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Conserved domains on  [gi|1845974882|ref|NP_001370107|]
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CBS domain-containing protein [Caenorhabditis elegans]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 215-355 2.25e-74

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: 233.22  E-value: 2.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 215 KCYDLIPTSSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDTDNQRFTGMLTITDFIKILCKHYDKGdnSERIRALEDQQI 294
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSP--SVQMEELEEHTI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 295 SHWRDQFELDGTlRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMK 355
Cdd:cd04618    79 ETWREIERQIGV-PPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 382-504 1.57e-69

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: 220.08  E-value: 1.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 382 WGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRSEWFEGVQTCL 461
Cdd:cd04641     2 YENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTCT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 462 ETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:cd04641    82 LNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 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 ...
 215-355 2.25e-74

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: 233.22  E-value: 2.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 215 KCYDLIPTSSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDTDNQRFTGMLTITDFIKILCKHYDKGdnSERIRALEDQQI 294
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSP--SVQMEELEEHTI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 295 SHWRDQFELDGTlRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMK 355
Cdd:cd04618    79 ETWREIERQIGV-PPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 382-504 1.57e-69

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: 220.08  E-value: 1.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 382 WGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRSEWFEGVQTCL 461
Cdd:cd04641     2 YENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTCT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 462 ETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:cd04641    82 LNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS COG0517
CBS domain [Signal transduction mechanisms];
384-504 2.72e-20

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 86.84  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHrsewfeGVQTCLET 463
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974882 464 DSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
308-434 3.57e-17

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 78.37  E-value: 3.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLS------LYMRDLPRP--SFMSctprelgi 379
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLpdrldeLEERLLDLPveDVMT-------- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1845974882 380 gawGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAES 434
Cdd:COG3448    81 ---RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARL 132
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 457-503 1.97e-09

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 53.29  E-value: 1.97e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1845974882  457 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNL 503
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 457-504 2.15e-08

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 50.67  E-value: 2.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1845974882 457 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 308-358 6.52e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 46.44  E-value: 6.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLS 358
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRALL 56
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 226-273 4.04e-06

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 44.04  E-value: 4.04e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1845974882  226 LVVFDTHLPVRKAFYALVYNGVRAAPLWDtDNQRFTGMLTITDFIKIL 273
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVD-EEGRLVGIVTRRDIIKAL 48
 
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 ...
 215-355 2.25e-74

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: 233.22  E-value: 2.25e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 215 KCYDLIPTSSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDTDNQRFTGMLTITDFIKILCKHYDKGdnSERIRALEDQQI 294
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSP--SVQMEELEEHTI 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 295 SHWRDQFELDGTlRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMK 355
Cdd:cd04618    79 ETWREIERQIGV-PPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 382-504 1.57e-69

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: 220.08  E-value: 1.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 382 WGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRSEWFEGVQTCL 461
Cdd:cd04641     2 YENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTCT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 462 ETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:cd04641    82 LNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS COG0517
CBS domain [Signal transduction mechanisms];
384-504 2.72e-20

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 86.84  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHrsewfeGVQTCLET 463
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974882 464 DSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:COG0517    84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
384-504 1.15e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 85.30  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVV------DIYAKFDVISLAaESSYDKLDCTVQEALQHRsewfegV 457
Cdd:COG3448    11 DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVgivterDLLRALLPDRLD-ELEERLLDLPVEDVMTRP------V 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1845974882 458 QTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:COG3448    84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 384-501 1.65e-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: 78.44  E-value: 1.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAEsSYDKLDCTVQEALQhrsewfEGVQTCLET 463
Cdd:cd02205     3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE-GGLALDTPVAEVMT------PDVITVSPD 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1845974882 464 DSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:cd02205    76 TDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 384-503 2.20e-17

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 78.33  E-value: 2.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRsewfegVQTCLET 463
Cdd:COG2905     8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRP------PITVSPD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1845974882 464 DSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 503
Cdd:COG2905    82 DSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRAL 120
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
384-501 2.97e-17

