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Conserved domains on  [gi|15218643|ref|NP_176711|]
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Cystathionine beta-synthase (CBS) family protein [Arabidopsis thaliana]

Protein Classification

CBS domain-containing protein( domain architecture ID 10115311)

CBS (cystathione beta synthase) domain-containing protein may bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet; similar to Arabidopsis thaliana CBS domain-containing protein CBSX6

CATH:  3.10.580.10
PubMed:  16275737|24161944|21958115
SCOP:  4000247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 23-134 1.45e-09

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: 55.33  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218643  23 FYETETVESAIRAIGESTECGIPVWRkrttpslpgfvensemRQQRFVGILNSLDIVAFLAKteclqEEKAMKIPVSEVV 102
Cdd:cd02205   7 VDPDTTVREALELMAENGIGALPVVD----------------DDGKLVGIVTERDILRALVE-----GGLALDTPVAEVM 65

                        90       100       110
                ....*....|....*....|....*....|...
gi 15218643 103 SPDntlLKQVDPGTRLIDALEMMKQ-GVRRLLV 134
Cdd:cd02205  66 TPD---VITVSPDTDLEEALELMLEhGIRRLPV 95
COG2905 super family cl34516
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 354-406 7.93e-03

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


The actual alignment was detected with superfamily member COG2905:

Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 36.35  E-value: 7.93e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15218643 354 PLTCKTSSSLAAVMAQMLSHRATHVWVTEadsDDVLVGVVGYGEILTAVTKQP 406
Cdd:COG2905  75 PITVSPDDSLAEALELMEEHRIRHLPVVD---DGKLVGIVSITDLLRALSEEL 124
 
Name Accession Description Interval E-value
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 23-134 1.45e-09

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: 55.33  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218643  23 FYETETVESAIRAIGESTECGIPVWRkrttpslpgfvensemRQQRFVGILNSLDIVAFLAKteclqEEKAMKIPVSEVV 102
Cdd:cd02205   7 VDPDTTVREALELMAENGIGALPVVD----------------DDGKLVGIVTERDILRALVE-----GGLALDTPVAEVM 65

                        90       100       110
                ....*....|....*....|....*....|...
gi 15218643 103 SPDntlLKQVDPGTRLIDALEMMKQ-GVRRLLV 134
Cdd:cd02205  66 TPD---VITVSPDTDLEEALELMLEhGIRRLPV 95
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
10-134 6.55e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.80  E-value: 6.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218643  10 VGDLTVGKPEMVEfyETETVESAIRAIGESTECGIPVwrkrttpslpgfVENsemrqQRFVGILNSLDIVAFLAKTECLq 89
Cdd:COG2524  88 VKDIMTKDVITVS--PDTTLEEALELMLEKGISGLPV------------VDD-----GKLVGIITERDLLKALAEGRDL- 147

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15218643  90 eekaMKIPVSEVVSPDntlLKQVDPGTRLIDALEMM-KQGVRRLLV 134
Cdd:COG2524 148 ----LDAPVSDIMTRD---VVTVSEDDSLEEALRLMlEHGIGRLPV 186
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 354-406 7.93e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 36.35  E-value: 7.93e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15218643 354 PLTCKTSSSLAAVMAQMLSHRATHVWVTEadsDDVLVGVVGYGEILTAVTKQP 406
Cdd:COG2905  75 PITVSPDDSLAEALELMEEHRIRHLPVVD---DGKLVGIVSITDLLRALSEEL 124
 
Name Accession Description Interval E-value
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 23-134 1.45e-09

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: 55.33  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218643  23 FYETETVESAIRAIGESTECGIPVWRkrttpslpgfvensemRQQRFVGILNSLDIVAFLAKteclqEEKAMKIPVSEVV 102
Cdd:cd02205   7 VDPDTTVREALELMAENGIGALPVVD----------------DDGKLVGIVTERDILRALVE-----GGLALDTPVAEVM 65

                        90       100       110
                ....*....|....*....|....*....|...
gi 15218643 103 SPDntlLKQVDPGTRLIDALEMMKQ-GVRRLLV 134
Cdd:cd02205  66 TPD---VITVSPDTDLEEALELMLEhGIRRLPV 95
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
10-134 6.55e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.80  E-value: 6.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218643  10 VGDLTVGKPEMVEfyETETVESAIRAIGESTECGIPVwrkrttpslpgfVENsemrqQRFVGILNSLDIVAFLAKTECLq 89
Cdd:COG2524  88 VKDIMTKDVITVS--PDTTLEEALELMLEKGISGLPV------------VDD-----GKLVGIITERDLLKALAEGRDL- 147

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15218643  90 eekaMKIPVSEVVSPDntlLKQVDPGTRLIDALEMM-KQGVRRLLV 134
Cdd:COG2524 148 ----LDAPVSDIMTRD---VVTVSEDDSLEEALRLMlEHGIGRLPV 186
CBS COG0517
CBS domain [Signal transduction mechanisms];
66-134 1.70e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 44.09  E-value: 1.70e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218643  66 QQRFVGILNSLDIVAFLAKteclQEEKAMKIPVSEVVSPDntlLKQVDPGTRLIDALEMMKQ-GVRRLLV 134
Cdd:COG0517  41 DGKLVGIVTDRDLRRALAA----EGKDLLDTPVSEVMTRP---PVTVSPDTSLEEAAELMEEhKIRRLPV 103
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 66-134 8.57e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 42.12  E-value: 8.57e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218643  66 QQRFVGILNSLDIVAFLAktecLQEEKAMKIPVSEVVSPDntlLKQVDPGTRLIDALEMM-KQGVRRLLV 134
Cdd:COG2905  39 DGRLVGIITDRDLRRRVL----AEGLDPLDTPVSEVMTRP---PITVSPDDSLAEALELMeEHRIRHLPV 101
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
65-134 4.63e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.23  E-value: 4.63e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15218643  65 RQQRFVGILNSLDIVAFLAKTECLQ-EEKAMKIPVSEVVSPDntlLKQVDPGTRLIDALEMM-KQGVRRLLV 134
Cdd:COG3448  41 EDGRLVGIVTERDLLRALLPDRLDElEERLLDLPVEDVMTRP---VVTVTPDTPLEEAAELMlEHGIHRLPV 109
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 70-134 1.77e-03

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 37.89  E-value: 1.77e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15218643  70 VGILNSLDIVAFLAkteclqEEKAMKIPVSEVVSPDntlLKQVDPGTRLIDALEMMKQ-GVRRLLV 134
Cdd:cd09836  39 VGIVTERDIVRAVA------EGIDLDTPVEEIMTKN---LVTVSPDESIYEAAELMREhNIRHLPV 95
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 70-134 2.20e-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: 37.91  E-value: 2.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15218643  70 VGILNSLDIV-AFLAKteclqEEKAMKIPVSEVVSPDNTLLKQVDPgtrLIDALEMMKQ-GVRRLLV 134
Cdd:cd17775  39 VGIVTDRDIVvEVVAK-----GLDPKDVTVGDIMSADLITAREDDG---LFEALERMREkGVRRLPV 97
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 354-406 7.93e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 36.35  E-value: 7.93e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15218643 354 PLTCKTSSSLAAVMAQMLSHRATHVWVTEadsDDVLVGVVGYGEILTAVTKQP 406
Cdd:COG2905  75 PITVSPDDSLAEALELMEEHRIRHLPVVD---DGKLVGIVSITDLLRALSEEL 124
 
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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