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Conserved domains on  [gi|662236737|ref|NP_001284529|]
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hsp70-binding protein 1 isoform 1 [Homo sapiens]

Protein Classification

Hsp70-binding protein( domain architecture ID 10554333)

Hsp70-binding protein such as the Hsp70 nucleotide exchange factor FES1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fes1 pfam08609
Nucleotide exchange factor Fes1; Fes1 is a cytosolic homolog of Sls1, an ER protein which has ...
 91-185 1.09e-08

Nucleotide exchange factor Fes1; Fes1 is a cytosolic homolog of Sls1, an ER protein which has nucleotide exchange factor activity. Fes1 in yeast has been shown to bind to the molecular chaperone Hsp70 and has adenyl-nucleotide exchange factor activity.


:

Pssm-ID: 462534  Cd Length: 89  Bit Score: 51.85  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236737   91 LQGLLQMAI--------TAGSEEPDPPPEPMSEERRQWLQEAMsaafrGQREEVEQMKSCLRVLSQPmpptageaeqAAD 162
Cdd:pfam08609   1 LNGLLKWAIenpgaasdSTPLPEAASEAPAPRDLDPEILDALL-----GGPSDAELMKEAMAVLNDP----------EVS 65

                          90       100
                  ....*....|....*....|...
gi 662236737  163 QQEREGALELLADLCENMDNAAD 185
Cdd:pfam08609  66 LEDKLIALDNLEQLVESIDNANN 88
 
Name Accession Description Interval E-value
Fes1 pfam08609
Nucleotide exchange factor Fes1; Fes1 is a cytosolic homolog of Sls1, an ER protein which has ...
 91-185 1.09e-08

Nucleotide exchange factor Fes1; Fes1 is a cytosolic homolog of Sls1, an ER protein which has nucleotide exchange factor activity. Fes1 in yeast has been shown to bind to the molecular chaperone Hsp70 and has adenyl-nucleotide exchange factor activity.


Pssm-ID: 462534  Cd Length: 89  Bit Score: 51.85  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236737   91 LQGLLQMAI--------TAGSEEPDPPPEPMSEERRQWLQEAMsaafrGQREEVEQMKSCLRVLSQPmpptageaeqAAD 162
Cdd:pfam08609   1 LNGLLKWAIenpgaasdSTPLPEAASEAPAPRDLDPEILDALL-----GGPSDAELMKEAMAVLNDP----------EVS 65

                          90       100
                  ....*....|....*....|...
gi 662236737  163 QQEREGALELLADLCENMDNAAD 185
Cdd:pfam08609  66 LEDKLIALDNLEQLVESIDNANN 88
 
Name Accession Description Interval E-value
Fes1 pfam08609
Nucleotide exchange factor Fes1; Fes1 is a cytosolic homolog of Sls1, an ER protein which has ...
 91-185 1.09e-08

Nucleotide exchange factor Fes1; Fes1 is a cytosolic homolog of Sls1, an ER protein which has nucleotide exchange factor activity. Fes1 in yeast has been shown to bind to the molecular chaperone Hsp70 and has adenyl-nucleotide exchange factor activity.


Pssm-ID: 462534  Cd Length: 89  Bit Score: 51.85  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 662236737   91 LQGLLQMAI--------TAGSEEPDPPPEPMSEERRQWLQEAMsaafrGQREEVEQMKSCLRVLSQPmpptageaeqAAD 162
Cdd:pfam08609   1 LNGLLKWAIenpgaasdSTPLPEAASEAPAPRDLDPEILDALL-----GGPSDAELMKEAMAVLNDP----------EVS 65

                          90       100
                  ....*....|....*....|...
gi 662236737  163 QQEREGALELLADLCENMDNAAD 185
Cdd:pfam08609  66 LEDKLIALDNLEQLVESIDNANN 88
 
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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