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Conserved domains on  [gi|508167908|gb|EOT44457|]
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hypothetical protein OMW_00513 [Enterococcus columbae DSM 7374 = ATCC 51263]

Protein Classification

CBS domain-containing protein( domain architecture ID 10140297)

CBS domain-containing protein similar to Bacillus subtilis YkuL

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_CbpB NF041630
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ...
 4-146 2.40e-73

cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase.


:

Pssm-ID: 469514 [Multi-domain]  Cd Length: 143  Bit Score: 216.16  E-value: 2.40e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908   4 KHVQALLTETEDTFLIPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQRLEV 83
Cdd:NF041630   1 KEIEELLLENIEDFLIPAEKVAHVQDTNNLEHALLVLTKVGYSKIPVLDKDKKFVGLISLSDITDYMLGLERIEFEKLSE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508167908  84 LTVADVMEVKVPKMTEKDDLETLLRRLVNEPFLPYVDQNNVFLGIFTRKAILKSVNHMVHEIE 146
Cdd:NF041630  81 LKVADVMNTDVPTITDDYDLEEILHLLVDHPFLPVVDEDGIFLGIITRREILKAVNYLLHEFE 143
 
Name Accession Description Interval E-value
CBS_CbpB NF041630
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ...
 4-146 2.40e-73

cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase.


Pssm-ID: 469514 [Multi-domain]  Cd Length: 143  Bit Score: 216.16  E-value: 2.40e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908   4 KHVQALLTETEDTFLIPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQRLEV 83
Cdd:NF041630   1 KEIEELLLENIEDFLIPAEKVAHVQDTNNLEHALLVLTKVGYSKIPVLDKDKKFVGLISLSDITDYMLGLERIEFEKLSE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508167908  84 LTVADVMEVKVPKMTEKDDLETLLRRLVNEPFLPYVDQNNVFLGIFTRKAILKSVNHMVHEIE 146
Cdd:NF041630  81 LKVADVMNTDVPTITDDYDLEEILHLLVDHPFLPVVDEDGIFLGIITRREILKAVNYLLHEFE 143
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 16-145 7.39e-67

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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 199.26  E-value: 7.39e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  16 TFLIPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQRLEVLTVADVMEVKVP 95
Cdd:cd04643    1 DFLIPAEKVAHVQDTNNLEHALLVLTKSGYSRIPVLDKDYKLVGLISLSMILDAILGLERIEFEKLSELKVEEVMNTDVP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 508167908  96 KMTEKDDLETLLRRLVNEPFLPYVDQNNVFLGIFTRKAILKSVNHMVHEI 145
Cdd:cd04643   81 TVSPDDDLEEVLHLLVDHPFLCVVDEDGYFLGIITRREILKAVNKLLHEF 130
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
4-141 1.66e-21

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 84.19  E-value: 1.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908   4 KHVqalLTETEDTFL--------IPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMqeisgltG 75
Cdd:COG4109    2 KHI---ISTSYDTFKeillvediMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL-------G 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508167908  76 FDMQrlevLTVADVMEVKVPKMTEKDDLETLLRRLVNE--PFLPYVDQNNVFLGIFTRKAILKSVNHM 141
Cdd:COG4109   72 KDDD----TPIEDVMTKNPITVTPDTSLASAAHKMIWEgiELLPVVDDDGRLLGIISRQDVLKALQKI 135
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 19-72 6.47e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.13  E-value: 6.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 508167908   19 IPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISG 72
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 23-66 9.18e-05

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 38.26  E-value: 9.18e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 508167908    23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADI 66
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 26-137 7.59e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 35.72  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  26 TLLYNHPLEHAMLILTNVGYSKIPVLDSEDH---LVGLISLADI--MQEISGLTGFDMQRLEVLTV-------ADVMEVK 93
Cdd:PTZ00314 108 VLSPNHTVADVLEIKEKKGFSSILITVDGKVggkLLGIVTSRDIdfVKDKSTPVSEVMTPREKLVVgntpislEEANEVL 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 508167908  94 VPKMTEKddletllrrlvnepfLPYVDQNNVFLGIFTRKAILKS 137
Cdd:PTZ00314 188 RESRKGK---------------LPIVNDNGELVALVSRSDLKKN 216
 
Name Accession Description Interval E-value
CBS_CbpB NF041630
cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS ...
 4-146 2.40e-73

cyclic-di-AMP-binding protein CbpB; CbpB (c-di-AMP-binding protein B) has two CBS (cystathionine beta synthase) domains (see PF00571). When levels of c-di-AMP are low, CbpB activates RelA, a bifunctional (p)ppGpp synthetase/hydrolase.


