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Conserved domains on  [gi|33186925|ref|NP_057287|]
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5'-AMP-activated protein kinase subunit gamma-2 isoform a [Homo sapiens]

Protein Classification

CBS_pair_5 and CBS_pair_28 domain-containing protein( domain architecture ID 10140186)

CBS_pair_5 and CBS_pair_28 domain-containing protein

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 ...
269-406 1.73e-87

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


:

Pssm-ID: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 266.73  E-value: 1.73e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 269 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 348
Cdd:cd04618   1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33186925 349 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILK 406
Cdd:cd04618  81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
432-555 4.21e-76

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: 236.64  E-value: 4.21e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 432 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 511
Cdd:cd04641   1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 512 NKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:cd04641  81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
46-221 1.60e-06

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925    46 PLLDGDLEGSGKHSSRKVDSPFGPGSPSKGFFSRGPQPR-PSSPMSAPVRPKTSPGSPKTVFPFSYQES--PPRSPRRMS 122
Cdd:PHA03307  132 PDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRqAALPLSSPEETARAPSSPPAEPPPSTPPAaaSPRPPRRSS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925   123 FSGIfrssskessPNSNPATSPGGIRFFSRSRKTSGLSSSPSTPTQVTKQHTFPLESykHEPERLENRIYASSSPPDTGQ 202
Cdd:PHA03307  212 PISA---------SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPR--PAPITLPTRIWEASGWNGPSS 280
                         170
                  ....*....|....*....
gi 33186925   203 RFCPSSFQSPTRPPLASPT 221
Cdd:PHA03307  281 RPGPASSSSSPRERSPSPS 299
 
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 ...
269-406 1.73e-87

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


Pssm-ID: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 266.73  E-value: 1.73e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 269 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 348
Cdd:cd04618   1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33186925 349 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILK 406
Cdd:cd04618  81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
432-555 4.21e-76

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: 236.64  E-value: 4.21e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 432 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 511
Cdd:cd04641   1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 512 NKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:cd04641  81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS COG0517
CBS domain [Signal transduction mechanisms];
435-555 6.84e-21

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 88.38  E-value: 6.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHrsqyfeGVVKCNKL 514
Cdd:COG0517  10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 33186925 515 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:COG0517  84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
359-484 1.87e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 84.53  E-value: 1.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILTHKRILKFLQLFMSDMPKPAFMKQNLDELgigTYHNIA 437
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVD--EDGRLVgIVTERDLLRALLPDRLDELEERLLDLPVEDV---MTRPVV 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 33186925 438 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 484
Cdd:COG3448  85 TVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
439-483 4.92e-11

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: 57.91  E-value: 4.92e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 33186925    439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAA 483
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
434-484 6.97e-10

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: 54.91  E-value: 6.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 33186925   434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 484
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
360-409 5.33e-08

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: 49.43  E-value: 5.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 33186925    360 PLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQ 409
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDE-EGRLVGIVTRRDIIKALA 49
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
46-221 1.60e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925    46 PLLDGDLEGSGKHSSRKVDSPFGPGSPSKGFFSRGPQPR-PSSPMSAPVRPKTSPGSPKTVFPFSYQES--PPRSPRRMS 122
Cdd:PHA03307  132 PDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRqAALPLSSPEETARAPSSPPAEPPPSTPPAaaSPRPPRRSS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925   123 FSGIfrssskessPNSNPATSPGGIRFFSRSRKTSGLSSSPSTPTQVTKQHTFPLESykHEPERLENRIYASSSPPDTGQ 202
Cdd:PHA03307  212 PISA---------SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPR--PAPITLPTRIWEASGWNGPSS 280
                         170
                  ....*....|....*....
gi 33186925   203 RFCPSSFQSPTRPPLASPT 221
Cdd:PHA03307  281 RPGPASSSSSPRERSPSPS 299
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
359-408 3.18e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.51  E-value: 3.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 33186925   359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 408
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRAL 55
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
435-550 1.51e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.36  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925  435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDvinLAaeKTYnnLDITVTQALQHRSQYFEGVVKCNKL 514
Cdd:PRK14869  77 KPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSD---LA--RAY--MDILDPEILSKSPTSLENIIRTLDG 149
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 33186925  515 EILeTIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 550
Cdd:PRK14869 150 EVL-VGAEEDKVEEGKVVVAAMAPESLLERIEEGDI 184
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
269-406 1.73e-87

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


Pssm-ID: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 266.73  E-value: 1.73e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 269 KCYDIVPTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQSFVGMLTITDFINILHRYYKSPMVQIYELEEHKIET 348
Cdd:cd04618   1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPSVQMEELEEHTIET 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 33186925 349 WRELYLQETFKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILK 406
Cdd:cd04618  81 WREIERQIGVPPLVSVHPEDSLYDAALLLLQNKIHRLPVIDPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
432-555 4.21e-76

