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Conserved domains on  [gi|159795325]
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Chain E, Protein C1556.08c

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_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 191-314 2.27e-64

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: 199.27  E-value: 2.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 191 TWSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALLKRPANFDGVHTC 270
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 159795325 271 RATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 23-168 2.57e-62

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: 194.70  E-value: 2.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  23 TSYDVLPTSFRLIVFDVTLFVKTSLSLLTLNNIVSAPLWDSEANKFAGLLTMADFVNVIKYYYQSSSfpEAIAEIDKFRL 102
Cdd:cd04618    1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPS--VQMEELEEHTI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 159795325 103 LGLREVERKIGaiPPETIYVHPMHSLMDACLAMSKSRARRIPLIDvdgeTGSEMIVSVLTQYRILK 168
Cdd:cd04618   79 ETWREIERQIG--VPPLVSVHPEDSLYDAALLLLQNKIHRLPVID----PLTGNVLSVLTHKRILK 138
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 191-314 2.27e-64

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: 199.27  E-value: 2.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 191 TWSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALLKRPANFDGVHTC 270
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 159795325 271 RATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 23-168 2.57e-62

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: 194.70  E-value: 2.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  23 TSYDVLPTSFRLIVFDVTLFVKTSLSLLTLNNIVSAPLWDSEANKFAGLLTMADFVNVIKYYYQSSSfpEAIAEIDKFRL 102
Cdd:cd04618    1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPS--VQMEELEEHTI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 159795325 103 LGLREVERKIGaiPPETIYVHPMHSLMDACLAMSKSRARRIPLIDvdgeTGSEMIVSVLTQYRILK 168
Cdd:cd04618   79 ETWREIERQIG--VPPLVSVHPEDSLYDAALLLLQNKIHRLPVID----PLTGNVLSVLTHKRILK 138
CBS COG0517
CBS domain [Signal transduction mechanisms];
187-315 2.82e-16

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 74.13  E-value: 2.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 187 MTIGTW--SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLL-NVYESvDVMHLIQDGDYSNLDLSVGEALLKRPan 263
Cdd:COG0517    1 MKVKDImtTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVgIVTDR-DLRRALAAEGKDLLDTPVSEVMTRPP-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 159795325 264 fdgvHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYIIY 315
Cdd:COG0517   78 ----VTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
26-229 2.76e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 47.57  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  26 DVLPTSFRLIVFDVTLFVKTSLSLLTLNNIVSAPLWDSEANKFAGLLTMADFVNVIKYYYQSSSFPEAIAEIDKFRLLGL 105
Cdd:COG2524    2 LVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 106 REVERKIG-AIPPETIYVHPMHSLMDACLAMSKSRARRIPLIDvDGEtgsemIVSVLTQYRILKFISmncKETAMLRVPL 184
Cdd:COG2524   82 LVLKMKVKdIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGK-----LVGIITERDLLKALA---EGRDLLDAPV 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 159795325 185 NQ-MTigtwSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLL 229
Cdd:COG2524  153 SDiMT----RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLV 194
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 267-314 3.90e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 40.66  E-value: 3.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 159795325  267 VHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 269-314 5.77e-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: 40.19  E-value: 5.77e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 159795325   269 TCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:smart00116   4 TVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 118-170 4.94e-03

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: 34.41  E-value: 4.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 159795325   118 ETIYVHPMHSLMDACLAMSKSRARRIPLIDVDGEtgsemIVSVLTQYRILKFI 170
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGR-----LVGIVTRRDIIKAL 48
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 191-314 2.27e-64

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: 199.27  E-value: 2.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 191 TWSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALLKRPANFDGVHTC 270
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 159795325 271 RATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:cd04641   81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 23-168 2.57e-62

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: 194.70  E-value: 2.57e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  23 TSYDVLPTSFRLIVFDVTLFVKTSLSLLTLNNIVSAPLWDSEANKFAGLLTMADFVNVIKYYYQSSSfpEAIAEIDKFRL 102
Cdd:cd04618    1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPS--VQMEELEEHTI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 159795325 103 LGLREVERKIGaiPPETIYVHPMHSLMDACLAMSKSRARRIPLIDvdgeTGSEMIVSVLTQYRILK 168
Cdd:cd04618   79 ETWREIERQIG--VPPLVSVHPEDSLYDAALLLLQNKIHRLPVID----PLTGNVLSVLTHKRILK 138
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 193-311 1.37e-17

