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Conserved domains on  [gi|71998166|ref|NP_508509|]
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CBS domain-containing protein [Caenorhabditis elegans]

Protein Classification

CBS domain-containing protein( domain architecture ID 66840)

CBS (cystathione beta synthase) domain-containing protein; the CBS domains may act as regulatory units

PubMed:  24161944

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 103-255 1.28e-27

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


The actual alignment was detected with superfamily member cd04618:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 138  Bit Score: 106.49  E-value: 1.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 103 QCYEAMARNNKLIVFTNDISVRKAFNGLIYNCMRTGLVADSQTLEITGVLSVTDFIMVLMMLWKY----RENLDELKgtp 178
Cdd:cd04618   1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSpsvqMEELEEHT--- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71998166 179 lshedfrqmdiaympISRWKGcLETKGQLKPFINIGLKESIFRAVELLTKYRIHRLPVMDEKTGDCAYILTHRRILH 255
Cdd:cd04618  78 ---------------IETWRE-IERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 281-408 6.79e-25

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


The actual alignment was detected with superfamily member cd04641:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 124  Bit Score: 98.74  E-value: 6.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 281 SWKNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAAS-AAFSDHIDLSVSVTRAIQER--DYQngir 357
Cdd:cd04641   1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDG-RVVDIYAKFDVINlAAEKTYNNLDLTVGEALQHRseDFE---- 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71998166 358 rdGVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLV 408
Cdd:cd04641  76 --GVHTCTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 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 ...
 103-255 1.28e-27

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: 106.49  E-value: 1.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 103 QCYEAMARNNKLIVFTNDISVRKAFNGLIYNCMRTGLVADSQTLEITGVLSVTDFIMVLMMLWKY----RENLDELKgtp 178
Cdd:cd04618   1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSpsvqMEELEEHT--- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71998166 179 lshedfrqmdiaympISRWKGcLETKGQLKPFINIGLKESIFRAVELLTKYRIHRLPVMDEKTGDCAYILTHRRILH 255
Cdd:cd04618  78 ---------------IETWRE-IERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 281-408 6.79e-25

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: 98.74  E-value: 6.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 281 SWKNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAAS-AAFSDHIDLSVSVTRAIQER--DYQngir 357
Cdd:cd04641   1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDG-RVVDIYAKFDVINlAAEKTYNNLDLTVGEALQHRseDFE---- 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71998166 358 rdGVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLV 408
Cdd:cd04641  76 --GVHTCTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
283-407 1.69e-11

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 63.36  E-value: 1.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNtlKVLEVYTRFDAASAAFSDHIDLSVSVtraiqeRDYqngIRRDgVV 362
Cdd:COG2524  94 KDVITVSPDTTLEEALELMLEKGISGLPVVDDG--KLVGIITERDLLKALAEGRDLLDAPV------SDI---MTRD-VV 161

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:COG2524 162 TVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
208-315 7.82e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 53.72  E-value: 7.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEK---TGdcayILTHRRILHYIWKHCALLPKPECLSQRVVDLeigSWKN 284
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDgrlVG----IVTERDLLRALLPDRLDELEERLLDLPVEDV---MTRP 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 71998166 285 LIFANEQTPLIECLDMLIDNNISGIPIVQKN 315
Cdd:COG3448  83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDDD 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 356-408 6.55e-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: 6.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71998166   356 IRRDGVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLV 408
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 361-407 4.13e-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: 40.57  E-value: 4.13e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 71998166    361 VVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 208-259 1.11e-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: 39.89  E-value: 1.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 71998166   208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHYIWK 259
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 217-258 2.50e-04

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 38.65  E-value: 2.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 71998166    217 ESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHYIW 258
Cdd:smart00116   9 TTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKALA 49
 
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 ...
 103-255 1.28e-27

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: 106.49  E-value: 1.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 103 QCYEAMARNNKLIVFTNDISVRKAFNGLIYNCMRTGLVADSQTLEITGVLSVTDFIMVLMMLWKY----RENLDELKgtp 178
Cdd:cd04618   1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSpsvqMEELEEHT--- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71998166 179 lshedfrqmdiaympISRWKGcLETKGQLKPFINIGLKESIFRAVELLTKYRIHRLPVMDEKTGDCAYILTHRRILH 255
Cdd:cd04618  78 ---------------IETWRE-IERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 281-408 6.79e-25