Pssm-ID: 469514 [Multi-domain]  Cd Length: 143  Bit Score: 216.16  E-value: 2.40e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908   4 KHVQALLTETEDTFLIPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQRLEV 83
Cdd:NF041630   1 KEIEELLLENIEDFLIPAEKVAHVQDTNNLEHALLVLTKVGYSKIPVLDKDKKFVGLISLSDITDYMLGLERIEFEKLSE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 508167908  84 LTVADVMEVKVPKMTEKDDLETLLRRLVNEPFLPYVDQNNVFLGIFTRKAILKSVNHMVHEIE 146
Cdd:NF041630  81 LKVADVMNTDVPTITDDYDLEEILHLLVDHPFLPVVDEDGIFLGIITRREILKAVNYLLHEFE 143
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 16-145 7.39e-67

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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 199.26  E-value: 7.39e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  16 TFLIPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQRLEVLTVADVMEVKVP 95
Cdd:cd04643    1 DFLIPAEKVAHVQDTNNLEHALLVLTKSGYSRIPVLDKDYKLVGLISLSMILDAILGLERIEFEKLSELKVEEVMNTDVP 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 508167908  96 KMTEKDDLETLLRRLVNEPFLPYVDQNNVFLGIFTRKAILKSVNHMVHEI 145
Cdd:cd04643   81 TVSPDDDLEEVLHLLVDHPFLCVVDEDGYFLGIITRREILKAVNKLLHEF 130
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
4-141 1.66e-21

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 84.19  E-value: 1.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908   4 KHVqalLTETEDTFL--------IPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMqeisgltG 75
Cdd:COG4109    2 KHI---ISTSYDTFKeillvediMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDIL-------G 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508167908  76 FDMQrlevLTVADVMEVKVPKMTEKDDLETLLRRLVNE--PFLPYVDQNNVFLGIFTRKAILKSVNHM 141
Cdd:COG4109   72 KDDD----TPIEDVMTKNPITVTPDTSLASAAHKMIWEgiELLPVVDDDGRLLGIISRQDVLKALQKI 135
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
23-144 5.79e-20

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 80.29  E-value: 5.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQ-RLEVLTVADVMEVKVPKMTEKD 101
Cdd:COG3448   11 DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEeRLLDLPVEDVMTRPVVTVTPDT 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 508167908 102 DLETLLRRLVNEP--FLPYVDQNNVFLGIFTRKAILKSVNHMVHE 144
Cdd:COG3448   91 PLEEAAELMLEHGihRLPVVDDDGRLVGIVTRTDLLRALARLLEE 135
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 23-136 4.56e-15

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 66.88  E-value: 4.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEIsgltgFDMQRLEVLTVADVMEVKVPKMTEKDD 102
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRAL-----VEGGLALDTPVAEVMTPDVITVSPDTD 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 508167908 103 LETLLRRLV--NEPFLPYVDQNNVFLGIFTRKAILK 136
Cdd:cd02205   78 LEEALELMLehGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
23-138 1.44e-13

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 65.29  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDsEDHLVGLISLADIMQEIsgltgFDMQRLEVLTVADVMEVKVPKMTEKDD 102
Cdd:COG2524   95 DVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKAL-----AEGRDLLDAPVSDIMTRDVVTVSEDDS 168

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 508167908 103 LETLLRRLV--NEPFLPYVDQNNVFLGIFTRKAILKSV 138
Cdd:COG2524  169 LEEALRLMLehGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
23-138 1.54e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 60.65  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQRlevlTVADVMEVKVPKMTEKDD 102
Cdd:COG0517   10 DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDT----PVSEVMTRPPVTVSPDTS 85