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: 236.64  E-value: 4.21e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 432 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKC 511
Cdd:cd04641   1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNNLDLTVGEALQHRSEDFEGVHTC 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 512 NKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:cd04641  81 TLNDTLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
434-552 5.42e-21

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: 88.46  E-value: 5.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQALQhrsqyfEGVVKCNK 513
Cdd:cd02205   2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG-GLALDTPVAEVMT------PDVITVSP 74
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 33186925 514 LEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQ 552
Cdd:cd02205  75 DTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
435-555 6.84e-21

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 88.38  E-value: 6.84e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHrsqyfeGVVKCNKL 514
Cdd:COG0517  10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTR------PPVTVSPD 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 33186925 515 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:COG0517  84 TSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
434-555 3.13e-20

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 86.84  E-value: 3.13e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNL-----DITVTQALQHRsqyfegV 508
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELeerllDLPVEDVMTRP------V 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 33186925 509 VKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:COG3448  84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
359-484 1.87e-19

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 84.53  E-value: 1.87e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILTHKRILKFLQLFMSDMPKPAFMKQNLDELgigTYHNIA 437
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVD--EDGRLVgIVTERDLLRALLPDRLDELEERLLDLPVEDV---MTRPVV 84
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 33186925 438 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 484
Cdd:COG3448  85 TVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
434-554 2.16e-17

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 81.08  E-value: 2.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEKTYNnLDITVTQALQhrsqyfEGVVKCNK 513
Cdd:COG2524  94 KDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDL-LDAPVSDIMT------RDVVTVSE 165
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 33186925 514 LEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 554
Cdd:COG2524 166 DDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
434-555 2.83e-16

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 75.25  E-value: 2.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRsqyfegVVKCNK 513
Cdd:COG2905   7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRP------PITVSP 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33186925 514 LEILETIVDRIVRAEVHRLVVVnEADSIVGIISLSDILQALI 555
Cdd:COG2905  81 DDSLAEALELMEEHRIRHLPVV-DDGKLVGIVSITDLLRALS 121
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
359-480 4.10e-16

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 77.23  E-value: 4.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPA--FMKQNLdelgigtyhni 436
Cdd:COG2524  94 KDVITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDLLDAPVsdIMTRDV----------- 160
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 437 AFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 480
Cdd:COG2524 161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
359-482 4.84e-16

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 74.77  E-value: 4.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpisGNALY-ILTHKRILKFLqlfMSDMPKPAFMKQNLDELGIgTYHNI- 436
Cdd:cd04584   8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVD---DGKLVgIVTDRDLLRAS---PSKATSLSIYELNYLLSKI-PVKDIm 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 33186925 437 ----AFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLA 482
Cdd:cd04584  81 tkdvITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129
CBS COG0517
CBS domain [Signal transduction mechanisms];
359-484 1.75e-15

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 72.98  E-value: 1.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILTHKRILKFLqlfmsdmpkpAFMKQNLDELGIGTY--HN 435
Cdd:COG0517   9 TDVVTVSPDATVREALELMSEKRIGGLPVVD--EDGKLVgIVTDRDLRRAL----------AAEGKDLLDTPVSEVmtRP 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 33186925 436 IAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 484
Cdd:COG0517  77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
439-553 1.79e-15

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 73.23  E-value: 1.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEGVVKCNKL---E 515
Cdd:cd04586   8 VTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRREEPGTEPRRVWWLDALLESPERLAEEYVKAHGRtvgD 87
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 33186925 516 I-------------LETIVDRIVRAEVHRLVVVNEaDSIVGIISLSDILQA 553
Cdd:cd04586  88 VmtrpvvtvspdtpLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLLRA 137
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
434-553 2.26e-14

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 69.39  E-value: 2.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLD-ITVtqalqhrSQYFEGVVKCN 512
Cdd:cd04629   3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPgGTV-------ADYMSTEVLTV 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 513 KLEilETIVD---RIVRAEVHRLVVVnEADSIVGIISLSDILQA 553
Cdd:cd04629  76 SPD--TSIVDlaqLFLKNKPRRYPVV-EDGKLVGQISRRDVLRA 116
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
277-406 5.59e-14

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: 68.43  E-value: 5.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 277 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILHRYYKSPMVQIYELEEHKIETwrelylqe 356
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK-LVGIVTERDILRALVEGGLALDTPVAEVMTPDVIT-------- 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 33186925 357 tfkplvnISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILK 406
Cdd:cd02205  72 -------VSPDTDLEEALELMLEHGIRRLPVVDD-DGKLVGIVTRRDILR 113
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
359-481 6.14e-12

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: 62.55  E-value: 6.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPAFMKQNldelgigtyhnIAF 438
Cdd:cd04588   2 KDLITLKPDATIKDAAKLLSENNIHGAPVVD--DGKLVGIVTLTDIAKALAEGKENAKVKDIMTKD-----------VIT 68
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINL 481
Cdd:cd04588  69 IDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILKV 111
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
439-553 7.91e-12