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: 77.28  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYsNLDLSVGEALLKRPanfdgvHTCRA 272
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGL-ALDTPVAEVMTPDV------ITVSP 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILN 311
Cdd:cd02205   75 DTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
187-315 2.82e-16

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 74.13  E-value: 2.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 187 MTIGTW--SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLL-NVYESvDVMHLIQDGDYSNLDLSVGEALLKRPan 263
Cdd:COG0517    1 MKVKDImtTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVgIVTDR-DLRRALAAEGKDLLDTPVSEVMTRPP-- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 159795325 264 fdgvHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYIIY 315
Cdd:COG0517   78 ----VTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
187-314 2.61e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 66.04  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 187 MTIGTW--SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLL-NVYESvDVMHLIQDGDYSNL-----DLSVGEaLL 258
Cdd:COG3448    2 MTVRDImtRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVgIVTER-DLLRALLPDRLDELeerllDLPVED-VM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 159795325 259 KRPanfdgVHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:COG3448   80 TRP-----VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 193-316 1.17e-12

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 64.08  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALLKRPanfdgvHTCRA 272
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPP------ITVSP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENlKLEGILSLADILNYIIYD 316
Cdd:COG2905   81 DDSLAEALELMEEHRIRHLPVVDDG-KLVGIVSITDLLRALSEE 123
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 187-310 1.63e-12

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: 63.99  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 187 MTigtwSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLN-VYESvDVMHLIQDGD---YSNLDLSVGEALLKRPA 262
Cdd:cd04586    1 MT----TDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGiVSEG-DLLRREEPGTeprRVWWLDALLESPERLAE 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159795325 263 NFD-------------GVHTCRATDRLDGIFDAIKHSRVHRLFVVDENlKLEGILSLADIL 310
Cdd:cd04586   76 EYVkahgrtvgdvmtrPVVTVSPDTPLEEAARLMERHRIKRLPVVDDG-KLVGIVSRADLL 135
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
193-313 5.26e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 58.36  E-value: 5.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNsEGTLLNVYESVDVMHLIQDGDYSnLDLSVGEALLKRPAnfdgvhTCRA 272
Cdd:COG2524   94 KDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGRDL-LDAPVSDIMTRDVV------TVSE 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYI 313
Cdd:COG2524  166 DDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 34-168 6.15e-10

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: 56.10  E-value: 6.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  34 LIVFDVTLFVKTSLSLLTLNNIVSAPLWDsEANKFAGLLTMADFVNVIKYYYQSSSFPeaIAEIdkfrllglreverkig 113
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVD-DDGKLVGIVTERDILRALVEGGLALDTP--VAEV---------------- 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 159795325 114 aIPPETIYVHPMHSLMDACLAMSKSRARRIPLIDVDGEtgsemIVSVLTQYRILK 168
Cdd:cd02205   65 -MTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGK-----LVGIVTRRDILR 113
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 193-309 7.32e-08

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


Pssm-ID: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 50.11  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALLKRpanfdgVHTCRA 272
Cdd:cd04623    2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRD------VVTCTP 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENlKLEGILSLADI 309
Cdd:cd04623   76 DDTVEECMALMTERRIRHLPVVEDG-KLVGIVSIGDV 111
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 117-231 1.87e-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: 49.65  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 117 PETIYVHPMHSLMDACLAMSKSRARRIPLID---VDGETGSEMIVSVLTQYRiLKFISMNCKETAMLRVpLNQMTIGTW- 192
Cdd:cd17777   10 PPVLSISPSAPILSAFEKMNRRGIRRLVVVDenkLEGILSARDLVSYLGGGC-LFKIVESRHQGDLYSA-LNREVVETIm 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 159795325 193 -SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNV 231
Cdd:cd17777   88 tPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGI 127
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 187-309 2.65e-07