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 508167908 103 LETLLRRLVNEPF--LPYVDQNNVFLGIFTRKAILKSV 138
Cdd:COG0517   86 LEEAAELMEEHKIrrLPVVDDDGRLVGIITIKDLLKAL 123
CBS_pair_bac cd09834
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 44-136 6.97e-12

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: 341404 [Multi-domain]  Cd Length: 118  Bit Score: 58.66  E-value: 6.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  44 GYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMQRLEVLTVADV-MEVKVPKMTEKDDLETLLRRLVNEPFLPYVDQN 122
Cdd:cd09834   24 RYTAIPILNRDGKYVGTITEGDLLWYIKNKPNLDLKDAEKISIKDIpRRRDNKPVNINANMEDLLDLAMNQNFVPVVDDR 103

                         90
                 ....*....|....
gi 508167908 123 NVFLGIFTRKAILK 136
Cdd:cd09834  104 GVFIGIVTRKDIIK 117
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 33-131 1.28e-08

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: 50.22  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  33 LEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGltgfDMQRLEvLTVADVMEVKVPKMTEKDDLETLLRRLVN 112
Cdd:cd04608   21 LGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLA----GRAQPS-DPVSKAMYKQFKQVDLDTPLGALSRILER 95

                         90
                 ....*....|....*....
gi 508167908 113 EPFLPYVDQNNVFLGIFTR 131
Cdd:cd04608   96 DHFALVVDGQGKVLGIVTR 114
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 23-136 1.01e-07

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: 47.82  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLTGFDMqrlEVLTVADVMEVKVPKMTEKDD 102
Cdd:cd04629    4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCE---PGGTVADYMSTEVLTVSPDTS 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 508167908 103 LETLLRRLVNEPF--LPYVDqNNVFLGIFTRKAILK 136
Cdd:cd04629   81 IVDLAQLFLKNKPrrYPVVE-DGKLVGQISRRDVLR 115
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 19-72 6.47e-07

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.13  E-value: 6.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 508167908   19 IPAANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISG 72
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 23-138 3.78e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 43.66  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEIsGLTGFDmqrLEVLTVADVMEVKVPKMTEKDD 102
Cdd:COG2905    8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRV-LAEGLD---PLDTPVSEVMTRPPITVSPDDS 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 508167908 103 LETLLRRLVNEPF--LPYVDQNNVfLGIFTRKAILKSV 138
Cdd:COG2905   84 LAEALELMEEHRIrhLPVVDDGKL-VGIVSITDLLRAL 120
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 23-136 5.65e-06

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: 43.57  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIM--QEISGLTGFDMQRLEVL---------------- 84
Cdd:cd04586    4 DVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLrrEEPGTEPRRVWWLDALLesperlaeeyvkahgr 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 508167908  85 TVADVMEVKVPKMTEKDDLETLLRRLVNEPF--LPYVDQNNVfLGIFTRKAILK 136
Cdd:cd04586   84 TVGDVMTRPVVTVSPDTPLEEAARLMERHRIkrLPVVDDGKL-VGIVSRADLLR 136
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 49-139 6.18e-06

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


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 42.95  E-value: 6.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  49 PVLDSEDHLVGLISLADIMQEIsgltgFDMQRLEVLTVADVMEVKVPKMTEKDDLETLLRRLVNEPF--LPYVDQNN--V 124
Cdd:cd04613   30 PVVDEQGRLTGILSIQDVRGVL-----FEEELWDLVVVKDLATTDVITVTPDDDLYTALLKFTSTNLdqLPVVDDDDpgK 104

                         90
                 ....*....|....*
gi 508167908 125 FLGIFTRKAILKSVN 139
Cdd:cd04613  105 VLGMLSRRDVIAAYN 119
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 23-136 6.46e-06

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: 43.18  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDsEDHLVGLISLADIMQ-EISGLTGFDMQRLEVL----TVADVMEVKVPKM 97
Cdd:cd04584    9 NVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRaSPSKATSLSIYELNYLlskiPVKDIMTKDVITV 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 508167908  98 TEKDDLETLLRRLVNEPF--LPYVDQNNVfLGIFTRKAILK 136
Cdd:cd04584   88 SPDDTVEEAALLMLENKIgcLPVVDGGKL-VGIITETDILR 127
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 36-137 6.67e-06