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 62.73  E-value: 7.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNN------------LDITVtqalqhRSQYFE 506
Cdd:cd04632   7 VNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTrggdrggekermLDLPV------YDIMSS 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 33186925 507 GVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQA 553
Cdd:cd04632  81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
432-554 9.40e-12

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 62.62  E-value: 9.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 432 TYHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLditVTQALQhrsqyfegVVKC 511
Cdd:COG4109  23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTPIEDV---MTKNPI--------TVTP 91
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33186925 512 NklEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 554
Cdd:COG4109  92 D--TSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKAL 132
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
435-554 3.04e-11

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 60.61  E-value: 3.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTynNLDITVTQALqhrsqyFEGVVKCNKL 514
Cdd:cd09836   4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGI--DLDTPVEEIM------TKNLVTVSPD 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 33186925 515 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 554
Cdd:cd09836  76 ESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
439-483 4.92e-11

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: 57.91  E-value: 4.92e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 33186925    439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAA 483
Cdd:smart00116   5 VSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
359-484 8.05e-11

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 59.46  E-value: 8.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLfmsdmpkpafMKQNLDELGIGTY--HNI 436
Cdd:COG2905   7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDD-DGRLVGIITDRDLRRRVLA----------EGLDPLDTPVSEVmtRPP 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 33186925 437 AFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAE 484
Cdd:COG2905  76 ITVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSE 122
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
439-554 1.44e-10

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 59.11  E-value: 1.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQyFEGVVKcnklEILE 518
Cdd:cd04600   8 VTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLDPPRGLRGRLRRTLGLRRD-RPETVG----DIMT 82
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 33186925 519 TIVdRIVRAEVH--RLV------------VVNEADSIVGIISLSDILQAL 554
Cdd:cd04600  83 RPV-VTVRPDTPiaELVplfsdgglhhipVVDADGRLVGIVTQSDLIAAL 131
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
359-479 2.87e-10

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


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 58.40  E-value: 2.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFL-----QLFMSDMPKPAFMK---QNLDElgI 430
Cdd:cd17779   8 KDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskYNLVEKKHNGNLLAainEPVRE--I 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 33186925 431 GTyHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 479
Cdd:cd17779  86 MT-RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
434-484 6.97e-10

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: 54.91  E-value: 6.97e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 33186925   434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAE 484
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
434-550 7.28e-10

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


Pssm-ID: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 56.66  E-value: 7.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRsqyfegVVKCNK 513
Cdd:cd04623   2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRD------VVTCTP 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 33186925 514 ----LEILETIVDRIVRaevHRLVVvnEADSIVGIISLSDI 550
Cdd:cd04623  76 ddtvEECMALMTERRIR---HLPVV--EDGKLVGIVSIGDV 111
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
277-408 7.50e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 58.74  E-value: 7.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 277 SSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKqsFVGMLTITDFINILHRYYKSPMVQIyeleehkietwRELYLqe 356
Cdd:COG2524  93 TKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK--LVGIITERDLLKALAEGRDLLDAPV-----------SDIMT-- 157
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33186925 357 tfKPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 408
Cdd:COG2524 158 --RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDD-DGKLVGIITRTDILRAL 206
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
434-552 2.94e-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: 54.85  E-value: 2.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEktyNNLDITVTQALQHRsqyfegVVKCNK 513
Cdd:cd04588   2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD-GKLVGIVTLTDIAKALAE---GKENAKVKDIMTKD------VITIDK 71
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 33186925 514 LEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQ 552
Cdd:cd04588  72 DEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
434-550 6.21e-09

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


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 53.96  E-value: 6.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVV------DIyskfdVIN-LAAEKTYNnlDITVTQALQHrsqyfe 506
Cdd:cd04622   3 RDVVTVSPDTTLREAARLMRDLDIGALPVCEG-DRLVgmvtdrDI-----VVRaVAEGKDPN--TTTVREVMTG------ 68
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 507 GVVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 550
Cdd:cd04622  69 DVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
359-480 1.31e-08

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 52.91  E-value: 1.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLFMS-DMPKPAFMKQNLdelgIGTYhnia 437
Cdd:cd09836   3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDD-DGKPVGIVTERDIVRAVAEGIDlDTPVEEIMTKNL----VTVS---- 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33186925 438 fihPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 480
Cdd:cd09836  74 ---PDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
359-479 1.78e-08

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


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 53.20  E-value: 1.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNAL-------------YILTHKRILKFLQLFMSDMPKPAfmKQNL 425
Cdd:cd04586   3 TDVVTVTPDTSVREAARLLLEHRISGLPVVD--DDGKLvgivsegdllrreEPGTEPRRVWWLDALLESPERLA--EEYV 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 33186925 426 DELG-----IGTyHNIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVI 479
Cdd:cd04586  79 KAHGrtvgdVMT-RPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLL 135
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
441-553 3.47e-08