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: 48.57  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 187 MTigtwSNLATASMETKVYDVIKMLAEKNISAVPIVNsEGTLLNVYESVD-VMHLIQDGDySNLDLSVGEALLKrpanfd 265
Cdd:cd04622    1 MT----RDVVTVSPDTTLREAARLMRDLDIGALPVCE-GDRLVGMVTDRDiVVRAVAEGK-DPNTTTVREVMTG------ 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 159795325 266 GVHTCRATDRLDgifDAIKH---SRVHRLFVVDENLKLEGILSLADI 309
Cdd:cd04622   69 DVVTCSPDDDVE---EAARLmaeHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 193-313 9.92e-07

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 46.75  E-value: 9.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDysNLDLSVGEALlkrpanFDGVHTCRA 272
Cdd:cd09836    3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGI--DLDTPVEEIM------TKNLVTVSP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYI 313
Cdd:cd09836   75 DESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 193-311 1.11e-06

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 46.64  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLiqdgdySNLDLSVGEALLKRpanfDGVHTCRA 272
Cdd:cd04601    2 TDPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFE------TDLSTPVSEVMTPD----ERLVTAPE 71

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILN 311
Cdd:cd04601   72 GITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK 110
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
26-229 2.76e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 47.57  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  26 DVLPTSFRLIVFDVTLFVKTSLSLLTLNNIVSAPLWDSEANKFAGLLTMADFVNVIKYYYQSSSFPEAIAEIDKFRLLGL 105
Cdd:COG2524    2 LVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 106 REVERKIG-AIPPETIYVHPMHSLMDACLAMSKSRARRIPLIDvDGEtgsemIVSVLTQYRILKFISmncKETAMLRVPL 184
Cdd:COG2524   82 LVLKMKVKdIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGK-----LVGIITERDLLKALA---EGRDLLDAPV 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 159795325 185 NQ-MTigtwSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLL 229
Cdd:COG2524  153 SDiMT----RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLV 194
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 194-311 2.92e-06

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 45.51  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 194 NLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMH-LIQDGDYSNLDLSVGEALLKrpanfdGVHTCRA 272
Cdd:cd04629    4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKaLLEASYHCEPGGTVADYMST------EVLTVSP 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 159795325 273 TdrlDGIFDAIK---HSRVHRLFVVDENlKLEGILSLADILN 311
Cdd:cd04629   78 D---TSIVDLAQlflKNKPRRYPVVEDG-KLVGQISRRDVLR 115
CBS COG0517
CBS domain [Signal transduction mechanisms];
120-229 5.06e-06

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 45.24  E-value: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 120 IYVHPMHSLMDACLAMSKSRARRIPLIDVDGEtgsemIVSVLTQYRILKFisMNCKETAMLRVPLNQ-MTigtwSNLATA 198
Cdd:COG0517   12 VTVSPDATVREALELMSEKRIGGLPVVDEDGK-----LVGIVTDRDLRRA--LAAEGKDLLDTPVSEvMT----RPPVTV 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 159795325 199 SMETKVYDVIKMLAEKNISAVPIVNSEGTLL 229
Cdd:COG0517   81 SPDTSLEEAAELMEEHKIRRLPVVDDDGRLV 111
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 193-312 1.53e-05

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 43.29  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNsEGTLLNVYESVDVMHLIQDGdysNLDLSVGEALLKRpanfdgVHTCRA 272
Cdd:cd04588    2 KDLITLKPDATIKDAAKLLSENNIHGAPVVD-DGKLVGIVTLTDIAKALAEG---KENAKVKDIMTKD------VITIDK 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 159795325 273 TDRldgIFDAIKHSRVH---RLFVVDENLKLEGILSLADILNY 312
Cdd:cd04588   72 DEK---IYDAIRLMNKHnigRLIVVDDNGKPVGIITRTDILKV 111
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
194-315 1.84e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 43.75  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 194 NLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHliqdgdySNLDLSVGEALLKRPAnfdgvhTCRAT 273
Cdd:COG4109   26 DVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG-------KDDDTPIEDVMTKNPI------TVTPD 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 159795325 274 DRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYIIY 315
Cdd:COG4109   93 TSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQK 134
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 267-314 3.90e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 40.66  E-value: 3.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 159795325  267 VHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 269-314 5.77e-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: 40.19  E-value: 5.77e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 159795325   269 TCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYII 314
Cdd:smart00116   4 TVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 118-241 1.91e-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: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 118 ETIYVHPMHSLMDACLAMSKSRARRIPLIDvdgeTGSEMIVSVLTQYRILKFISMNCKET-----------AMLRVPLNQ 186
Cdd:cd17779    9 DVITIPPTTTIIGAIKTMTEKGFRRLPVAD----AGTKRLEGIVTSMDIVDFLGGGSKYNlvekkhngnllAAINEPVRE 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 159795325 187 -MTigtwSNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLI 241
Cdd:cd17779   85 iMT----RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 193-243 2.52e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 38.35  E-value: 2.52e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 159795325  193 SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQD 243
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 194-311 2.83e-04