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 43.09  E-value: 6.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  36 AMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEI--------SGLTGFDMQRLEVLTVADVMEVKVPKMTEKDDLETLL 107
Cdd:cd04632   16 AINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVvrpgtktrGGDRGGEKERMLDLPVYDIMSSPVVTVTRDATVADAV 95

                         90       100       110
                 ....*....|....*....|....*....|..
gi 508167908 108 RRLVNEPF--LPYVDQNNVFLGIFTRKAILKS 137
Cdd:cd04632   96 ERMLENDIsgLVVTPDDNMVIGILTKTDVLRA 127
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 32-131 1.58e-05

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: 42.16  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  32 PLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQ--EISGLTGFDMQRLEVL--------TVADVMEVKVPKMTEKD 101
Cdd:cd04600   13 SLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKhaDLDPPRGLRGRLRRTLglrrdrpeTVGDIMTRPVVTVRPDT 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 508167908 102 DLETLLRRLVNEPF--LPYVDQNNVFLGIFTR 131
Cdd:cd04600   93 PIAELVPLFSDGGLhhIPVVDADGRLVGIVTQ 124
CBS_pair_KefB_assoc cd04603
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 30-136 2.22e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain which is involved in inorganic ion transport and metabolism. 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: 341377 [Multi-domain]  Cd Length: 112  Bit Score: 41.29  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  30 NHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQeisgltgFDMQRLEVLTVADVMEVKVPKMTEKDDLETLLR- 108
Cdd:cd04603   10 NEPLREIIKKITELNARAIVIVNNNMSVLGQITVSDLLE-------IGPSQYETLTAYDLILVPLIRVNCDAPITDLLRk 82

                         90       100
                 ....*....|....*....|....*....
gi 508167908 109 -RLVNEPFLPYVDQNNVFLGIFTRKAILK 136
Cdd:cd04603   83 fRETDPPIIAVIDDESKFIGTIYERELLK 111
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 22-68 3.11e-05

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 41.08  E-value: 3.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 508167908  22 ANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQ 68
Cdd:cd02205   67 PDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
6-70 3.88e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 41.00  E-value: 3.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908   6 VQALLTETEDTFLIPAA-----NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEI 70
Cdd:COG0517   54 RRALAAEGKDLLDTPVSevmtrPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKAL 123
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 23-137 7.79e-05

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 39.82  E-value: 7.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDsEDHLVGLISLADIMQEISgltgfdmQRLEVLTVADVMEVKVPKMTEKDD 102
Cdd:cd04588    3 DLITLKPDATIKDAAKLLSENNIHGAPVVD-DGKLVGIVTLTDIAKALA-------EGKENAKVKDIMTKDVITIDKDEK 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 508167908 103 LETLLRRLVNEP--FLPYVDQNNVFLGIFTRKAILKS 137
Cdd:cd04588   75 IYDAIRLMNKHNigRLIVVDDNGKPVGIITRTDILKV 111
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 23-66 9.18e-05

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


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 38.26  E-value: 9.18e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 508167908    23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADI 66
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 23-140 1.20e-04

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 41.22  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908   23 NVATLLYNHPLEHAMLILTNVGYSKIPVLDsEDHLVGLISLADImqeisgltgfDMQRLEVLTVADVM----EVKVPKMT 98
Cdd:pfam00478  89 DPVTLSPDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDL----------RFETDLSQPVSEVMtkenLVTAPEGT 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 508167908   99 EKDDLETLLRRLVNEpFLPYVDQNNVFLGIFTRKAILKSVNH 140
Cdd:pfam00478 158 TLEEAKEILHKHKIE-KLPVVDDNGRLVGLITIKDIEKAKEY 198
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 6-71 1.42e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.43  E-value: 1.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508167908   6 VQALLTETEDTFLIPAA-----NVATLLYNHPLEHAMLILTNVGYSKIPVLDsEDHLVGLISLADIMQEIS 71
Cdd:COG2905   52 RRRVLAEGLDPLDTPVSevmtrPPITVSPDDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRALS 121
CBS_pair_ABC_OpuCA_assoc cd04582
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 32-134 2.87e-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: 341359 [Multi-domain]  Cd Length: 111  Bit Score: 38.52  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  32 PLEHAMLILTNVGYSKIPVLDSEDHLVGLISladiMQEISGLTGfdmqrlevlTVADVMEVKVPKMTEKDDLETLLRRLV 111
Cdd:cd04582   15 PLSDALGIMDDADSRYLVVVDADGRPLGYVT----RRDARGASG---------TCGDFAHPFKATVPVDENLRVVLSRMY 81