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


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 52.47  E-value: 3.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 441 PDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKTYNNLDITVTQALQHRSQYFEG---VVKCNKLEI- 516
Cdd:cd17789  10 PNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDNNFPPADSTWKTFNEVqklLSKTNGKVVg 89
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33186925 517 -LETIVDRIVRAE--------------VHRLVVVNEADSIVGIISLSDILQA 553
Cdd:cd17789  90 dVMTPSPLVVREKtnledaarilletkFRRLPVVDSDGKLVGIITRGNVVRA 141
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
362-480 5.16e-08

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 51.84  E-value: 5.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 362 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFL---QLFMS----------DMPKPAFMKQNldel 428
Cdd:cd04631  11 ITATPGTPIEDVAKIMVRNGFRRLPVVS--DGKLVGIVTSTDIMRYLgsgEAFEKlktgnihevlNVPISSIMKRD---- 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 33186925 429 gigtyhnIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 480
Cdd:cd04631  85 -------IITTTPDTDLGEAAELMLEKNIGALPVVDD-GKLVGIITERDILR 128
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
360-409 5.33e-08

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: 49.43  E-value: 5.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 33186925    360 PLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQ 409
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDE-EGRLVGIVTRRDIIKALA 49
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
361-480 6.14e-08

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 51.28  E-value: 6.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 361 LVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLqlfmsdmpkpafmkqnLDelgiGTYHN----- 435
Cdd:cd04629   5 PVTLTPDTSILEAVELLLEHKISGAPVVDE-QGRLVGFLSEQDCLKAL----------------LE----ASYHCepggt 63
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33186925 436 --------IAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 480
Cdd:cd04629  64 vadymsteVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQISRRDVLR 115
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
359-481 8.48e-08

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: 50.64  E-value: 8.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPISGNALYILTHKRILKFLQLFMSDMPKPAFMKQnldelgigtyhNIAF 438
Cdd:cd17772   2 SPVISVEPDTTIAEAAELMTRYNINALPVVDGGTGRLVGIITRQVAEKAIYHGLGDLPVSEYMTT-----------EFAT 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINL 481
Cdd:cd17772  71 VTPDAPLSEIQEIIVEQRQRLVPVVED-GRLVGVITRTDLLNL 112
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
351-479 1.05e-07

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


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 51.19  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 351 ELYLQETfKPLVNISPDASLFDAVYSLIKNKIHRLPVIDpisGNALY-ILTHKRILKFLQLFMSDMPKPAFMKQNLDELG 429
Cdd:cd17777   3 ELMIIAS-PPVLSISPSAPILSAFEKMNRRGIRRLVVVD---ENKLEgILSARDLVSYLGGGCLFKIVESRHQGDLYSAL 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 33186925 430 ----IGTYH--NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 479
Cdd:cd17777  79 nrevVETIMtpNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
284-408 2.24e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 50.25  E-value: 2.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 284 DTTLqvKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILHRYYKSPMVqiYELEEHKIE---TwrelylqetfKP 360
Cdd:COG3448  18 DTTL--REALELMREHGIRGLPVVDEDGR-LVGIVTERDLLRALLPDRLDELE--ERLLDLPVEdvmT----------RP 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 33186925 361 LVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 408
Cdd:COG3448  83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDD-DGRLVGIVTRTDLLRAL 129
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
359-479 2.56e-07

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 49.64  E-value: 2.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFL--QLFMSDMPKP---AFMKQNLDELgigTY 433
Cdd:cd17778   8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVS--GGKLVGIVTAMDIVKYFgsHEAKKRLTTGdidEAYSTPVEEI---MS 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 479
Cdd:cd17778  83 KEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVL 128
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
508-555 3.27e-07

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 47.12  E-value: 3.27e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 33186925    508 VVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKALA 49
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
359-474 3.65e-07

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


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 48.77  E-value: 3.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLqlfmsdmpkpAFMKQNLDElgIGTyHNIAF 438
Cdd:cd04605   8 KDVATIREDISIEEAAKIMIDKNVTHLPVVSE-DGKLIGIVTSWDISKAV----------ALKKDSLEE--IMT-RNVIT 73
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYS 474
Cdd:cd04605  74 ARPDEPIELAARKMEKHNISALPVVDDDRRVIGIIT 109
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
360-480 1.45e-06