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 80.70  E-value: 2.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDeNGRVVDIYAKFDVISlAAESSYDKLDCTVQEALQhrsewfEGVQTCLET 463
Cdd:COG2524    95 DVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLK-ALAEGRDLLDAPVSDIMT------RDVVTVSED 166

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1845974882 464 DSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:COG2524   167 DSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
308-434 3.57e-17

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 78.37  E-value: 3.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLS------LYMRDLPRP--SFMSctprelgi 379
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDED-GRLVGIVTERDLLRALLpdrldeLEERLLDLPveDVMT-------- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1845974882 380 gawGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAES 434
Cdd:COG3448    81 ---RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARL 132
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 389-501 1.32e-14

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 70.16  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 389 HVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLD-CTVQEALQHrsewfeGVQTCLETDSLF 467
Cdd:cd04629     9 TPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPgGTVADYMST------EVLTVSPDTSIV 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1845974882 468 QVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 501
Cdd:cd04629    83 DLAQLFLKNKPRRYPVVE-DGKLVGQISRRDVLR 115
CBS COG0517
CBS domain [Signal transduction mechanisms];
308-433 1.77e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 70.28  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLSLYMRDLP-RP--SFMSctprelgigawGD 384
Cdd:COG0517     9 TDVVTVSPDATVREALELMSEKRIGGLPVVD-EDGKLVGIVTDRDLRRALAAEGKDLLdTPvsEVMT-----------RP 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1845974882 385 ILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAE 433
Cdd:COG0517    77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 384-501 2.04e-14

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 70.15  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVV------DIYAKFDVISLA---------------AESSYDK-LDC 441
Cdd:cd04586     4 DVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVgivsegDLLRREEPGTEPrrvwwldallesperLAEEYVKaHGR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 442 TVQEALQHRsewfegVQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 501
Cdd:cd04586    84 TVGDVMTRP------VVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLLR 136
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
308-419 4.95e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 71.07  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMKFLSLYMRDLPRP--SFMSctprelgigawGDI 385
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVDD--GKLVGIITERDLLKALAEGRDLLDAPvsDIMT-----------RDV 160

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1845974882 386 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVV 419
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLV 194
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 308-428 4.50e-13

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 65.73  E-value: 4.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLSLYMRDLPRP--SFMSctprelgigawGDI 385
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDD-GKLVGIVTERDILRALVEGGLALDTPvaEVMT-----------PDV 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 386 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 428
Cdd:cd02205    70 ITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 384-499 3.15e-12

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: 63.21  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPlIDENGRVV------DIyakfdVISLAAESSyDKLDCTVQEALQHrsewfeGV 457
Cdd:cd04622     4 DVVTVSPDTTLREAARLMRDLDIGALP-VCEGDRLVgmvtdrDI-----VVRAVAEGK-DPNTTTVREVMTG------DV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1845974882 458 QTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDI 499
Cdd:cd04622    71 VTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 383-501 4.23e-12

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


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 64.03  E-value: 4.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 383 GDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQhrsEW--FEGVQTC 460
Cdd:cd17789     3 GKLHVVKPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADS---TWktFNEVQKL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 461 L--------------------ETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:cd17789    80 LsktngkvvgdvmtpsplvvrEKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVVR 140
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 308-421 1.88e-11

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 61.67  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKT--GnityILTHKRIMKFLSlymrdlprPSFMSCTPRELGIGAWG-- 383
Cdd:cd04584     8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKlvG----IVTDRDLLRASP--------SKATSLSIYELNYLLSKip 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1845974882 384 -------DILCCHVDTPIHDALELFLKNRVSALPLIDeNGRVVDI 421
Cdd:cd04584    76 vkdimtkDVITVSPDDTVEEAALLMLENKIGCLPVVD-GGKLVGI 119
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
162-357 5.70e-11