                         90       100
                 ....*....|....*....|....*
gi 508167908 112 --NEPFLPYVDQNNVFLGIFTRKAI 134
Cdd:cd04582   82 ehNTSWLPVVDEDGRYAGEVTQDSI 106
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
47-130 6.82e-04

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 38.89  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  47 KIPVLDSEDHLVGLISLADIMqeisgltgfdMQRLEVlTVADVMEVKVPKMTEKDDLETLLRRLVNEPF--LPYVDQNNV 124
Cdd:COG2239  167 YIYVVDDDGRLVGVVSLRDLL----------LADPDT-KVSDIMDTDVISVPADDDQEEVARLFERYDLlaLPVVDEEGR 235


                 ....*.
gi 508167908 125 FLGIFT 130
Cdd:COG2239  236 LVGIIT 241
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 22-135 7.15e-04

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 37.70  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  22 ANVATLLYNHPLEHAMLILTNVGYSKIPVLDSEDhLVGLISLADIMQEISGLTGF----DMQRLEVLT--VADVMEVKVP 95
Cdd:cd17778    8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK-LVGIVTAMDIVKYFGSHEAKkrltTGDIDEAYStpVEEIMSKEVV 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 508167908  96 KMTEKDDLETLLRRLV--NEPFLPYVDQNNVFLGIFTRKAIL 135
Cdd:cd17778   87 TIEPDADIAEAARLMIkkNVGSLLVVDDEGELKGIITERDVL 128
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 50-135 7.25e-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: 37.11  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  50 VLDSEDHLVGLISLADImqeisgltgfDMQRLEVLTVADVMEVKVPKMTEKDDLETLLRRLVNE--PFLPYVDQNNVFLG 127
Cdd:cd04583   30 VVDKDNVLLGIVDIEDI----------NRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDRILKRglKYVPVVDEQGRLVG 99


                 ....*...
gi 508167908 128 IFTRKAIL 135
Cdd:cd04583  100 LVTRASLV 107
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 86-140 1.34e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 35.27  E-value: 1.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 508167908   86 VADVMEVKVPKMTEKDDLETLLRRLVNEPF--LPYVDQNNVFLGIFTRKAILKSVNH 140
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGIsrLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 48-130 1.59e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. 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: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 36.54  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  48 IPVLDSEDHLVGLISLADIMqeisgltgfdMQRLEVLtVADVMEVKVPKMTEKDDLETLLRR-----LVNepfLPYVDQN 122
Cdd:cd04606   40 IYVVDEDRRLLGVVSLRDLL----------LADPDTK-VSDIMDTDVISVSADDDQEEVARLfakydLLA---LPVVDEE 105


                 ....*...
gi 508167908 123 NVFLGIFT 130
Cdd:cd04606  106 GRLVGIIT 113
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 46-137 1.73e-03

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


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 36.68  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  46 SKIPVLDSEDHLVGLISLADIM--QEISGL---------------TGFDMQRLEVLT----VADVMEVKVPKMTEKDDLE 104
Cdd:cd17789   27 TGLPVIDEDWRLVGVVSDYDLLalDSISGRsqtdnnfppadstwkTFNEVQKLLSKTngkvVGDVMTPSPLVVREKTNLE 106

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 508167908 105 TLLRRLVNEPF--LPYVDQNNVFLGIFTRKAILKS 137
Cdd:cd17789  107 DAARILLETKFrrLPVVDSDGKLVGIITRGNVVRA 141
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 32-136 2.19e-03