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: 98.74  E-value: 6.79e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 281 SWKNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAAS-AAFSDHIDLSVSVTRAIQER--DYQngir 357
Cdd:cd04641   1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDG-RVVDIYAKFDVINlAAEKTYNNLDLTVGEALQHRseDFE---- 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 71998166 358 rdGVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLV 408
Cdd:cd04641  76 --GVHTCTLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
283-407 1.69e-11

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 63.36  E-value: 1.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNtlKVLEVYTRFDAASAAFSDHIDLSVSVtraiqeRDYqngIRRDgVV 362
Cdd:COG2524  94 KDVITVSPDTTLEEALELMLEKGISGLPVVDDG--KLVGIITERDLLKALAEGRDLLDAPV------SDI---MTRD-VV 161

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:COG2524 162 TVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
283-408 5.55e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 59.88  E-value: 5.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAASAAFSDHIDLSVSVTRAIQERDyqngIRRDGVV 362
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDG-RLVGIVTERDLLRALLPDRLDELEERLLDLPVED----VMTRPVV 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLV 408
Cdd:COG3448  85 TVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS COG0517
CBS domain [Signal transduction mechanisms];
283-408 6.19e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 59.49  E-value: 6.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAASAAFSDHIDLSvsvTRAIQErdyqngIRRDGVV 362
Cdd:COG0517   9 TDVVTVSPDATVREALELMSEKRIGGLPVVDEDG-KLVGIVTDRDLRRALAAEGKDLL---DTPVSE------VMTRPPV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLV 408
Cdd:COG0517  79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 283-404 1.55e-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: 58.02  E-value: 1.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAASAAFSDHIDLSVSVTraiqerdyqnGIRRDGVV 362
Cdd:cd02205   2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDG-KLVGIVTERDILRALVEGGLALDTPVA----------EVMTPDVI 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVI 404
Cdd:cd02205  71 TVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
208-315 7.82e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 53.72  E-value: 7.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEK---TGdcayILTHRRILHYIWKHCALLPKPECLSQRVVDLeigSWKN 284
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDgrlVG----IVTERDLLRALLPDRLDELEERLLDLPVEDV---MTRP 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 71998166 285 LIFANEQTPLIECLDMLIDNNISGIPIVQKN 315
Cdd:COG3448  83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDDD 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
208-331 2.23e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 52.18  E-value: 2.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHYIWKHcallpKPECLSQRVVDLeigSWKNLIF 287
Cdd:COG0517   9 TDVVTVSPDATVREALELMSEKRIGGLPVVDED-GKLVGIVTDRDLRRALAAE-----GKDLLDTPVSEV---MTRPPVT 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 71998166 288 ANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAASA 331
Cdd:COG0517  80 VSPDTSLEEAAELMEEHKIRRLPVVDDDG-RLVGIITIKDLLKA 122
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 283-407 2.62e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 52.14  E-value: 2.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAASAAFSDHIDLSVSVTRAIQERDyqngirrdgVV 362
Cdd:COG2905   7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDG-RLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRP---------PI 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILkGIISLSDVIEFL 407
Cdd:COG2905  77 TVSPDDSLAEALELMEEHRIRHLPVVDDGKLV-GIVSITDLLRAL 120
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 208-315 4.97e-08

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: 51.09  E-value: 4.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHYIWKHCALLPKP--ECLSqrvvdleigswKNL 285
Cdd:cd02205   2 RDVVTVDPDTTVREALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPvaEVMT-----------PDV 69

                        90       100       110
                ....*....|....*....|....*....|
gi 71998166 286 IFANEQTPLIECLDMLIDNNISGIPIVQKN 315
Cdd:cd02205  70 ITVSPDTDLEEALELMLEHGIRRLPVVDDD 99
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 208-317 1.49e-07

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: 50.11  E-value: 1.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEktGDCAYILTHRRILHyiwkhcALLPKPECLSQRVVDLEIGSW----- 282
Cdd:cd04584   8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVDD--GKLVGIVTDRDLLR------ASPSKATSLSIYELNYLLSKIpvkdi 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71998166 283 --KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTL 317
Cdd:cd04584  80 mtKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKL 116
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 283-405 4.14e-07

