwRELYLqe 231
Cdd:COG2524   93 TKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDAPV-----------SDIMT-- 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 751557642 232 tfKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 283
Cdd:COG2524  158 --RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDD-DGKLVGIITRTDILRAL 206
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 309-359 2.01e-09

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: 53.37  E-value: 2.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 751557642  309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 359
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 309-425 4.69e-09

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: 53.96  E-value: 4.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVV------DIyskfdVIN-LAAEKTYNnlDITVTQALQHrsqyfe 381
Cdd:cd04622    3 RDVVTVSPDTTLREAARLMRDLDIGALPVCEG-DRLVgmvtdrDI-----VVRaVAEGKDPN--TTTVREVMTG------ 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 382 GVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 425
Cdd:cd04622   69 DVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 309-427 7.28e-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: 7.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEktyNNLDITVTQALQHRsqyfegVVKCNK 388
Cdd:cd04588    2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD-GKLVGIVTLTDIAKALAE---GKENAKVKDIMTKD------VITIDK 71

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 751557642 389 LEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQ 427
Cdd:cd04588   72 DEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 234-355 1.53e-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: 52.53  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLFMS-DMPKPAFMKQNLdelgIGTYhnia 312
Cdd:cd09836    3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVAEGIDlDTPVEEIMTKNL----VTVS---- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 751557642 313 fihPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 355
Cdd:cd09836   74 ---PDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 234-354 1.74e-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: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNAL-------------YILTHKRILKFLQLFMSDMPKPAfmKQNL 300
Cdd:cd04586    3 TDVVTVTPDTSVREAARLLLEHRISGLPVVD--DDGKLvgivsegdllrreEPGTEPRRVWWLDALLESPERLA--EEYV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 751557642 301 DELG-----IGTyHNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVI 354
Cdd:cd04586   79 KAHGrtvgdVMT-RPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLL 135
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 316-428 2.56e-08

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: 52.47  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 316 PDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEG---VVKCNKLEI- 391
Cdd:cd17789   10 PNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADSTWKTFNEVqklLSKTNGKVVg 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 751557642 392 -LETIVDRIVRAE--------------VHRLVVVNEADSIVGIISLSDILQA 428
Cdd:cd17789   90 dVMTPSPLVVREKtnledaarilletkFRRLPVVDSDGKLVGIITRGNVVRA 141
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 237-355 4.65e-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: 51.46  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 237 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFL---QLFMS----------DMPKPAFMKQNldel 303
Cdd:cd04631   11 ITATPGTPIEDVAKIMVRNGFRRLPVVS--DGKLVGIVTSTDIMRYLgsgEAFEKlktgnihevlNVPISSIMKRD---- 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 751557642 304 gigtyhnIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 355
Cdd:cd04631   85 -------IITTTPDTDLGEAAELMLEKNIGALPVVDD-GKLVGIITERDILR 128
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 236-355 7.11e-08

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: 50.51  E-value: 7.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 236 LVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLqlfmsdmpkpafmkqnLDelgiGTYHN----- 310
Cdd:cd04629    5 PVTLTPDTSILEAVELLLEHKISGAPVVDE-QGRLVGFLSEQDCLKAL----------------LE----ASYHCepggt 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 751557642 311 --------IAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 355
Cdd:cd04629   64 vadymsteVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDVLR 115
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 226-354 1.24e-07

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


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 50.42  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 226 ELYLQETfKPLVNISPDASLFDAVYSLIKNKIHRLPVIDpisGNALY-ILTHKRILKFLQLFMSDMPKPAFMKQNLDELG 304
Cdd:cd17777    3 ELMIIAS-PPVLSISPSAPILSAFEKMNRRGIRRLVVVD---ENKLEgILSARDLVSYLGGGCLFKIVESRHQGDLYSAL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 751557642 305 ----IGTYH--NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 354
Cdd:cd17777   79 nrevVETIMtpNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 234-356 1.25e-07

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: 49.87  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQnldelgigtyhNIAF 313
Cdd:cd17772    2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIYHGLGDLPVSEYMTT-----------EFAT 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINL 356
Cdd:cd17772   71 VTPDAPLSEIQEIIVEQRQRLVPVVED-GRLVGVITRTDLLNL 112
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 235-284 1.56e-07

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: 47.51  E-value: 1.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 751557642   235 PLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQ 284
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDE-EGRLVGIVTRRDIIKALA 49
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 234-354 3.80e-07