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: 35.79  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  32 PLEHAMLILTNVGYSKIPVLDSEDHLVGLISLADIMQEISGLtgfdMQRLEVLTV--ADVMEVKVPKMtekddLETLLRR 109
Cdd:cd04597   15 SIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIARTVDYI----MTKDNLIVFkeDDYLDEVKEIM-----LNTNFRN 85

                         90       100
                 ....*....|....*....|....*..
gi 508167908 110 lvnepfLPYVDQNNVFLGIFTRKAILK 136
Cdd:cd04597   86 ------YPVVDENNKFLGTISRKHLIN 106
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 50-106 3.24e-03

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


Pssm-ID: 341398 [Multi-domain]  Cd Length: 133  Bit Score: 35.62  E-value: 3.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 508167908  50 VLDSEDHLVGLISLADIMQE--ISGLTGFDMQRLEVLtVADVmevkvpkMTEKDDLETL 106
Cdd:cd04640   33 VVDANNRVIGLITARDILGEkpLKIVQERGIPREELL-VADV-------MTPRDKLEAL 83
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 44-136 5.63e-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: 35.01  E-value: 5.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  44 GYSKIPVLDsEDHLVGLISLADImqeISGLTGFDMQR-------------LEVLTVADVMEVKVPKMTEKDDLETLLRRL 110
Cdd:cd17777   32 GIRRLVVVD-ENKLEGILSARDL---VSYLGGGCLFKivesrhqgdlysaLNREVVETIMTPNPVYVYEDSDLIEALTIM 107

                         90       100
                 ....*....|....*....|....*...
gi 508167908 111 V--NEPFLPYVDQNNVFLGIFTRKAILK 136
Cdd:cd17777  108 VtrGIGSLPVVDRDGRPVGIVTERDLVL 135
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 48-66 6.28e-03

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: 34.70  E-value: 6.28e-03
                         10
                 ....*....|....*....
gi 508167908  48 IPVLDSEDHLVGLISLADI 66
Cdd:cd04622   94 LPVVDDDGRLVGIVSLGDL 112
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 23-138 7.35e-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: 34.90  E-value: 7.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  23 NVATLLYNHPLEHAMLILTNVGYSKIPVLdSEDHLVGLISLADIMQEISGLTGFDmqRLEVLTVADVMEVKV-------P 95
Cdd:cd04631    9 NVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIMRYLGSGEAFE--KLKTGNIHEVLNVPIssimkrdI 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 508167908  96 KMTEKD-DLETLLRRLVNEPF--LPYVDqNNVFLGIFTRKAILKSV 138
Cdd:cd04631   86 ITTTPDtDLGEAAELMLEKNIgaLPVVD-DGKLVGIITERDILRAI 130
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 26-137 7.59e-03

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 35.72  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  26 TLLYNHPLEHAMLILTNVGYSKIPVLDSEDH---LVGLISLADI--MQEISGLTGFDMQRLEVLTV-------ADVMEVK 93
Cdd:PTZ00314 108 VLSPNHTVADVLEIKEKKGFSSILITVDGKVggkLLGIVTSRDIdfVKDKSTPVSEVMTPREKLVVgntpislEEANEVL 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 508167908  94 VPKMTEKddletllrrlvnepfLPYVDQNNVFLGIFTRKAILKS 137
Cdd:PTZ00314 188 RESRKGK---------------LPIVNDNGELVALVSRSDLKKN 216
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 20-137 8.79e-03

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


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 34.08  E-value: 8.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508167908  20 PAANVATLLynhpleHAMLILTNVGYskiPVLDSeDHLVGLISLADImQEISGLTGFDMqrlevlTVADVMEVKVPKMTE 99
Cdd:cd04801   12 PEMTVSELL------DRMFEEKHLGY---PVVEN-GRLVGIVTLEDI-RKVPEVEREAT------RVRDVMTKDVITVSP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 508167908 100 KDDLETLLRRLVNEPF--LPYVDqNNVFLGIFTRKAILKS 137
Cdd:cd04801   75 DADAMEALKLMSQNNIgrLPVVE-DGELVGIISRTDLMRA 113
 
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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