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: 39.64  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 194 NLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESvdvmhliqdgdySNLDLSVGEALLKrpanfDGVHTCRAT 273
Cdd:cd04597    6 KVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSI------------SDIARTVDYIMTK-----DNLIVFKED 68

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 159795325 274 DRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILN 311
Cdd:cd04597   69 DYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 193-309 5.04e-04

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: 39.14  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQdGDYSNLDlsvgEALLKRpanfdgVHTCRA 272
Cdd:cd04605    8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVA-LKKDSLE----EIMTRN------VITARP 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADI 309
Cdd:cd04605   77 DEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 197-311 5.61e-04

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: 41.61  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  197 TASMETKVYDVIKMLAEKNISAVPIVNsEGTLLNVYESVDVMHLiqdgdySNLDLSVGEALLKRPanfdgVHTCRATDRL 276
Cdd:pfam00478  92 TLSPDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDLRFE------TDLSQPVSEVMTKEN-----LVTAPEGTTL 159

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 159795325  277 DGIFDAIKHSRVHRLFVVDENLKLEGILSLADILN 311
Cdd:pfam00478 160 EEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIEK 194
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 194-313 5.63e-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: 39.33  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 194 NLATASMETKVYDVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMH-LIQDgDYSnLDLSVGEALLKRpanfdgVHTCRA 272
Cdd:cd17784    3 NVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHnLILD-KYE-LGTTVEEVMVKD------VATVHP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 159795325 273 TDRldgIFDAIK--------HSRVHRLFVVDENlKLEGILSLADILNYI 313
Cdd:cd17784   75 DET---LLEAIKkmdsnapdEEIINQLPVVDDG-KLVGIISDGDIIRAI 119
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 187-314 7.47e-04

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: 38.94  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 187 MTigtwSNLATASMETKVYDVIKMLAEKNISAVPIVN--------SEGTLLNVYESVDVMHLIQDGDYSNLDLSVGEALL 258
Cdd:cd04584    6 MT----KNVVTVTPDTSLAEARELMKEHKIRHLPVVDdgklvgivTDRDLLRASPSKATSLSIYELNYLLSKIPVKDIMT 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 159795325 259 KRpanfdgVHTCRAtdrLDGIFDAIKHSRVHR---LFVVDENlKLEGILSLADILNYII 314
Cdd:cd04584   82 KD------VITVSP---DDTVEEAALLMLENKigcLPVVDGG-KLVGIITETDILRAFI 130
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 196-310 1.36e-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: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 196 ATASMETKVYDVIKMLAEKNISAVPIVNSEG-----------TLLNVYESVDVMhliqdgdysnlDLSVGEaLLKRPanf 264
Cdd:cd17775    6 VTASPDTSVLEAARLMRDHHVGSVVVVEEDGkpvgivtdrdiVVEVVAKGLDPK-----------DVTVGD-IMSAD--- 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 159795325 265 dgVHTCRATDrldGIFDAIKHSRVH---RLFVVDENLKLEGILSLADIL 310
Cdd:cd17775   71 --LITAREDD---GLFEALERMREKgvrRLPVVDDDGELVGIVTLDDIL 114
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 267-321 1.67e-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: 1.67e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 159795325 267 VHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYIIYDKTTTP 321
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALD 58
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 206-312 1.86e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 37.51  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 206 DVIKMLAEKNISAVPIVNSEGTLLNVYESVDVMHLIQDGDySNLDLSVGEALLKRpanfdgVHTCRATD---RLDGIFDa 282
Cdd:cd04608   23 EAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGR-AQPSDPVSKAMYKQ------FKQVDLDTplgALSRILE- 94