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


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 47.11  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 360 PLVNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFLQLFMSDMPKPAFMKQNldelgigtyhnIAFI 439
Cdd:cd04595   3 PVKTVSPDTTIEEARKIMLRYGHTGLPVVE--DGKLVGIISRRDVDKAKHHGLGHAPVKGYMSTN-----------VITI 69
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 33186925 440 HPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVIN 480
Cdd:cd04595  70 DPDTSLEEAQELMVEHDIGRLPVVEE-GKLVGIVTRSDVLR 109
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
46-221 1.60e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 51.33  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925    46 PLLDGDLEGSGKHSSRKVDSPFGPGSPSKGFFSRGPQPR-PSSPMSAPVRPKTSPGSPKTVFPFSYQES--PPRSPRRMS 122
Cdd:PHA03307  132 PDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRqAALPLSSPEETARAPSSPPAEPPPSTPPAaaSPRPPRRSS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925   123 FSGIfrssskessPNSNPATSPGGIRFFSRSRKTSGLSSSPSTPTQVTKQHTFPLESykHEPERLENRIYASSSPPDTGQ 202
Cdd:PHA03307  212 PISA---------SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPR--PAPITLPTRIWEASGWNGPSS 280
                         170
                  ....*....|....*....
gi 33186925   203 RFCPSSFQSPTRPPLASPT 221
Cdd:PHA03307  281 RPGPASSSSSPRERSPSPS 299
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
364-480 2.89e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 46.83  E-value: 2.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 364 ISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFlqlfMSDMPKPAFMKqnldelgigtyHNIAFIHPDT 443
Cdd:COG4109  30 LSEDDTVEDALELLEKTGHSRFPVVDE-NGRLVGIVTSKDILGK----DDDTPIEDVMT-----------KNPITVTPDT 93
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 33186925 444 PIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN 480
Cdd:COG4109  94 SLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
508-555 3.06e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.51  E-value: 3.06e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 33186925   508 VVKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:pfam00571   9 VVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
359-408 3.18e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.51  E-value: 3.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 33186925   359 KPLVNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFL 408
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRAL 55
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
364-480 4.43e-06

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 45.42  E-value: 4.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 364 ISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQLFMSdmpkpafmKQNLdelgigtyhnIAFIHPDT 443
Cdd:cd04597  10 LSPETSIKDAWNLMDENNLKTLPVTDD-NGKLIGLLSISDIARTVDYIMT--------KDNL----------IVFKEDDY 70
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 33186925 444 -PIIKalNIFVERRISALPVVDESGKVVDIYSKFDVIN 480
Cdd:cd04597  71 lDEVK--EIMLNTNFRNYPVVDENNKFLGTISRKHLIN 106
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
435-550 5.46e-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: 5.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAAEKtYNNLDITVTQalqhrsqyfeGVVKCNKL 514
Cdd:cd04605   9 DVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALK-KDSLEEIMTR----------NVITARPD 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33186925 515 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 550
Cdd:cd04605  78 EPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
280-328 7.12e-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: 43.27  E-value: 7.12e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 33186925    280 LVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINILH 328
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGR-LVGIVTRRDIIKALA 49
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
439-550 9.34e-06

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: 45.25  E-value: 9.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDV-----INLAAEKTYNNLDITVTQALQHRSQY----FEGVV 509
Cdd:cd04640  10 IDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDIlgekpLKIVQERGIPREELLVADVMTPRDKLealdYEDVA 89
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 510 KCNKLEILETIVDrivRAEVHRLVVVNEADS---IVGIISLSDI 550
Cdd:cd04640  90 HARVGDVVETLKA---SGRQHALVVDRDEDGrqeVRGIFSASQI 130
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
284-408 9.74e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 45.21  E-value: 9.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 284 DTTlqVKKAFFALVANGVRAAPLwESKKQSFVGMLTITDFINILHRYYKSPM-VQIYEleehkIETwrelylqetfKPLV 362
Cdd:COG2905  15 DAT--VREAARLMTEKGVGSLVV-VDDDGRLVGIITDRDLRRRVLAEGLDPLdTPVSE-----VMT----------RPPI 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 33186925 363 NISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILKFL 408
Cdd:COG2905  77 TVSPDDSLAEALELMEEHRIRHLPVVD--DGKLVGIVSITDLLRAL 120
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
435-554 1.16e-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: 45.01  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDeSGKVVDIYSKFDVI-NLAAEKTYNNLDIT-VTQALQHRSQYF--EGVVK 510
Cdd:cd17778   9 PVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVkYFGSHEAKKRLTTGdIDEAYSTPVEEImsKEVVT 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33186925 511 CNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 554
Cdd:cd17778  88 IEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
438-551 1.23e-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: 44.33  E-value: 1.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 438 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLAaektynNLDITVtqalqhrSQY---FEGVVKCNKL 514
Cdd:cd04601   6 TLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIRFET------DLSTPV-------SEVmtpDERLVTAPEG 72
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 33186925 515 EILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDIL 551
Cdd:cd04601  73 ITLEEAKEILHKHKIEKLPIVDDNGELVGLITRKDIE 109
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
438-551 1.32e-05

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


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 44.45  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 438 FIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVIN-LAAEKTynNLDITVTQALQHRsqyFEGVVKCNKLEI 516
Cdd:cd04608  14 TVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSsLLAGRA--QPSDPVSKAMYKQ---FKQVDLDTPLGA 88
                        90       100       110
                ....*....|....*....|....*....|....*
gi 33186925 517 LETIVDRivraeVHRLVVVNEADSIVGIISLSDIL 551
Cdd:cd04608  89 LSRILER-----DHFALVVDGQGKVLGIVTRIDLL 118
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
441-550 1.73e-05