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 62.21  E-value: 5.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 162 ANSMSSLRVSPGAIGPSGVVKAPLSDPNFDFYTWHTSEADNHDAVYSLFMKAHkcyDLIptSSKLVVFDTHLPVRKAFYA 241
Cdd:COG2524    37 AAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVK---DIM--TKDVITVSPDTTLEEALEL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 242 LVYNGVRAAPLwdTDNQRFTGMLTITDFIKILckhydkgdnsERIRALEDQQISHwrdqfeldgtL--RPFVYIDPNESL 319
Cdd:COG2524   112 MLEKGISGLPV--VDDGKLVGIITERDLLKAL----------AEGRDLLDAPVSD----------ImtRDVVTVSEDDSL 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1845974882 320 HRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL 357
Cdd:COG2524   170 EEALRLMLEHGIGRLPVVDDD-GKLVGIITRTDILRAL 206
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 385-501 2.67e-10

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: 57.92  E-value: 2.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 385 ILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAEssyDKLDCTVQEALQhrsewFEGVQTCLETD 464
Cdd:cd09836     5 VVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAE---GIDLDTPVEEIM-----TKNLVTVSPDE 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1845974882 465 SLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:cd09836    77 SIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
223-357 4.92e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 57.57  E-value: 4.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 223 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDtDNQRFTGMLTITDFIKILckhyDKGDNSERIRALEDQQIShwrdqfe 302
Cdd:COG3448     9 TRDVVTVSPDTTLREALELMREHGIRGLPVVD-EDGRLVGIVTERDLLRAL----LPDRLDELEERLLDLPVE------- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1845974882 303 lDGTLRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL 357
Cdd:COG3448    77 -DVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDD-GRLVGIVTRTDLLRAL 129
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 457-503 1.97e-09

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 53.29  E-value: 1.97e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1845974882  457 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNL 503
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 385-502 5.24e-09

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: 54.15  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 385 ILCCHVDTPIHDALELFLKNRVSALpLIDENGRVVDIYAKFDVISLAaESSYDKLDCTVQEALQHRsewfegVQTcleTD 464
Cdd:cd09833     7 LLTCSPDTPLADAAARMAERRCSSI-LIVENGEIVGIWTERDALKLD-FSDPDAFRRPISEVMSSP------VLT---IP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974882 465 SLFQVLEAIVK---AEVHRLIVTDQDKKVVGVVSLSDILKN 502
Cdd:cd09833    76 QDTTLGEAAVRfrqEGVRHLLVVDDDGRPVGIVSQTDVVLN 116
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 384-432 5.51e-09

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: 52.13  E-value: 5.51e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1845974882  384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAA 432
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 391-501 7.74e-09

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 53.69  E-value: 7.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 391 DTPIHDALELFLKNRVSALPLIDeNGRVVDIYAKFDVISLAAEssyDKLDCTVQEALQHRsewfegVQTCLETDSLFQVL 470
Cdd:cd04588    10 DATIKDAAKLLSENNIHGAPVVD-DGKLVGIVTLTDIAKALAE---GKENAKVKDIMTKD------VITIDKDEKIYDAI 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1845974882 471 EAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:cd04588    80 RLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
389-503 8.86e-09

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 54.15  E-value: 8.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 389 HVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVIslaaessyDKLDCTVQEALQHRSewfegVQTCLETDSLFQ 468
Cdd:COG4109    31 SEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL--------GKDDDTPIEDVMTKN-----PITVTPDTSLAS 97

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1845974882 469 VLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNL 503
Cdd:COG4109    98 AAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 457-504 2.15e-08

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 50.67  E-value: 2.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1845974882 457 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 383-501 5.26e-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: 51.26  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 383 GDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRsewfegVQTCLE 462
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRD------VVTCTP 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1845974882 463 TDSLFQVLEAIVKaevHR---LIVTDqDKKVVGVVSLSDILK 501
Cdd:cd04623    76 DDTVEECMALMTE---RRirhLPVVE-DGKLVGIVSIGDVVK 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 384-433 6.45e-08

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 49.13  E-value: 6.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAE 433
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 384-498 1.41e-07