                         90       100       110
                 ....*....|....*....|....*....|
gi 159795325 283 ikhsRVHRLFVVDENLKLEGILSLADILNY 312
Cdd:cd04608   95 ----RDHFALVVDGQGKVLGIVTRIDLLNY 120
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 277-322 2.52e-03

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: 37.31  E-value: 2.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 159795325 277 DGIFDAIKHSRVH---RLFVVDENLKLEGILSLADILNYIIYDKTTTPG 322
Cdd:cd04632   11 DTIGKAINLLREHgisRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRG 59
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 120-223 2.78e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 37.12  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 120 IYVHPMHSLMDACLAMSKSRARRIPLIDVDGEtgsemIVSVLTQYRILKFISMncKETAMLRVPLNQ-MTigtwSNLATA 198
Cdd:COG2905   10 VTVSPDATVREAARLMTEKGVGSLVVVDDDGR-----LVGIITDRDLRRRVLA--EGLDPLDTPVSEvMT----RPPITV 78

                         90       100
                 ....*....|....*....|....*
gi 159795325 199 SMETKVYDVIKMLAEKNISAVPIVN 223
Cdd:COG2905   79 SPDDSLAEALELMEEHRIRHLPVVD 103
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 187-313 2.82e-03

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: 37.60  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 187 MTIGTwSNLATASMETKVYDVIKMLAEKNISAVPIVNSeGT--LLNVYESVDVMHLIQDGDYSNL-------------DL 251
Cdd:cd17779    3 MAIAT-KDVITIPPTTTIIGAIKTMTEKGFRRLPVADA-GTkrLEGIVTSMDIVDFLGGGSKYNLvekkhngnllaaiNE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 159795325 252 SVGEALLKRpanfdgVHTCRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADILNYI 313
Cdd:cd17779   81 PVREIMTRD------VISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 273-313 3.85e-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: 36.94  E-value: 3.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 159795325 273 TDRLDGIFDAIKHSRVHRLFVVDENlKLEGILSLADILNYI 313
Cdd:cd17777   18 SAPILSAFEKMNRRGIRRLVVVDEN-KLEGILSARDLVSYL 57
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 193-309 4.49e-03

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


Pssm-ID: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 36.43  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 193 SNLATASMETKVYDVIKMLAEKNISAVpIVNSEGTLLNVYESVDVMHLiqdgDYSN---LDLSVGEaLLKRPanfdgVHT 269
Cdd:cd09833    5 TSLLTCSPDTPLADAAARMAERRCSSI-LIVENGEIVGIWTERDALKL----DFSDpdaFRRPISE-VMSSP-----VLT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 159795325 270 CRATDRLDGIFDAIKHSRVHRLFVVDENLKLEGILSLADI 309
Cdd:cd09833   74 IPQDTTLGEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDV 113
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 118-170 4.94e-03

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: 34.41  E-value: 4.94e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 159795325   118 ETIYVHPMHSLMDACLAMSKSRARRIPLIDVDGEtgsemIVSVLTQYRILKFI 170
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGR-----LVGIVTRRDIIKAL 48
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
64-168 7.79e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 36.00  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325  64 EANKFAGLLTMADFVNVIKyyyqsssfpeaiaeIDKFRLLGLREVERKIGAI-PPETIYVHPMHSLMDACLAMSKSRARR 142
Cdd:COG3448   41 EDGRLVGIVTERDLLRALL--------------PDRLDELEERLLDLPVEDVmTRPVVTVTPDTPLEEAAELMLEHGIHR 106

                         90       100
                 ....*....|....*....|....*.
gi 159795325 143 IPLIDVDGEtgsemIVSVLTQYRILK 168
Cdd:COG3448  107 LPVVDDDGR-----LVGIVTRTDLLR 127
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 194-313 9.07e-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: 36.05  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159795325 194 NLATASMETKVYDVIKMLAEKNISAVPIVnSEGTLLNVYESVDVMHLIQDGD-YSNLDLSVGEALLKRPAN---FDGVHT 269
Cdd:cd04631    9 NVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIMRYLGSGEaFEKLKTGNIHEVLNVPISsimKRDIIT 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 159795325 270 CRATDRLDGIFDAIKHSRVHRLFVVDeNLKLEGILSLADILNYI 313
Cdd:cd04631   88 TTPDTDLGEAAELMLEKNIGALPVVD-DGKLVGIITERDILRAI 130
 
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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