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


Pssm-ID: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 44.14  E-value: 1.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 441 PDTPIIKALNIFVERRISALpVVDESGKVVDIYSKFDVinLAaektynnLDITVTQALQHR-SQYFEGVVKCnkLEILET 519
Cdd:cd09833  12 PDTPLADAAARMAERRCSSI-LIVENGEIVGIWTERDA--LK-------LDFSDPDAFRRPiSEVMSSPVLT--IPQDTT 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 33186925 520 IVDRIVR---AEVHRLVVVNEADSIVGIISLSDI 550
Cdd:cd09833  80 LGEAAVRfrqEGVRHLLVVDDDGRPVGIVSQTDV 113
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
433-551 2.81e-05

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 43.49  E-value: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 433 YHNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSkfdVINLAAEKTYnnldITVTqalqhrsqyfEGVVKCN 512
Cdd:cd04597   4 YDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLS---ISDIARTVDY----IMTK----------DNLIVFK 66
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 33186925 513 KLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDIL 551
Cdd:cd04597  67 EDDYLDEVKEIMLNTNFRNYPVVDENNKFLGTISRKHLI 105
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
435-472 3.37e-05

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


Pssm-ID: 341417 [Multi-domain]  Cd Length: 118  Bit Score: 43.34  E-value: 3.37e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDI 472
Cdd:cd17781  69 NPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGV 106
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
434-554 3.41e-05

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 43.30  E-value: 3.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFD-VINLAAEktynNLDITVTQALQHRSQyfEGVVKCN 512
Cdd:cd17775   3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDiVVEVVAK----GLDPKDVTVGDIMSA--DLITARE 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 33186925 513 KLEILETIvdRIVRAE-VHRLVVVNEADSIVGIISLSDILQAL 554
Cdd:cd17775  77 DDGLFEAL--ERMREKgVRRLPVVDDDGELVGIVTLDDILELL 117
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
439-470 3.84e-05

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


Pssm-ID: 341378 [Multi-domain]  Cd Length: 124  Bit Score: 43.52  E-value: 3.84e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVV 470
Cdd:cd04604  83 ISPDALAAEALELMEEHKITVLPVVDEDGKPV 114
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
362-470 7.04e-05

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 45.46  E-value: 7.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925   362 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILThKRILKFLqlfmSDMPKP--AFMkqnldelgigTYHNIAFI 439
Cdd:pfam00478  91 VTLSPDATVADALALMERYGISGVPVVD--DGKLVGIVT-NRDLRFE----TDLSQPvsEVM----------TKENLVTA 153
                          90       100       110
                  ....*....|....*....|....*....|.
gi 33186925   440 HPDTPIIKALNIFVERRISALPVVDESGKVV 470
Cdd:pfam00478 154 PEGTTLEEAKEILHKHKIEKLPVVDDNGRLV 184
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
364-481 8.56e-05

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


Pssm-ID: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 42.17  E-value: 8.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 364 ISPDASLFDAVYSLI--KNKIHRLPVIDP-------ISGNAL-YILTHKrilkflqlfMSDMPKPAFMKqnldelgigTY 433
Cdd:cd04639  10 VDADLTLREFADDYLigKKSWREFLVTDEagrlvglITVDDLrAIPTSQ---------WPDTPVRELMK---------PL 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINL 481
Cdd:cd04639  72 EEIPTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIEL 119
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
435-554 1.24e-04

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


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 42.02  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDV-INLAAEKTynNLDITVTQALQhrsqyfEGVVKCNK 513
Cdd:cd17784   3 NVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLgHNLILDKY--ELGTTVEEVMV------KDVATVHP 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 33186925 514 leiLETIVDRIVRAE--------VHRLVVVNEADsIVGIISLSDILQAL 554
Cdd:cd17784  75 ---DETLLEAIKKMDsnapdeeiINQLPVVDDGK-LVGIISDGDIIRAI 119
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
439-551 1.92e-04

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 40.79  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAektyNNLditVTQALQhrsqyfEGVVKCNKLEILE 518
Cdd:cd04599   8 ISPLDSVARAAALMERQRIGGLPVVEN-GKLVGIITSRDVRRAHP----NRL---VADAMS------RNVVTISPEASLW 73
                        90       100       110
                ....*....|....*....|....*....|...
gi 33186925 519 TIVDRIVRAEVHRLVVVnEADSIVGIISLSDIL 551
Cdd:cd04599  74 EAKELMEEHGIERLVVV-EEGRLVGIITKSTLY 105
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
439-551 1.96e-04