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 50.64  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLDCTVQEALQHRSEWFEG------- 456
Cdd:cd04600     4 DVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRDRPETvgdimtr 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 457 -VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSD 498
Cdd:cd04600    84 pVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSD 126
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
457-506 3.55e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 49.48  E-value: 3.55e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1845974882 457 VQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLVLD 506
Cdd:COG3448    12 VVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPD 61
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 308-430 6.43e-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: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMKFLSLYMRDLPRPSFMSctprelgigawGDILC 387
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD--GKLVGIVTLTDIAKALAEGKENAKVKDIMT-----------KDVIT 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 388 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISL 430
Cdd:cd04588    69 IDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 308-358 6.52e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 46.44  E-value: 6.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLS 358
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDED-GKLVGIVTLKDLLRALL 56
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 384-501 8.55e-07

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 47.92  E-value: 8.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFD-VISLAAESSyDKLDCTVQEALQhrsewfEGVQTCLE 462
Cdd:cd17775     4 EVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDiVVEVVAKGL-DPKDVTVGDIMS------ADLITARE 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1845974882 463 TDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:cd17775    77 DDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILE 115
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 311-428 9.36e-07

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


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 48.38  E-value: 9.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 311 VYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKFL-----SLYMRDLPRPSFMSCTPRELGIGAWGDI 385
Cdd:cd17779    11 ITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskYNLVEKKHNGNLLAAINEPVREIMTRDV 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 386 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 428
Cdd:cd17779    91 ISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 396-503 1.73e-06

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


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 47.03  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 396 DALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYdKLDCTVQEALQhrsewfEGVQTCLETDSLfqvLEAIVK 475
Cdd:cd17784    15 EAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKY-ELGTTVEEVMV------KDVATVHPDETL---LEAIKK 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1845974882 476 AE--------VHRLIVTDqDKKVVGVVSLSDILKNL 503
Cdd:cd17784    85 MDsnapdeeiINQLPVVD-DGKLVGIISDGDIIRAI 119
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 308-419 2.99e-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: 46.28  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFL--SLYMRDLPRP--SFMSctprelgigawG 383
Cdd:cd04629     3 RNPVTLTPDTSILEAVELLLEHKISGAPVVD-EQGRLVGFLSEQDCLKALleASYHCEPGGTvaDYMS-----------T 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIdENGRVV 419
Cdd:cd04629    71 EVLTVSPDTSIVDLAQLFLKNKPRRYPVV-EDGKLV 105
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 223-358 3.16e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 46.36  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 223 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDtDNQRFTGMLTITDfikILCKHYDKGDNSERIRAledQQISHwrdqfe 302
Cdd:COG2905     6 SRDVVTVSPDATVREAARLMTEKGVGSLVVVD-DDGRLVGIITDRD---LRRRVLAEGLDPLDTPV---SEVMT------ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974882 303 ldgtlRPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMKFLS 358
Cdd:COG2905    73 -----RPPITVSPDDSLAEALELMEEHRIRHLPVVDD--GKLVGIVSITDLLRALS 121
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 391-501 3.82e-06

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 46.56  E-value: 3.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 391 DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLA---------AESSYDK---LDCTVqealqhRSEWFEGVQ 458
Cdd:cd04632    10 DDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVvrpgtktrgGDRGGEKermLDLPV------YDIMSSPVV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 459 TCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:cd04632    84 TVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 226-273 4.04e-06

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 44.04  E-value: 4.04e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1845974882  226 LVVFDTHLPVRKAFYALVYNGVRAAPLWDtDNQRFTGMLTITDFIKIL 273
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVD-EEGRLVGIVTRRDIIKAL 48
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 308-421 5.82e-06

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: 45.69  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLSLYMRDLPRpsFMSCtprelgigawgDILC 387
Cdd:cd04605     8 KDVATIREDISIEEAAKIMIDKNVTHLPVVS-EDGKLIGIVTSWDISKAVALKKDSLEE--IMTR-----------NVIT 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1845974882 388 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDI 421
Cdd:cd04605    74 ARPDEPIELAARKMEKHNISALPVVDDDRRVIGI 107
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 304-419 6.18e-06