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: 48.87  E-value: 3.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFL--QLFMSDMPKP---AFMKQNLDELgigTY 308
Cdd:cd17778    8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFgsHEAKKRLTTGdidEAYSTPVEEI---MS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 354
Cdd:cd17778   83 KEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
159-283 6.70e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 48.32  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 159 DTTLqvKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILHRYYKSPMVqiYELEEHKIE---TwrelylqetfKP 235
Cdd:COG3448   18 DTTL--REALELMREHGIRGLPVVDEDGR-LVGIVTERDLLRALLPDRLDELE--ERLLDLPVEdvmT----------RP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 751557642 236 LVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 283
Cdd:COG3448   83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDD-DGRLVGIVTRTDLLRAL 129
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 383-430 8.02e-07

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: 45.58  E-value: 8.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 751557642   383 VVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 234-349 8.24e-07

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: 47.62  E-value: 8.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLqlfmsdmpkpAFMKQNLDElgIGTyHNIAF 313
Cdd:cd04605    8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSE-DGKLIGIVTSWDISKAV----------ALKKDSLEE--IMT-RNVIT 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYS 349
Cdd:cd04605   74 ARPDEPIELAARKMEKHNISALPVVDDDRRVIGIIT 109
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 235-355 1.21e-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: 47.11  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 235 PLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPAFMKQNldelgigtyhnIAFI 314
Cdd:cd04595    3 PVKTVSPDTTIEEARKIMLRYGHTGLPVVE--DGKLVGIISRRDVDKAKHHGLGHAPVKGYMSTN-----------VITI 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 751557642 315 HPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 355
Cdd:cd04595   70 DPDTSLEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVLR 109
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 383-430 7.05e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 43.36  E-value: 7.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 751557642  383 VVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 234-283 8.09e-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: 42.97  E-value: 8.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 751557642  234 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 283
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRAL 55
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
239-355 8.64e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 45.29  E-value: 8.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 239 ISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFlqlfMSDMPKPAFMKqnldelgigtyHNIAFIHPDT 318
Cdd:COG4109   30 LSEDDTVEDALELLEKTGHSRFPVVDE-NGRLVGIVTSKDILGK----DDDTPIEDVMT-----------KNPITVTPDT 93

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 751557642 319 PIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 355
Cdd:COG4109   94 SLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 310-425 1.01e-05

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


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 44.54  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQalqhrsqyfeGVVKCNKL 389
Cdd:cd04605    9 DVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALK-KDSLEEIMTR----------NVITARPD 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557642 390 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 425
Cdd:cd04605   78 EPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 239-355 1.44e-05

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 43.87  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 239 ISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLFMSdmpkpafmKQNLdelgigtyhnIAFIHPDT 318
Cdd:cd04597   10 LSPETSIKDAWNLMDENNLKTLPVTDD-NGKLIGLLSISDIARTVDYIMT--------KDNL----------IVFKEDDY 70

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 751557642 319 -PIIKalNIFVERRISALPVVDESGKVVDIYSKFDVIN 355
Cdd:cd04597   71 lDEVK--EIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 316-425 1.53e-05

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


Pssm-ID: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 44.14  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 316 PDTPIIKALNIFVERRISALpVVDESGKVVDIYSKFDVinLAaektynnLDITVTQALQHR-SQYFEGVVKCnkLEILET 394
Cdd:cd09833   12 PDTPLADAAARMAERRCSSI-LIVENGEIVGIWTERDA--LK-------LDFSDPDAFRRPiSEVMSSPVLT--IPQDTT 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 751557642 395 IVDRIVR---AEVHRLVVVNEADSIVGIISLSDI 425
Cdd:cd09833   80 LGEAAVRfrqEGVRHLLVVDDDGRPVGIVSQTDV 113
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 310-429 1.65e-05

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 44.24  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDeSGKVVDIYSKFDVI-NLAAEKTYNNLDIT-VTQALQHRSQYF--EGVVK 385
Cdd:cd17778    9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVkYFGSHEAKKRLTTGdIDEAYSTPVEEImsKEVVT 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 386 CNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 429
Cdd:cd17778   88 IEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 313-426 1.71e-05

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: 44.06  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 313 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN-LAAEKTynNLDITVTQALQHRsqyFEGVVKCNKLEI 391
Cdd:cd04608   14 TVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSsLLAGRA--QPSDPVSKAMYKQ---FKQVDLDTPLGA 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 751557642 392 LETIVDRivraeVHRLVVVNEADSIVGIISLSDIL 426
Cdd:cd04608   89 LSRILER-----DHFALVVDGQGKVLGIVTRIDLL 118
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 155-203 1.75e-05