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


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 40.96  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSkFDVINLAAEKtynnlDITVTQALQHRSQYfegvVKCNKLeiLE 518
Cdd:cd04583   7 ITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVD-IEDINRNYRK-----AKKVGEIMERDVFT----VKEDSL--LR 74
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33186925 519 TIVDRIVRAEVHRLVVVNEADSIVGII---SLSDIL 551
Cdd:cd04583  75 DTVDRILKRGLKYVPVVDEQGRLVGLVtraSLVDIV 110
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
439-554 2.14e-04

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


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 41.45  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDE-SGKVVDIYSKFDVI---------NLAAEKTYNNLDITVTQALqhRSQYFEGV 508
Cdd:cd17779  13 IPPTTTIIGAIKTMTEKGFRRLPVADAgTKRLEGIVTSMDIVdflgggskyNLVEKKHNGNLLAAINEPV--REIMTRDV 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 33186925 509 VKCNKLEILETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQAL 554
Cdd:cd17779  91 ISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
447-553 2.20e-04

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


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 40.79  E-value: 2.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 447 KALNIFVERRISALPVV-DESGKVVDIYSKFDVINlaaektynNLDITVTQALQHRSqyfegVVKCNKLEILETIVDRIV 525
Cdd:cd04638  16 DVLEILKKKAISGVPVVkKETGKLVGIVTRKDLLR--------NPDEEQIALLMSRD-----PITISPDDTLSEAAELML 82
                        90       100
                ....*....|....*....|....*...
gi 33186925 526 RAEVHRLVVVnEADSIVGIISLSDILQA 553
Cdd:cd04638  83 EHNIRRVPVV-DDDKLVGIVTVADLVRA 109
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
264-409 3.46e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.05  E-value: 3.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 264 FMRSHKCYDIVpTSSKLVVFDTTLQVKKAFFALVANGVRAAPLWESKKQsFVGMLTITDFINilhryyKSPMVQIYELEE 343
Cdd:COG4109  12 FKEILLVEDIM-TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGR-LVGIVTSKDILG------KDDDTPIEDVMT 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33186925 344 HKIETwrelylqetfkplvnISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFLQ 409
Cdd:COG4109  84 KNPIT---------------VTPDTSLASAAHKMIWEGIELLPVVDD-DGRLLGIISRQDVLKALQ 133
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
362-405 6.78e-04

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 39.25  E-value: 6.78e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 33186925 362 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRIL 405
Cdd:cd04599  64 VTISPEASLWEAKELMEEHGIERLVVVE--EGRLVGIITKSTLY 105
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
315-389 7.62e-04

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


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 39.31  E-value: 7.62e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33186925 315 VGMLTITDFINILHRYYKS-PMVQIYELEEHkietwrelylqetfkPLVNISPDASLFDAVYSLIKNKIHRLPVID 389
Cdd:cd17776  38 AGILTETDALHAGYATDDPfSEIPVRAVASR---------------PLVTISPTATLREAAERMVDEGVKKLPVVD 98
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
439-553 9.78e-04

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


Pssm-ID: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 38.86  E-value: 9.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVinlaAEKTYNNLDITVTQALQHrsqyfegVVKCNKLE-IL 517
Cdd:cd04594   7 VSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDI----ENKSPGKVGKYVVRGSPY-------VTPTSSLEeAW 75
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33186925 518 ETIVdrIVRAevhRLVVVNEADSIVGIISLSDILQA 553
Cdd:cd04594  76 EIMM--RNKS---RWVAVVEKGKFLGIITLDDLLEA 106
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
362-472 1.07e-03

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


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 38.93  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 362 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALY-ILThKRILKFLQlfMSDMPKPAFMKQNLDelgigtyhnIAFIH 440
Cdd:cd04601   5 VTLSPDATVADVLELKAEYGISGVPVTE--DGGKLVgIVT-SRDIRFET--DLSTPVSEVMTPDER---------LVTAP 70
                        90       100       110
                ....*....|....*....|....*....|..
gi 33186925 441 PDTPIIKALNIFVERRISALPVVDESGKVVDI 472
Cdd:cd04601  71 EGITLEEAKEILHKHKIEKLPIVDDNGELVGL 102
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
359-482 1.37e-03

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 38.68  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVID----PISgnalyILTHKRILKflqlfmsdmpkpAFMKQNLDELGIgTYH 434
Cdd:cd17775   3 REVVTASPDTSVLEAARLMRDHHVGSVVVVEedgkPVG-----IVTDRDIVV------------EVVAKGLDPKDV-TVG 64
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33186925 435 NI-----AFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVINLA 482
Cdd:cd17775  65 DImsadlITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
362-484 1.38e-03