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


Pssm-ID: 341421 [Multi-domain]  Cd Length: 136  Bit Score: 46.11  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 304 DGTLRPFVyIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKflSLYMRDLPRPS--FMSCTPRELGIGA 381
Cdd:cd17785     7 LITKKPSV-VHENTSIRDVIDKMIEDPKTRSVYVVDDDEKLLGIITLMELLK--YIGYRFGVTIYkgVSFGLLLRISLKE 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 382 -WGDIL----CCHVDTPIHDALELFLKNRVSALPLIDENGRVV 419
Cdd:cd17785    84 kAKDIMlspiYVKKEDTLEEALELMVKNRLQELPVVDENGKVI 126
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 311-421 1.86e-05

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 43.94  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 311 VYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILThKRIMKFLSlyMRDLPRPSFMscTPRELGIGAwgdilccHV 390
Cdd:cd04601     5 VTLSPDATVADVLELKAEYGISGVPVTEDG-GKLVGIVT-SRDIRFET--DLSTPVSEVM--TPDERLVTA-------PE 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1845974882 391 DTPIHDALELFLKNRVSALPLIDENGRVVDI 421
Cdd:cd04601    72 GITLEEAKEILHKHKIEKLPIVDDNGELVGL 102
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 309-357 2.34e-05

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 41.73  E-value: 2.34e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1845974882  309 PFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL 357
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEE-GRLVGIVTRRDIIKAL 48
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 308-428 2.76e-05

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 43.86  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDrkTGNITYILTHKRIMKFLSlYMRDLPRPS------FMSCTPRELgigA 381
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFG-SHEAKKRLTtgdideAYSTPVEEI---M 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1845974882 382 WGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 428
Cdd:cd17778    82 SKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 388-500 3.53e-05

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


Pssm-ID: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 43.46  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 388 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDkLDCTVQEALQHRSEWFEgvqtclETDSLF 467
Cdd:cd17771     9 CSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQID-LDAPISEVMTPDPVRLP------PSASAF 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845974882 468 QVLEAIVKAEVHRLIVTDQDkKVVGVVSLSDIL 500
Cdd:cd17771    82 EAALLMAEHGFRHVCVVDNG-RLVGVVSERDLF 113
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 308-419 4.38e-05

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: 42.94  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKFLSLYMRDLPRPSFMSCTPRELGigawgdilc 387
Cdd:cd17772     2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIYHGLGDLPVSEYMTTEFATVT--------- 72

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1845974882 388 chVDTPIHDALELFLKNRVSALPLIdENGRVV 419
Cdd:cd17772    73 --PDAPLSEIQEIIVEQRQRLVPVV-EDGRLV 101
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 455-506 4.55e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 43.28  E-value: 4.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1845974882 455 EGVQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLVLD 506
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAE 58
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
306-428 4.55e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 43.36  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 306 TLRPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKflslYMRDLPRPSFMSctprelgigawGDI 385
Cdd:COG4109    23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDEN-GRLVGIVTSKDILG----KDDDTPIEDVMT-----------KNP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 386 LCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 428
Cdd:COG4109    87 ITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 459-504 4.77e-05

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: 43.00  E-value: 4.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1845974882 459 TCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:cd02205     6 TVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 389-499 5.20e-05

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


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 43.00  E-value: 5.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 389 HVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDvISLAAESSYDKLdctvqEALQHRSewfegVQTCLETDSLFQ 468
Cdd:cd04605    14 REDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWD-ISKAVALKKDSL-----EEIMTRN-----VITARPDEPIEL 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1845974882 469 VLEAIVKAEVHRLIVTDQDKKVVGVVSLSDI 499
Cdd:cd04605    83 AARKMEKHNISALPVVDDDRRVIGIITSDDI 113
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 223-354 6.26e-05

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 43.09  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 223 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLwdTDNQRFTGMLTITDFIKILCKHYDKGDNSERiraledqQISHWRDQFE 302
Cdd:cd17778     7 TTPVVTIYPDDTLKEAMELMVTRGFRRLPV--VSGGKLVGIVTAMDIVKYFGSHEAKKRLTTG-------DIDEAYSTPV 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1845974882 303 LDGTLRPFVYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIM 354
Cdd:cd17778    78 EEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVD-DEGELKGIITERDVL 128
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 388-501 6.69e-05

