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Conserved domains on  [gi|66773038|ref|NP_060383|]
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hsp90 co-chaperone Cdc37-like 1 [Homo sapiens]

Protein Classification

CDC37_N and CDC37_M domain-containing protein( domain architecture ID 10263481)

CDC37_N and CDC37_M domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC37_M smart01070
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 138-282 4.50e-60

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 whose function is unclear.


:

Pssm-ID: 215010  Cd Length: 155  Bit Score: 189.90  E-value: 4.50e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773038    138 KSFINQDKRKDTE-DEDKSESFMQKYEQKIRHFGMLS--RWDDSQRFLSDHPYLVCEETAKYLILWCFHLEAEKKGALME 214
Cdd:smart01070   4 TSSKNPPSAPSEEeDEIDDKDFVLKLEPATKKFGMIPagDYDDSQKFLSEHPHIVSEETADALVMWAFDLELEGKEALME 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773038    215 QIAHQAVVMQFIMEMAKNCNVDPRGCFRLFFQKAKAE----EEGYFEAFKNELEAFKSRVRLYSQSQSFQPM 282
Cdd:smart01070  84 QVAHQAILMQYILELAKSLKVDPRNCVRLFFQKIKTPshpaKEGFLEDVQSEFEHIKTRVRIIAQEQAEEAM 155
CDC37_N super family cl03951
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 71-139 4.17e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain pfam08565. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


The actual alignment was detected with superfamily member smart01071:

Pssm-ID: 446243 [Multi-domain]  Cd Length: 154  Bit Score: 37.40  E-value: 4.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773038     71 LAEAQQKLGSLALHNSESLDQEHAKAQTAVSELRQREEEWRQKEEALVQREKMCLWSTDaiSKDVFNKS 139
Cdd:smart01071  88 LAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKLDELEKEEKKKIWSVD--THTGFDKS 154
 
Name Accession Description Interval E-value
CDC37_M smart01070
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 138-282 4.50e-60

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 whose function is unclear.


Pssm-ID: 215010  Cd Length: 155  Bit Score: 189.90  E-value: 4.50e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773038    138 KSFINQDKRKDTE-DEDKSESFMQKYEQKIRHFGMLS--RWDDSQRFLSDHPYLVCEETAKYLILWCFHLEAEKKGALME 214
Cdd:smart01070   4 TSSKNPPSAPSEEeDEIDDKDFVLKLEPATKKFGMIPagDYDDSQKFLSEHPHIVSEETADALVMWAFDLELEGKEALME 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773038    215 QIAHQAVVMQFIMEMAKNCNVDPRGCFRLFFQKAKAE----EEGYFEAFKNELEAFKSRVRLYSQSQSFQPM 282
Cdd:smart01070  84 QVAHQAILMQYILELAKSLKVDPRNCVRLFFQKIKTPshpaKEGFLEDVQSEFEHIKTRVRIIAQEQAEEAM 155
CDC37_M pfam08565
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 169-278 2.56e-17

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain pfam03234, which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 pfam08564 whose function is unclear.


Pssm-ID: 430078  Cd Length: 113  Bit Score: 76.46  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773038   169 FGMLSR--WDDSQRFLSDHPYLVCEETAKYLILWCFHLEAEKKGALMEQIAHQAVVMQFIMEMAkncnvDPRGCFRLFFQ 246
Cdd:pfam08565   2 FAKIPSgdYKASEQFLLKHPEILSEQQKDALLMEAFDAQLEGKTKYARQCVHQSLLLQYCRQLD-----GRINGVKLFFK 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 66773038   247 KAKAEEEGYFEAFKNELEAF----KSRVRLYSQSQS 278
Cdd:pfam08565  77 RITTKDHQAKKLFLDDVQSTynhiKTRAEEIKQEQA 112
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 71-139 4.17e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 37.40  E-value: 4.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773038     71 LAEAQQKLGSLALHNSESLDQEHAKAQTAVSELRQREEEWRQKEEALVQREKMCLWSTDaiSKDVFNKS 139
Cdd:smart01071  88 LAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKLDELEKEEKKKIWSVD--THTGFDKS 154
 
Name Accession Description Interval E-value
CDC37_M smart01070
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 138-282 4.50e-60

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 whose function is unclear.


Pssm-ID: 215010  Cd Length: 155  Bit Score: 189.90  E-value: 4.50e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773038    138 KSFINQDKRKDTE-DEDKSESFMQKYEQKIRHFGMLS--RWDDSQRFLSDHPYLVCEETAKYLILWCFHLEAEKKGALME 214
Cdd:smart01070   4 TSSKNPPSAPSEEeDEIDDKDFVLKLEPATKKFGMIPagDYDDSQKFLSEHPHIVSEETADALVMWAFDLELEGKEALME 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66773038    215 QIAHQAVVMQFIMEMAKNCNVDPRGCFRLFFQKAKAE----EEGYFEAFKNELEAFKSRVRLYSQSQSFQPM 282
Cdd:smart01070  84 QVAHQAILMQYILELAKSLKVDPRNCVRLFFQKIKTPshpaKEGFLEDVQSEFEHIKTRVRIIAQEQAEEAM 155
CDC37_M pfam08565
Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of ...
 169-278 2.56e-17

Cdc37 Hsp90 binding domain; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domains corresponds to the Hsp90 chaperone (Heat shocked protein 90) binding domain of Cdc37. It is found between the N terminal Cdc37 domain pfam03234, which is predominantly involved in kinase binding, and the C terminal domain of Cdc37 pfam08564 whose function is unclear.


Pssm-ID: 430078  Cd Length: 113  Bit Score: 76.46  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66773038   169 FGMLSR--WDDSQRFLSDHPYLVCEETAKYLILWCFHLEAEKKGALMEQIAHQAVVMQFIMEMAkncnvDPRGCFRLFFQ 246
Cdd:pfam08565   2 FAKIPSgdYKASEQFLLKHPEILSEQQKDALLMEAFDAQLEGKTKYARQCVHQSLLLQYCRQLD-----GRINGVKLFFK 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 66773038   247 KAKAEEEGYFEAFKNELEAF----KSRVRLYSQSQS 278
Cdd:pfam08565  77 RITTKDHQAKKLFLDDVQSTynhiKTRAEEIKQEQA 112
CDC37_N smart01071
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
 71-139 4.17e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 198139 [Multi-domain]  Cd Length: 154  Bit Score: 37.40  E-value: 4.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66773038     71 LAEAQQKLGSLALHNSESLDQEHAKAQTAVSELRQREEEWRQKEEALVQREKMCLWSTDaiSKDVFNKS 139
Cdd:smart01071  88 LAELQDQLKKELEEANGDSEGLLEELKKHRDKLKKEQKELRKKLDELEKEEKKKIWSVD--THTGFDKS 154
 
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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