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 39.01  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 362 VNISPDASLFDAVYSLIKNKIHRLPVIDPiSGNALYILTHKRILKFlqlfmsdmpkpAFMKQNLDELGIGT----YHNIA 437
Cdd:cd04617   7 VVVDETTSVYDAIVTLFLEDVGSLFVVDE-EGYLVGVVSRKDLLKA-----------TLGGQDLEKTPVSMimtrMPNIV 74
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 33186925 438 FIHPDTPIIKALNIFVERRISALPVVDESG---KVVDIYSKFDVINLAAE 484
Cdd:cd04617  75 TVTPDDSVLEAARKLIEHEIDSLPVVEKEDgklKVVGRITKTNITRLFVE 124
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
435-550 1.51e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.36  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925  435 NIAFIHPDTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDvinLAaeKTYnnLDITVTQALQHRSQYFEGVVKCNKL 514
Cdd:PRK14869  77 KPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSD---LA--RAY--MDILDPEILSKSPTSLENIIRTLDG 149
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 33186925  515 EILeTIVDRIVRAEVHRLVVVNEADSIVGIISLSDI 550
Cdd:PRK14869 150 EVL-VGAEEDKVEEGKVVVAAMAPESLLERIEEGDI 184
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
359-389 1.64e-03

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


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 38.56  E-value: 1.64e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 33186925 359 KPLVNISPDASLFDAVYSLIKNKIHRLPVID 389
Cdd:cd04587  68 PPPVTIDADALVFEALLLMLERNIHHLPVVD 98
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
517-555 1.85e-03

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 38.38  E-value: 1.85e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 33186925 517 LETIVDRIVRAEVHRLVVVNEADSIVGIISLSDILQALI 555
Cdd:cd02205  13 VREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
529-554 2.64e-03

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


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 38.29  E-value: 2.64e-03
                        10        20
                ....*....|....*....|....*.
gi 33186925 529 VHRLVVVNEADSIVGIISLSDILQAL 554
Cdd:cd17774 100 IRRLVVVGEQGELLGIVTQTSLLQAL 125
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
362-479 5.22e-03

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 36.92  E-value: 5.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 362 VNISPDASLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILkflqLFMSDMPKPAFMKQNldelgigtyhnIAFIHP 441
Cdd:cd04610   6 ITVSPDDTVKDVIKLIKETGHDGFPVVD--DGKVVGYVTAKDLL----GKDDDEKVSEIMSRD-----------TVVADP 68
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 33186925 442 DTPIIKALNIFVERRISALPVVDESGKVVDIYSKFDVI 479
Cdd:cd04610  69 DMDITDAARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
434-487 6.11e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 39.28  E-value: 6.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 434 HNIAFIHPDTPIIKALNIFVERRISALPVVDESGKVV------DIYskfDVINLAAEKTY 487
Cdd:COG2239 201 TDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVgiitvdDVV---DVIEEEATEDI 257
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
296-406 6.34e-03

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 37.21  E-value: 6.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 296 LVANGVRAAPLWESKKqsFVGMLTITDFInilhRYYKSPMV-------QIYELEEHKIetwRELYLQEtfkpLVNISPDA 368
Cdd:cd04631  26 MVRNGFRRLPVVSDGK--LVGIVTSTDIM----RYLGSGEAfeklktgNIHEVLNVPI---SSIMKRD----IITTTPDT 92
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 33186925 369 SLFDAVYSLIKNKIHRLPVIDpiSGNALYILTHKRILK 406
Cdd:cd04631  93 DLGEAAELMLEKNIGALPVVD--DGKLVGIITERDILR 128
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
435-554 6.71e-03

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 37.21  E-value: 6.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 435 NIAFIHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEKtynnlditvtqalqhrsQYFEGVVKCNKL 514
Cdd:cd04631   9 NVITATPGTPIEDVAKIMVRNGFRRLPVVSD-GKLVGIVTSTDIMRYLGSG-----------------EAFEKLKTGNIH 70
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 515 EILETIVDRIVRAEVHRL--------------------VVVNEADSIVGIISLSDILQAL 554
Cdd:cd04631  71 EVLNVPISSIMKRDIITTtpdtdlgeaaelmleknigaLPVVDDGKLVGIITERDILRAI 130
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
440-472 7.10e-03

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


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 36.65  E-value: 7.10e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 33186925 440 HPDTPIIKALNIFVERRISALPVVDESGKVVDI 472
Cdd:cd04607  72 SPSTSREELLALMRAKKILQLPIVDEQGRVVGL 104
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
439-554 8.31e-03

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


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 36.94  E-value: 8.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33186925 439 IHPDTPIIKALNIFVERRISALPVVDEsGKVVDIYSKFDVINLAAEKTYNNLditvtqaLQHRSQYfeGVVKCNKLEILE 518
Cdd:cd17777  15 ISPSAPILSAFEKMNRRGIRRLVVVDE-NKLEGILSARDLVSYLGGGCLFKI-------VESRHQG--DLYSALNREVVE 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 33186925 519 TIVDR-------------IVRAEVHR----LVVVNEADSIVGIISLSDILQAL 554
Cdd:cd17777  85 TIMTPnpvyvyedsdlieALTIMVTRgigsLPVVDRDGRPVGIVTERDLVLYL 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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