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Conserved domains on  [gi|6319691|ref|NP_009773|]
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Sds24p [Saccharomyces cerevisiae S288C]

Protein Classification

CBS and CBS_pair domain-containing protein( domain architecture ID 11424839)

CBS and CBS_pair domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG2524 super family cl34478
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
188-331 1.58e-07

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


The actual alignment was detected with superfamily member COG2524:

Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 51.81  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  188 KPVPVGE-MVKltpknPFYKLPENESLSTVMGIL-GSGVHRVAITNEEmtKVKGILSQRRLIKYLWDNarsftslEPLLN 265
Cdd:COG2524  84 LKMKVKDiMTK-----DVITVSPDTTLEEALELMlEKGISGLPVVDDG--KLVGIITERDLLKALAEG-------RDLLD 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319691  266 SSLQDLHigvlniqskptsrQSRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:COG2524 150 APVSDIM-------------TRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
COG3448 super family cl34614
CBS-domain-containing membrane protein [Signal transduction mechanisms];
287-396 5.53e-04

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


The actual alignment was detected with superfamily member COG3448:

Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.23  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  287 SRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV-KHVTRTSQYPLLHKTCRHFISVILNSrgletgkd 365
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLlRALLPDRLDELEERLLDLPVEDVMTR-------- 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 6319691  366 sfPIFHVYPSSSLARTLAKLVATKSHRLWIV 396
Cdd:COG3448  82 --PVVTVTPDTPLEEAAELMLEHGIHRLPVV 110
 
Name Accession Description Interval E-value
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
188-331 1.58e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 51.81  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  188 KPVPVGE-MVKltpknPFYKLPENESLSTVMGIL-GSGVHRVAITNEEmtKVKGILSQRRLIKYLWDNarsftslEPLLN 265
Cdd:COG2524  84 LKMKVKDiMTK-----DVITVSPDTTLEEALELMlEKGISGLPVVDDG--KLVGIITERDLLKALAEG-------RDLLD 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319691  266 SSLQDLHigvlniqskptsrQSRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:COG2524 150 APVSDIM-------------TRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
203-331 5.84e-06

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: 45.31  E-value: 5.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  203 PFYKLPENESLSTVMGILG-SGVHRVAITNEEmTKVKGILSQRRLIKYLwdnarsftsLEPLLNSSLQdlhigVLNIQSK 281
Cdd:cd02205   3 DVVTVDPDTTVREALELMAeNGIGALPVVDDD-GKLVGIVTERDILRAL---------VEGGLALDTP-----VAEVMTP 67
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6319691  282 PtsrqsrVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:cd02205  68 D------VITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
288-334 4.94e-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: 40.96  E-value: 4.94e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6319691     288 RVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDVKHV 334
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
287-396 5.53e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.23  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  287 SRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV-KHVTRTSQYPLLHKTCRHFISVILNSrgletgkd 365
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLlRALLPDRLDELEERLLDLPVEDVMTR-------- 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 6319691  366 sfPIFHVYPSSSLARTLAKLVATKSHRLWIV 396
Cdd:COG3448  82 --PVVTVTPDTPLEEAAELMLEHGIHRLPVV 110
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
287-331 1.05e-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: 37.19  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6319691    287 SRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
 
Name Accession Description Interval E-value
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
188-331 1.58e-07

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 51.81  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  188 KPVPVGE-MVKltpknPFYKLPENESLSTVMGIL-GSGVHRVAITNEEmtKVKGILSQRRLIKYLWDNarsftslEPLLN 265
Cdd:COG2524  84 LKMKVKDiMTK-----DVITVSPDTTLEEALELMlEKGISGLPVVDDG--KLVGIITERDLLKALAEG-------RDLLD 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6319691  266 SSLQDLHigvlniqskptsrQSRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:COG2524 150 APVSDIM-------------TRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
207-331 3.31e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 46.78  E-value: 3.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  207 LPENESLSTVMGIL-GSGVHRVAITNEEMtKVKGILSQRRLIKylwdnaRSFTSLEPLLNSSLQDLHIGvlNIQSKPtsr 285
Cdd:COG3448  15 VSPDTTLREALELMrEHGIRGLPVVDEDG-RLVGIVTERDLLR------ALLPDRLDELEERLLDLPVE--DVMTRP--- 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6319691  286 qsrVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:COG3448  83 ---VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDL 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
203-331 5.84e-06

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: 45.31  E-value: 5.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  203 PFYKLPENESLSTVMGILG-SGVHRVAITNEEmTKVKGILSQRRLIKYLwdnarsftsLEPLLNSSLQdlhigVLNIQSK 281
Cdd:cd02205   3 DVVTVDPDTTVREALELMAeNGIGALPVVDDD-GKLVGIVTERDILRAL---------VEGGLALDTP-----VAEVMTP 67
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 6319691  282 PtsrqsrVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:cd02205  68 D------VITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
288-334 4.94e-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: 40.96  E-value: 4.94e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6319691     288 RVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDVKHV 334
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKA 47
CBS COG0517
CBS domain [Signal transduction mechanisms];
207-331 4.71e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 40.23  E-value: 4.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  207 LPENESLSTVMGILG-SGVHRVAITNEEMtKVKGILSQRRLIKYLWDNARSFTSLEpllnsslqdlhigVLNIQSKPtsr 285
Cdd:COG0517  14 VSPDATVREALELMSeKRIGGLPVVDEDG-KLVGIVTDRDLRRALAAEGKDLLDTP-------------VSEVMTRP--- 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 6319691  286 qsrVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:COG0517  77 ---PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDL 119
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
287-396 5.53e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.23  E-value: 5.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6319691  287 SRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV-KHVTRTSQYPLLHKTCRHFISVILNSrgletgkd 365
Cdd:COG3448  10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLlRALLPDRLDELEERLLDLPVEDVMTR-------- 81
                        90       100       110
                ....*....|....*....|....*....|.
gi 6319691  366 sfPIFHVYPSSSLARTLAKLVATKSHRLWIV 396
Cdd:COG3448  82 --PVVTVTPDTPLEEAAELMLEHGIHRLPVV 110
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
287-331 1.05e-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: 37.19  E-value: 1.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6319691    287 SRVISIQGEEPLIMGLYKMHVERISSIAVIDKQGNLLGNISVTDV 331
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
203-251 2.61e-03

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: 35.95  E-value: 2.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 6319691     203 PFYKLPENESLSTVMGILG-SGVHRVAITNEEmTKVKGILSQRRLIKYLW 251
Cdd:smart00116   1 DVVTVSPDTTLEEALELLReNGIRRLPVVDEE-GRLVGIVTRRDIIKALA 49
 
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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