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Conserved domains on  [gi|639315271|ref|WP_024594284|]
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MULTISPECIES: CBS domain-containing protein [Pseudoalteromonas]

Protein Classification

CBS domain-containing protein( domain architecture ID 66840)

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

PubMed:  24161944

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 41-167 7.63e-24

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


The actual alignment was detected with superfamily member cd04640:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 133  Bit Score: 91.09  E-value: 7.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  41 FTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQSSKITIIAERLNTPRSEVSLRDIMTPISRLT 120
Cdd:cd04640    2 FRRVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPLKIVQERGIPREELLVADVMTPRDKLE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639315271 121 GVSMQSLSYACIGDALQTMEHQGVMFLLV----TTASSEICGLISARQIAK 167
Cdd:cd04640   82 ALDYEDVAHARVGDVVETLKASGRQHALVvdrdEDGRQEVRGIFSASQIAR 132
 
Name Accession Description Interval E-value
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 41-167 7.63e-24

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: 91.09  E-value: 7.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  41 FTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQSSKITIIAERLNTPRSEVSLRDIMTPISRLT 120
Cdd:cd04640    2 FRRVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPLKIVQERGIPREELLVADVMTPRDKLE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639315271 121 GVSMQSLSYACIGDALQTMEHQGVMFLLV----TTASSEICGLISARQIAK 167
Cdd:cd04640   82 ALDYEDVAHARVGDVVETLKASGRQHALVvdrdEDGRQEVRGIFSASQIAR 132
CBS COG0517
CBS domain [Signal transduction mechanisms];
38-169 7.21e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 54.49  E-value: 7.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  38 VNNFTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADlqsskITIIAERLNTPRSEVSLRDIMT--P 115
Cdd:COG0517    3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRD-----LRRALAAEGKDLLDTPVSEVMTrpP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 639315271 116 ISRLTGVSmqslsyacIGDALQTMEHQGVMFLLVTTASSEICGLISARQIAKTL 169
Cdd:COG0517   78 VTVSPDTS--------LEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKAL 123
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 38-88 3.91e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 37.19  E-value: 3.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 639315271   38 VNNFTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADL 88
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 45-172 5.33e-03

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 36.95  E-value: 5.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  45 TPIRAEHTTTITDALKQVSAQQSDFVLVTD---ENQKLIGLVSSADlqsskITIIAERlntprsEVSLRDIMTPISRLTG 121
Cdd:PLN02274 109 DPVVKSPSSTISSLDELKASRGFSSVCVTEtgtMGSKLLGYVTKRD-----WDFVNDR------ETKLSEVMTSDDDLVT 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639315271 122 VSmQSLSYACIGDALqtmEHQGVMFLLVTTASSEICGLISARQIAKTLHIP 172
Cdd:PLN02274 178 AP-AGIDLEEAEAVL---KDSKKGKLPLVNEDGELVDLVTRTDVKRVKGYP 224
 
Name Accession Description Interval E-value
CBS_pair_proteobact cd04640
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 41-167 7.63e-24

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: 91.09  E-value: 7.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  41 FTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQSSKITIIAERLNTPRSEVSLRDIMTPISRLT 120
Cdd:cd04640    2 FRRVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILGEKPLKIVQERGIPREELLVADVMTPRDKLE 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639315271 121 GVSMQSLSYACIGDALQTMEHQGVMFLLV----TTASSEICGLISARQIAK 167
Cdd:cd04640   82 ALDYEDVAHARVGDVVETLKASGRQHALVvdrdEDGRQEVRGIFSASQIAR 132
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 46-170 3.38e-10

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: 55.29  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  46 PIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQSSkitIIAERLNTPRSEVSlrDIMTPisRLTGVSMQ 125
Cdd:cd17781    4 ALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARR---VVASGLDPRSTLVS--SVMTP--NPLCVTMD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 639315271 126 SLsyacIGDALQTMEHQGVMFLLVTTASSEICGLISarqIAKTLH 170
Cdd:cd17781   77 TS----ATDALDLMVEGKFRHLPVVDDDGDVVGVLD---ITKCLY 114
CBS COG0517
CBS domain [Signal transduction mechanisms];
38-169 7.21e-10

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 54.49  E-value: 7.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  38 VNNFTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADlqsskITIIAERLNTPRSEVSLRDIMT--P 115
Cdd:COG0517    3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRD-----LRRALAAEGKDLLDTPVSEVMTrpP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 639315271 116 ISRLTGVSmqslsyacIGDALQTMEHQGVMFLLVTTASSEICGLISARQIAKTL 169
Cdd:COG0517   78 VTVSPDTS--------LEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKAL 123
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 44-169 2.05e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 53.29  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  44 KTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLqssKITIIAERLNTprSEVSLRDIMTpiSRLTGVS 123
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDL---RRRVLAEGLDP--LDTPVSEVMT--RPPITVS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 639315271 124 MQSLsyacIGDALQTMEHQGVMFLLVTTAsSEICGLISARQIAKTL 169
Cdd:COG2905   80 PDDS----LAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRAL 120
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
44-170 1.52e-08

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 51.02  E-value: 1.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  44 KTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQSSKITIIAERLNTPRSEVSLRDIMTP----ISRL 119
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDLPVEDVMTRpvvtVTPD 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639315271 120 TGVSmqslsyacigDALQTMEHQGVMFLLVTTASSEICGLISARQIAKTLH 170
Cdd:COG3448   90 TPLE----------EAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 46-167 1.42e-07