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 42.48  E-value: 6.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 388 CHVDTPIHDALELFLKNRVSALPLIdENGRVVDIYAKFDVislaaessyDKldcTVQEALQH---RSEWFEGVQTCLETD 464
Cdd:cd04595     7 VSPDTTIEEARKIMLRYGHTGLPVV-EDGKLVGIISRRDV---------DK---AKHHGLGHapvKGYMSTNVITIDPDT 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1845974882 465 SLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 501
Cdd:cd04595    74 SLEEAQELMVEHDIGRLPVVE-EGKLVGIVTRSDVLR 109
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 373-500 6.72e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 42.48  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 373 TPRElgigawgDILCCHVDTPIHDALELFLKNRVSALPLIDEN-GRVVDI-YAKfDVISLAAEssyDKLDCTVQEALqhR 450
Cdd:cd04590     7 TPRT-------DVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVlHVK-DLLAALLE---GREKLDLRALL--R 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1845974882 451 SEWFegVQtclETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDIL 500
Cdd:cd04590    74 PPLF--VP---ETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 311-431 7.54e-05

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: 42.41  E-value: 7.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 311 VYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHkrimkflslymRDL----------PRpsfmSCTPRELgig 380
Cdd:cd04622     6 VTVSPDTTLREAARLMRDLDIGALPVCEG--DRLVGMVTD-----------RDIvvravaegkdPN----TTTVREV--- 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 381 AWGDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIyakfdvISLA 431
Cdd:cd04622    66 MTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGI------VSLG 110
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
 384-502 9.94e-05

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


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 42.01  E-value: 9.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDEnGRVVDIYAKFDVisLAAESSYDKL--DCTVQEALQHRSEWFEGVQTcl 461
Cdd:cd17776     4 DVVTVDADASLEDAAERMLRNRVGSVVVTDD-GTPAGILTETDA--LHAGYATDDPfsEIPVRAVASRPLVTISPTAT-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974882 462 etdsLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKN 502
Cdd:cd17776    79 ----LREAAERMVDEGVKKLPVVD-GLDLVGILTATDIIRA 114
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 389-501 1.03e-04

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


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 41.79  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 389 HVDTPIHDALELFLKNRVSALPLIdENGRVVDIYAKFDVISLAAEssyDKLDCTVQEALQhrsewfEGVQTCLETDSLFQ 468
Cdd:cd04801    11 TPEMTVSELLDRMFEEKHLGYPVV-ENGRLVGIVTLEDIRKVPEV---EREATRVRDVMT------KDVITVSPDADAME 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845974882 469 VLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILK 501
Cdd:cd04801    81 ALKLMSQNNIGRLPVVE-DGELVGIISRTDLMR 112
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 374-503 1.38e-04

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: 41.94  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 374 PRELGIGAWGDILCCHVDTPIHDALELFLKNRVSALPLIDENgRVVDIYAKFDVISLAAESSYDKL--DCT---VQEALq 448
Cdd:cd17777     1 EKELMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDEN-KLEGILSARDLVSYLGGGCLFKIveSRHqgdLYSAL- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 449 hRSEWFEGVQT-----CLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNL 503
Cdd:cd17777    79 -NREVVETIMTpnpvyVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL 137
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 384-421 2.74e-04

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


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 40.65  E-value: 2.74e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDI 421
Cdd:cd17781    69 NPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGV 106
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 311-419 2.94e-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: 43.53  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 311 VYIDPNESLHRAVELLCESKVHRLPVLDRKT--GnityILThKRIMKFLSLYmrDLPRPSFMscTPRELgIGAwgdilcc 388
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVDDGKlvG----IVT-NRDLRFETDL--SQPVSEVM--TKENL-VTA------- 153

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1845974882 389 HVDTPIHDALELFLKNRVSALPLIDENGRVV 419
Cdd:pfam00478 154 PEGTTLEEAKEILHKHKIEKLPVVDDNGRLV 184
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
427-500 3.01e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.05  E-value: 3.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1845974882 427 VISlaaeSSYD--KLDCTVQEALQHRSewfegVQTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDIL 500
Cdd:COG4109     4 IIS----TSYDtfKEILLVEDIMTLED-----VATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL 70
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 308-421 5.66e-04