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 41.73  E-value: 1.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 751557642   155 LVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILH 203
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGR-LVGIVTRRDIIKALA 49
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 313-426 1.82e-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: 43.56  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 313 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAaektynNLDITVtqalqhrSQY---FEGVVKCNKL 389
Cdd:cd04601    6 TLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFET------DLSTPV-------SEVmtpDERLVTAPEG 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 751557642 390 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDIL 426
Cdd:cd04601   73 ITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIE 109
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 314-425 1.88e-05

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


Pssm-ID: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 44.09  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDV-----INLAAEKTYNNLDITVTQALQHRSQY----FEGVV 384
Cdd:cd04640   10 IDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDIlgekpLKIVQERGIPREELLVADVMTPRDKLealdYEDVA 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 751557642 385 KCNKLEILETIVDrivRAEVHRLVVVNEADS---IVGIISLSDI 425
Cdd:cd04640   90 HARVGDVVETLKA---SGRQHALVVDRDEDGrqeVRGIFSASQI 130
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 310-347 2.94e-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: 43.34  E-value: 2.94e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDI 347
Cdd:cd17781   69 NPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGV 106
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 309-429 4.55e-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: 42.53  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFD-VINLAAEktynNLDITVTQALQHRSQyfEGVVKCN 387
Cdd:cd17775    3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDiVVEVVAK----GLDPKDVTVGDIMSA--DLITARE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 751557642 388 KLEILETIvdRIVRAE-VHRLVVVNEADSIVGIISLSDILQAL 429
Cdd:cd17775   77 DDGLFEAL--ERMREKgVRRLPVVDDDGELVGIVTLDDILELL 117
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 237-345 4.85e-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: 45.46  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642  237 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILThKRILKFLqlfmSDMPKP--AFMkqnldelgigTYHNIAFI 314
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVD--DGKLVGIVT-NRDLRFE----TDLSQPvsEVM----------TKENLVTA 153

                          90       100       110
                  ....*....|....*....|....*....|.
gi 751557642  315 HPDTPIIKALNIFVERRISALPVVDESGKVV 345
Cdd:pfam00478 154 PEGTTLEEAKEILHKHKIEKLPVVDDNGRLV 184
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 314-345 4.96e-05

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: 42.75  E-value: 4.96e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVV 345
Cdd:cd04604   83 ISPDALAAEALELMEEHKITVLPVVDEDGKPV 114
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 308-426 6.58e-05

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 41.95  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 308 YHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSkfdVINLAAEKTYnnldITVTqalqhrsqyfEGVVKCN 387
Cdd:cd04597    4 YDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLS---ISDIARTVDY----IMTK----------DNLIVFK 66

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 751557642 388 KLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDIL 426
Cdd:cd04597   67 EDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLI 105
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 239-356 1.91e-04

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: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 41.02  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 239 ISPDASLFDAVYSLI--KNKIHRLPVIDP-------ISGNAL-YILTHKrilkflqlfMSDMPKPAFMKqnldelgigTY 308
Cdd:cd04639   10 VDADLTLREFADDYLigKKSWREFLVTDEagrlvglITVDDLrAIPTSQ---------WPDTPVRELMK---------PL 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINL 356
Cdd:cd04639   72 EEIPTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIEL 119
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 314-426 1.97e-04

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: 40.40  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAektyNNLditVTQALQhrsqyfEGVVKCNKLEILE 393
Cdd:cd04599    8 ISPLDSVARAAALMERQRIGGLPVVEN-GKLVGIITSRDVRRAHP----NRL---VADAMS------RNVVTISPEASLW 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 751557642 394 TIVDRIVRAEVHRLVVVnEADSIVGIISLSDIL 426
Cdd:cd04599   74 EAKELMEEHGIERLVVV-EEGRLVGIITKSTLY 105
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 322-428 2.25e-04

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


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 40.40  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 322 KALNIFVERRISALPVV-DESGKVVDIYSKFDVINlaaektynNLDITVTQALQHRSqyfegVVKCNKLEILETIVDRIV 400
Cdd:cd04638   16 DVLEILKKKAISGVPVVkKETGKLVGIVTRKDLLR--------NPDEEQIALLMSRD-----PITISPDDTLSEAAELML 82

                         90       100
                 ....*....|....*....|....*...
gi 751557642 401 RAEVHRLVVVnEADSIVGIISLSDILQA 428
Cdd:cd04638   83 EHNIRRVPVV-DDDKLVGIVTVADLVRA 109
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 314-429 2.66e-04