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 48.30  E-value: 4.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNtlKVLEVYTRFDAASAAFSDHIDLSVSvtrAIQERDyqngirrdgVV 362
Cdd:cd04588   2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDDG--KLVGIVTLTDIAKALAEGKENAKVK---DIMTKD---------VI 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIE 405
Cdd:cd04588  68 TIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 356-408 6.55e-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: 6.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 71998166   356 IRRDGVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLV 408
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 283-407 2.92e-05

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: 42.90  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAASAAfSDHIDLSVSVTRaiqerdyqngIRRDGVV 362
Cdd:cd09836   3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDG-KPVGIVTERDIVRAV-AEGIDLDTPVEE----------IMTKNLV 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:cd09836  71 TVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 361-407 4.13e-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: 40.57  E-value: 4.13e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 71998166    361 VVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 218-317 7.13e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 42.12  E-value: 7.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 218 SIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHyiwkhcALLPKPECLSQRVVDlEIGSwKNLIFANEQTPLIEC 297
Cdd:COG2905  17 TVREAARLMTEKGVGSLVVVDDD-GRLVGIITDRDLRR------RVLAEGLDPLDTPVS-EVMT-RPPITVSPDDSLAEA 87

                        90       100
                ....*....|....*....|
gi 71998166 298 LDMLIDNNISGIPIVQKNTL 317
Cdd:COG2905  88 LELMEEHRIRHLPVVDDGKL 107
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 361-407 7.16e-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: 42.14  E-value: 7.16e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 71998166 361 VVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:cd17775  71 LITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 208-259 1.11e-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: 39.89  E-value: 1.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 71998166   208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHYIWK 259
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRALLG 57
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 283-404 1.12e-04

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: 42.03  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYT------RFDAASAAFSDHIDLSVSVTRAIQERDYQ--N 354
Cdd:cd04586   3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDDDG-KLVGIVSegdllrREEPGTEPRRVWWLDALLESPERLAEEYVkaH 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71998166 355 GIR-RD----GVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTiLKGIISLSDVI 404
Cdd:cd04586  82 GRTvGDvmtrPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGK-LVGIVSRADLL 135
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 217-258 2.50e-04

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 38.65  E-value: 2.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 71998166    217 ESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHYIW 258
Cdd:smart00116   9 TTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKALA 49
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 292-406 5.07e-04

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: 39.40  E-value: 5.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 292 TPLIECLDMLIDNNISGIPIVQKNtlKVLEVYTRFDAASAAfsdHIDLSVSVTRAIQERDyqngirrdgVVTANYTTTLW 371
Cdd:cd04595  11 TTIEEARKIMLRYGHTGLPVVEDG--KLVGIISRRDVDKAK---HHGLGHAPVKGYMSTN---------VITIDPDTSLE 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 71998166 372 SLIEIFIDKNVHRIFMVDDrTILKGIISLSDVIEF 406
Cdd:cd04595  77 EAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVLRY 110
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 296-404 6.48e-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: 39.25  E-value: 6.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 296 ECLDMLIDNNISGIPIVQKNTLKVLEVYTRFDAASAafSDHIDLSVSVTRaiqerdyqngirrdGVVTANYTTTLWSLIE 375
Cdd:cd04638  16 DVLEILKKKAISGVPVVKKETGKLVGIVTRKDLLRN--PDEEQIALLMSR--------------DPITISPDDTLSEAAE 79

                        90       100
                ....*....|....*....|....*....
gi 71998166 376 IFIDKNVHRIFMVDDRTiLKGIISLSDVI 404
Cdd:cd04638  80 LMLEHNIRRVPVVDDDK-LVGIVTVADLV 107
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 361-422 1.03e-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: 38.85  E-value: 1.03e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71998166 361 VVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFlVLRPTKKNgvTTGEP 422
Cdd:cd04632   4 VITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDF-VVRPGTKT--RGGDR 62
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 283-408 1.59e-03

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: 38.56  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNtlKVLEVYTRFDAASAAFSDHIDLSvsvtraIQERDYQ-NGIR---- 357
Cdd:cd04584   8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVDDG--KLVGIVTDRDLLRASPSKATSLS------IYELNYLlSKIPvkdi 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 71998166 358 --RDgVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTiLKGIISLSDVIEFLV 408
Cdd:cd04584  80 mtKD-VITVSPDDTVEEAALLMLENKIGCLPVVDGGK-LVGIITETDILRAFI 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
361-410 1.67e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 38.31  E-value: 1.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71998166 361 VVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLVLR 410
Cdd:COG3448  12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPD 61
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 208-251 1.72e-03