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


Pssm-ID: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 39.71  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFLSLYMRD-LPRP--SFMSCtprelgigawgD 384
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDG-GRLVGILSERDYVRKLALRGASsLDTPvsEIMTR-----------D 69

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1845974882 385 ILCCHVDTPIHDALELFLKNRVSALPLIDeNGRVVDI 421
Cdd:cd04623    70 VVTCTPDDTVEECMALMTERRIRHLPVVE-DGKLVGI 105
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 311-429 5.79e-04

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 40.01  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 311 VYIDPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLSLYMRDLPRPSFMSCTPRELGIGAWgDILCCHV 390
Cdd:cd04632     5 ITVNEDDTIGKAINLLREHGISRLPVVD-DNGKLVGIVTTYDIVDFVVRPGTKTRGGDRGGEKERMLDLPVY-DIMSSPV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1845974882 391 -----DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVIS 429
Cdd:cd04632    83 vtvtrDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
457-503 8.05e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 41.02  E-value: 8.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1845974882 457 VQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 503
Cdd:COG2524    96 VITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKAL 141
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 311-354 1.37e-03

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 38.48  E-value: 1.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1845974882 311 VYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIM 354
Cdd:cd04599    64 VTISPEASLWEAKELMEEHGIERLVVVEE--GRLVGIITKSTLY 105
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 465-505 1.44e-03

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


Pssm-ID: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 39.08  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1845974882 465 SLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLVL 505
Cdd:cd04640    15 SADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPL 55
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 311-419 1.55e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 38.63  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 311 VYIDPNESLHRAVELLCESKVHRLPVLDRKTGNITYILTHKRIMKFLSLYMRDLPRPSFMsctpRElgigawgdILCCHV 390
Cdd:cd04590    13 VALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAALLEGREKLDLRALL----RP--------PLFVPE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1845974882 391 DTPIHDALELFLKNRVS-ALpLIDENGRVV 419
Cdd:cd04590    81 TTPLDDLLEEFRKERSHmAI-VVDEYGGTA 109
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 308-429 1.76e-03

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


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 38.33  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRKtGNITYILTHKRIMKFL-------SLYMRDLPRPSFMSCTPrelgig 380
Cdd:cd04613     3 RKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQ-GRLTGILSIQDVRGVLfeeelwdLVVVKDLATTDVITVTP------ 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 381 awgdilcchvDTPIHDALELFLKNRVSALPLIDEN--GRVVDIYAKFDVIS 429
Cdd:cd04613    76 ----------DDDLYTALLKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVIA 116
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 389-421 2.01e-03

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


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 38.19  E-value: 2.01e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1845974882 389 HVDTPIHDALELFLKNRVSALPLIDENGRVVDI 421
Cdd:cd04607    72 SPSTSREELLALMRAKKILQLPIVDEQGRVVGL 104
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 223-273 2.30e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.42  E-value: 2.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 223 SSKLVVFDTHLPVRKAFYALVYNGVRAAPLWDTDNqRFTGMLTITDFIKIL 273
Cdd:pfam00571   6 TKDVVTVSPDTTLEEALELMREHGISRLPVVDEDG-KLVGIVTLKDLLRAL 55
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 234-358 3.12e-03

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: 37.89  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 234 PVRKAFYALVYNGVRAAPLWDTDNqRFTGMLTITDFIKILCkhyDKGDNSERIRaledqqishwrdqfelDGTLRPFVYI 313
Cdd:cd09836    13 TIREAAKLMAENNIGSVVVVDDDG-KPVGIVTERDIVRAVA---EGIDLDTPVE----------------EIMTKNLVTV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1845974882 314 DPNESLHRAVELLCESKVHRLPVLDrKTGNITYILTHKRIMKFLS 358
Cdd:cd09836    73 SPDESIYEAAELMREHNIRHLPVVD-GGGKLVGVISIRDLARELS 116
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 383-501 4.09e-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: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 383 GDILCCHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVIS--LAAESsydKLDCTVQEALQHRsewFE--GVQ 458
Cdd:cd04608    10 GAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSslLAGRA---QPSDPVSKAMYKQ---FKqvDLD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1845974882 459 TCLETdsLFQVLEaivkaEVHRLIVTDQDKKVVGVVSLSDILK 501
Cdd:cd04608    84 TPLGA--LSRILE-----RDHFALVVDGQGKVLGIVTRIDLLN 119
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 308-428 4.24e-03