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: 48.01  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  46 PIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLqsskITIIAERLNTPrsEVSLRDIMTPiSRLTGVSMQ 125
Cdd:cd02205    4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDI----LRALVEGGLAL--DTPVAEVMTP-DVITVSPDT 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 639315271 126 SLSyacigDALQTMEHQGVMFLLVTTASSEICGLISARQIAK 167
Cdd:cd02205   77 DLE-----EALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
38-169 2.56e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 48.73  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  38 VNNFTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENqKLIGLVSSADLqsskitIIAERLNTPRSEVSLRDIMTPis 117
Cdd:COG2524   88 VKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDG-KLVGIITERDL------LKALAEGRDLLDAPVSDIMTR-- 158

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639315271 118 RLTGVSmqslSYACIGDALQTMEHQGVMFLLVTTASSEICGLISARQIAKTL 169
Cdd:COG2524  159 DVVTVS----EDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
41-170 3.59e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 41.82  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  41 FTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADlqsskitIIAERLNTPrsevsLRDIMT--PISR 118
Cdd:COG4109   22 MTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKD-------ILGKDDDTP-----IEDVMTknPITV 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639315271 119 LTGVSmqslsyacIGDALQTMEHQGVMFLLVTTASSEICGLISARQIAKTLH 170
Cdd:COG4109   90 TPDTS--------LASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQ 133
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 41-163 5.13e-05

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


Pssm-ID: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 41.15  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  41 FTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQsSKITIIAERLNTPRSEVSLRDimtPISrlt 120
Cdd:cd17771    1 LIRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLL-SRVALPQIDLDAPISEVMTPD---PVR--- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 639315271 121 gVSMQSLSYacigDALQTMEHQGVMFLLVtTASSEICGLISAR 163
Cdd:cd17771   74 -LPPSASAF----EAALLMAEHGFRHVCV-VDNGRLVGVVSER 110
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 44-170 6.73e-05

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 40.58  E-value: 6.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  44 KTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLqsskITIIAERLNTprsEVSLRDIMT--PISRLTG 121
Cdd:cd09836    3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDI----VRAVAEGIDL---DTPVEEIMTknLVTVSPD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 639315271 122 VSmqslsyacIGDALQTMEHQGVMFLLVTTASSEICGLISARQIAKTLH 170
Cdd:cd09836   76 ES--------IYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 52-167 7.91e-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: 40.47  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  52 TTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQsskitiIAERLNTPrsevsLRDIMTPISRLT----GVSMQsl 127
Cdd:cd04601   10 DATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIR------FETDLSTP-----VSEVMTPDERLVtapeGITLE-- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 639315271 128 syacigDALQTMEHQGVMFLLVTTASSEICGLISARQIAK 167
Cdd:cd04601   77 ------EAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK 110
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 45-165 3.26e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; 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: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 38.77  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  45 TPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQSSkitIIAERLNTprSEVSLRDIMTPISRLTGVSM 124
Cdd:cd17782    3 PPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVLR---VLAAGLDP--ATTSVVRVMTPNPETAPPST 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 639315271 125 QslsyacIGDALQTMEHQGVMFLLVTTASSEICGLISARQI 165
Cdd:cd17782   78 T------ILDALHKMHEGKFLNLPVVDDEGEIVGLVDVLQL 112
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 38-88 3.91e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 37.19  E-value: 3.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 639315271   38 VNNFTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADL 88
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
38-88 8.64e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.97  E-value: 8.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639315271  38 VNNFTQKTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADL 88
Cdd:COG4109   78 IEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 70-169 2.71e-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: 35.98  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  70 VLVTDENQKLIGLVSSADLQsskITIIAERLNTprSEVSLRDIMTPisRLTGVSmqslSYACIGDALQTMEHQGVMFLLV 149
Cdd:cd17775   29 VVVVEEDGKPVGIVTDRDIV---VEVVAKGLDP--KDVTVGDIMSA--DLITAR----EDDGLFEALERMREKGVRRLPV 97

                         90       100
                 ....*....|....*....|
gi 639315271 150 TTASSEICGLISARQIAKTL 169
Cdd:cd17775   98 VDDDGELVGIVTLDDILELL 117
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 16-88 3.39e-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: 35.68  E-value: 3.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639315271  16 VIASTFADDQPLIDLSSPAlkmvnnftqktPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADL 88
Cdd:cd02205   50 LVEGGLALDTPVAEVMTPD-----------VITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 45-172 5.33e-03

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 36.95  E-value: 5.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  45 TPIRAEHTTTITDALKQVSAQQSDFVLVTD---ENQKLIGLVSSADlqsskITIIAERlntprsEVSLRDIMTPISRLTG 121
Cdd:PLN02274 109 DPVVKSPSSTISSLDELKASRGFSSVCVTEtgtMGSKLLGYVTKRD-----WDFVNDR------ETKLSEVMTSDDDLVT 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639315271 122 VSmQSLSYACIGDALqtmEHQGVMFLLVTTASSEICGLISARQIAKTLHIP 172
Cdd:PLN02274 178 AP-AGIDLEEAEAVL---KDSKKGKLPLVNEDGELVDLVTRTDVKRVKGYP 224
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 44-160 5.71e-03

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: 35.19  E-value: 5.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639315271  44 KTPIRAEHTTTITDALKQVSAQQSDFVLVTDENQKLIGLVSSADLQSSKitiiaerlntpRSEVSLRDIMTPisRLTGVS 123
Cdd:cd04583    2 TNPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNY-----------RKAKKVGEIMER--DVFTVK 68

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 639315271 124 MQSLsyacIGDALQTMEHQGVMFLLVTTASSEICGLI 160
Cdd:cd04583   69 EDSL----LRDTVDRILKRGLKYVPVVDEQGRLVGLV 101
 
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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