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: 37.93  E-value: 1.72e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEKTGDCAYILTHR 251
Cdd:cd17772   2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQ 45
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 283-405 2.37e-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: 37.70  E-value: 2.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTlKVLEVYTRFDAASAAFSDHIDLSVSVTRAIQERDYQNGIR---RD 359
Cdd:cd04632   2 EEVITVNEDDTIGKAINLLREHGISRLPVVDDNG-KLVGIVTTYDIVDFVVRPGTKTRGGDRGGEKERMLDLPVYdimSS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 71998166 360 GVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIE 405
Cdd:cd04632  81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 208-257 2.67e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 37.50  E-value: 2.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEktGDCAYILTHRRILHYI 257
Cdd:COG2905  73 RPPITVSPDDSLAEALELMEEHRIRHLPVVDD--GKLVGIVSITDLLRAL 120
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 217-317 2.92e-03

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


Pssm-ID: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 37.40  E-value: 2.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 217 ESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHyiwkHCALLPKpECLSQRVVDLeigSWKNLIFANEQTPLIE 296
Cdd:cd04623  11 ATVAEALRLLAEKNIGALVVVDDG-GRLVGILSERDYVR----KLALRGA-SSLDTPVSEI---MTRDVVTCTPDDTVEE 81

                        90       100
                ....*....|....*....|.
gi 71998166 297 CLDMLIDNNISGIPIVQKNTL 317
Cdd:cd04623  82 CMALMTERRIRHLPVVEDGKL 102
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 291-404 3.00e-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: 37.20  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 291 QTPLIECLDMLIDNNISGIPIVQKNtlKVLEVYTRFDAASAAFSDHIDLSVSVtraiqeRDYQNGirrdGVVTANYTTTL 370
Cdd:cd09833  13 DTPLADAAARMAERRCSSILIVENG--EIVGIWTERDALKLDFSDPDAFRRPI------SEVMSS----PVLTIPQDTTL 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 71998166 371 WSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVI 404
Cdd:cd09833  81 GEAAVRFRQEGVRHLLVVDDDGRPVGIVSQTDVV 114
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 358-423 3.57e-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: 3.57e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71998166 358 RDGVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFLVLRPTKKNGVTTGEPM 423
Cdd:COG2905   6 SRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVM 71
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
283-407 3.69e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.58  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNtLKVLEVYTRFDAASAAFSDHIDlsvsvtrAIQERDyqngirrdgVV 362
Cdd:COG4109  25 EDVATLSEDDTVEDALELLEKTGHSRFPVVDEN-GRLVGIVTSKDILGKDDDTPIE-------DVMTKN---------PI 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71998166 363 TANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:COG4109  88 TVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
208-257 5.21e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 37.94  E-value: 5.21e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71998166 208 KPFINIGLKESIFRAVELLTKYRIHRLPVMDEKtGDCAYILTHRRILHYI 257
Cdd:COG2524 158 RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDD-GKLVGIITRTDILRAL 206
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 283-407 5.35e-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: 37.21  E-value: 5.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166 283 KNLIFANEQTPLIECLDMLIDNNISGIPIVQKNTLKVLEVYTRFDAAS--------------------AAFSDHIdlsvs 342
Cdd:cd17779   8 KDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDflgggskynlvekkhngnllAAINEPV----- 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71998166 343 vtRAIQERDyqngirrdgVVTANYTTTLWSLIEIFIDKNVHRIFMVDDRTILKGIISLSDVIEFL 407
Cdd:cd17779  83 --REIMTRD---------VISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 296-403 5.66e-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: 38.91  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998166   296 ECLDMLIDNNISGIPIVQKNTLkvLEVYTRFDAAsaaFSDHIDLSVS--VTRaiqerdyqngirrDGVVTANYTTTLWSL 373
Cdd:pfam00478 101 DALALMERYGISGVPVVDDGKL--VGIVTNRDLR---FETDLSQPVSevMTK-------------ENLVTAPEGTTLEEA 162

                          90       100       110
                  ....*....|....*....|....*....|
gi 71998166   374 IEIFIDKNVHRIFMVDDRTILKGIISLSDV 403
Cdd:pfam00478 163 KEILHKHKIEKLPVVDDNGRLVGLITIKDI 192
 
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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