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: 40.68  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDE-SGKVVDIYSKFDVI---------NLAAEKTYNNLDITVTQALqhRSQYFEGV 383
Cdd:cd17779   13 IPPTTTIIGAIKTMTEKGFRRLPVADAgTKRLEGIVTSMDIVdflgggskyNLVEKKHNGNLLAAINEPV--REIMTRDV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 751557642 384 VKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 429
Cdd:cd17779   91 ISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 310-429 2.75e-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: 40.48  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDV-INLAAEKTynNLDITVTQALqhrsqyfegVVKCNK 388
Cdd:cd17784    3 NVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLgHNLILDKY--ELGTTVEEVM---------VKDVAT 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 751557642 389 LEILETIVDRIVRAE--------VHRLVVVNEADsIVGIISLSDILQAL 429
Cdd:cd17784   72 VHPDETLLEAIKKMDsnapdeeiINQLPVVDDGK-LVGIISDGDIIRAI 119
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 314-426 5.56e-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: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSkFDVINLAAEKtynnlDITVTQALQHRsqyfegVVKCNKLEILE 393
Cdd:cd04583    7 ITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVD-IEDINRNYRK-----AKKVGEIMERD------VFTVKEDSLLR 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557642 394 TIVDRIVRAEVHRLVVVNEADSIVGII---SLSDIL 426
Cdd:cd04583   75 DTVDRILKRGLKYVPVVDEQGRLVGLVtraSLVDIV 110
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 190-264 5.76e-04

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: 39.31  E-value: 5.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751557642 190 VGMLTITDFINILHRYYKS-PMVQIYELEEHkietwrelylqetfkPLVNISPDASLFDAVYSLIKNKIHRLPVID 264
Cdd:cd17776   38 AGILTETDALHAGYATDDPfSEIPVRAVASR---------------PLVTISPTATLREAAERMVDEGVKKLPVVD 98
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 237-280 6.49e-04

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: 39.25  E-value: 6.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 751557642 237 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRIL 280
Cdd:cd04599   64 VTISPEASLWEAKELMEEHGIERLVVVE--EGRLVGIITKSTLY 105
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
139-284 1.09e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 39.13  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 139 FMRSHKCYDIVpTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINilhryyKSPMVQIYELEE 218
Cdd:COG4109   12 FKEILLVEDIM-TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGR-LVGIVTSKDILG------KDDDTPIEDVMT 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 751557642 219 HKIETwrelylqetfkplvnISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQ 284
Cdd:COG4109   84 KNPIT---------------VTPDTSLASAAHKMIWEGIELLPVVDD-DGRLLGIISRQDVLKALQ 133
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 ...
 234-264 1.43e-03

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: 38.18  E-value: 1.43e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVID 264
Cdd:cd04587   68 PPPVTIDADALVFEALLLMLERNIHHLPVVD 98
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 237-347 1.59e-03

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 38.16  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 237 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILThKRILKFLQlfMSDMPKPAFMKQNLDelgigtyhnIAFIH 315
Cdd:cd04601    5 VTLSPDATVADVLELKAEYGISGVPVTE--DGGKLVgIVT-SRDIRFET--DLSTPVSEVMTPDER---------LVTAP 70

                         90       100       110
                 ....*....|....*....|....*....|..
gi 751557642 316 PDTPIIKALNIFVERRISALPVVDESGKVVDI 347
Cdd:cd04601   71 EGITLEEAKEILHKHKIEKLPIVDDNGELVGL 102
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 314-428 1.78e-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: 37.71  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVinlaAEKTYNNLDITVTQALQHrsqyfegVVKCNKLE-IL 392
Cdd:cd04594    7 VSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDI----ENKSPGKVGKYVVRGSPY-------VTPTSSLEeAW 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557642 393 ETIVdrIVRAevhRLVVVNEADSIVGIISLSDILQA 428
Cdd:cd04594   76 EIMM--RNKS---RWVAVVEKGKFLGIITLDDLLEA 106
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 234-357 1.90e-03

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: 37.91  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 234 KPLVNISPDASLFDAVYSLIKNKIHRLPVID----PISgnalyILTHKRILKflqlfmsdmpkpAFMKQNLDELGIgTYH 309
Cdd:cd17775    3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEedgkPVG-----IVTDRDIVV------------EVVAKGLDPKDV-TVG 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 751557642 310 NI-----AFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLA 357
Cdd:cd17775   65 DImsadlITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
310-425 1.98e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 40.59  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDvinLAaeKTYnnLDITVTQALQHRSQYFEGVVKCNKL 389
Cdd:PRK14869  77 KPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSD---LA--RAY--MDILDPEILSKSPTSLENIIRTLDG 149