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 37.30  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRktGNITYILTHKRIMkflsLYMRDLPRPSFMSctprelgigawGDILC 387
Cdd:cd04610     3 RDVITVSPDDTVKDVIKLIKETGHDGFPVVDD--GKVVGYVTAKDLL----GKDDDEKVSEIMS-----------RDTVV 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1845974882 388 CHVDTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 428
Cdd:cd04610    66 ADPDMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 391-500 4.25e-03

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


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 37.56  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 391 DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVISLAAESSYDKLdCTVQEALQhrsewfEGVQTCLETDSLFQVL 470
Cdd:cd04613    11 GMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEELWDL-VVVKDLAT------TDVITVTPDDDLYTAL 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1845974882 471 EAIVKAEVHRLIVTDQD--KKVVGVVSLSDIL 500
Cdd:cd04613    84 LKFTSTNLDQLPVVDDDdpGKVLGMLSRRDVI 115
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 308-428 4.64e-03

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 37.54  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 308 RPFVYIDPNESLHRAVELLCESKVHRLPVLDRK---TGNITYI--LTHKRIMKFLSLYMRDLPRPSFMSCTPRELGigaw 382
Cdd:cd04600     3 RDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRArrlVGIVTLAdlLKHADLDPPRGLRGRLRRTLGLRRDRPETVG---- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1845974882 383 gDILCCHV-----DTPIHDALELFLKNRVSALPLIDENGRVVDIYAKFDVI 428
Cdd:cd04600    79 -DIMTRPVvtvrpDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 457-503 4.69e-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: 37.40  E-value: 4.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1845974882 457 VQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 503
Cdd:cd04584    10 VVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRAS 55
TlyC COG1253
Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction ...
 373-504 5.51e-03

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


Pssm-ID: 440865 [Multi-domain]  Cd Length: 435  Bit Score: 39.33  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 373 TPRElgigawgDILCCHVDTPIHDALELFLKNRVSALPLIDENgrvVD-----IYAKfDVISLAAESSYDKLDCTVQEAL 447
Cdd:COG1253   221 TPRT-------DVVALDLDDTLEEALELILESGHSRIPVYEGD---LDdivgvVHVK-DLLRALLEGEPFDLRDLLRPPL 289

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1845974882 448 qhrsewfegvqTCLETDSLFQVLEAIVKAEVHRLIVTDQDKKVVGVVSLSDILKNLV 504
Cdd:COG1253   290 -----------FVPETKPLDDLLEEFRRERVHMAIVVDEYGGTAGLVTLEDILEEIV 335
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 455-503 5.92e-03

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 37.31  E-value: 5.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1845974882 455 EGVQTCLETDSLFQVLEAIVKAEVHRLIVTDqDKKVVGVVSLSDILKNL 503
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVKYF 55
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 309-416 5.99e-03

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


Pssm-ID: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 37.35  E-value: 5.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845974882 309 PFVYIDPNESLHRAVELLCESKVHRLPVLDrkTGNITY-ILTHKRIMKFLSLYMRDLPRP--SFMS--CTpreLGIGAWG 383
Cdd:cd04592     4 RYITVLMSTTLKEAVLLMLEEKQSCALIVD--SDDFLIgILTLGDIQRFLKRAKADNEDPktILVSsiCT---RNGGYCR 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1845974882 384 DILCCHVDTPIHDALELFLKNRVSALPLIDENG 416
Cdd:cd04592    79 GLWTCTPDMDLLTAKMLMEARGINQLPVVKRGG 111
 
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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