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 751557642 390 EILeTIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 425
Cdd:PRK14869 150 EVL-VGAEEDKVEEGKVVVAAMAPESLLERIEEGDI 184
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 237-359 2.26e-03

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: 37.85  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 237 VNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFlqlfmsdmpkpAFMKQNLDELGIGT----YHNIA 312
Cdd:cd04617    7 VVVDETTSVYDAIVTLFLEDVGSLFVVDE-EGYLVGVVSRKDLLKA-----------TLGGQDLEKTPVSMimtrMPNIV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 751557642 313 FIHPDTPIIKALNIFVERRISALPVVDESG---KVVDIYSKFDVINLAAE 359
Cdd:cd04617   75 TVTPDDSVLEAARKLIEHEIDSLPVVEKEDgklKVVGRITKTNITRLFVE 124
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 392-430 2.78e-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: 37.61  E-value: 2.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 751557642 392 LETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 430
Cdd:cd02205   13 VREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 404-429 3.79e-03

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: 37.52  E-value: 3.79e-03
                         10        20
                 ....*....|....*....|....*.
gi 751557642 404 VHRLVVVNEADSIVGIISLSDILQAL 429
Cdd:cd17774  100 IRRLVVVGEQGELLGIVTQTSLLQAL 125
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 237-354 4.45e-03

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 36.92  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 237 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILkflqLFMSDMPKPAFMKQNldelgigtyhnIAFIHP 316
Cdd:cd04610    6 ITVSPDDTVKDVIKLIKETGHDGFPVVD--DGKVVGYVTAKDLL----GKDDDEKVSEIMSRD-----------TVVADP 68

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 751557642 317 DTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 354
Cdd:cd04610   69 DMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 310-429 5.88e-03

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: 36.82  E-value: 5.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEKtynnlditvtqalqhrsQYFEGVVKCNKL 389
Cdd:cd04631    9 NVITATPGTPIEDVAKIMVRNGFRRLPVVSD-GKLVGIVTSTDIMRYLGSG-----------------EAFEKLKTGNIH 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 390 EILETIVDRIVRAEVHRL--------------------VVVNEADSIVGIISLSDILQAL 429
Cdd:cd04631   71 EVLNVPISSIMKRDIITTtpdtdlgeaaelmleknigaLPVVDDGKLVGIITERDILRAI 130
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 171-281 6.00e-03

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: 36.82  E-value: 6.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 171 LVANGVRAAPLWESKKqsFVGMLTITDFInilhRYYKSPMV-------QIYELEEHKIetwRELYLQEtfkpLVNISPDA 243
Cdd:cd04631   26 MVRNGFRRLPVVSDGK--LVGIVTSTDIM----RYLGSGEAfeklktgNIHEVLNVPI---SSIMKRD----IITTTPDT 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 751557642 244 SLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILK 281
Cdd:cd04631   93 DLGEAAELMLEKNIGALPVVD--DGKLVGIITERDILR 128
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
309-362 6.03e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 38.89  E-value: 6.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 309 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVV------DIYskfDVINLAAEKTY 362
Cdd:COG2239  201 TDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVgiitvdDVV---DVIEEEATEDI 257
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 315-347 6.40e-03

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


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 36.27  E-value: 6.40e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 751557642 315 HPDTPIIKALNIFVERRISALPVVDESGKVVDI 347
Cdd:cd04607   72 SPSTSREELLALMRAKKILQLPIVDEQGRVVGL 104
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 232-281 7.50e-03

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: 38.52  E-value: 7.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 751557642  232 TFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILK 281
Cdd:pfam00478 146 TKENLVTAPEGTTLEEAKEILHKHKIEKLPVVDD-NGRLVGLITIKDIEK 194
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 314-354 7.96e-03

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


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 36.68  E-value: 7.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 354
Cdd:cd17789   99 VREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVV 139
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 310-354 8.64e-03

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: 36.01  E-value: 8.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 751557642 310 NIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVI 354
Cdd:cd04801   68 DVITVSPDADAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 314-429 9.67e-03

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: 36.55  E-value: 9.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751557642 314 IHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEKTYNNLditvtqaLQHRSQYfeGVVKCNKLEILE 393
Cdd:cd17777   15 ISPSAPILSAFEKMNRRGIRRLVVVDE-NKLEGILSARDLVSYLGGGCLFKI-------VESRHQG--DLYSALNREVVE 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 751557642 394 TIVDR-------------IVRAEVHR----LVVVNEADSIVGIISLSDILQAL 429
Cdd:cd17777   85 TIMTPnpvyvyedsdlieALTIMVTRgigsLPVVDRDGRPVGIVTERDLVLYL 137
 
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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