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Conserved domains on  [gi|1988744664|ref|WP_204301992|]
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Hsp33 family molecular chaperone HslO, partial [Klebsiella pneumoniae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hslO super family cl29487
Hsp33 family molecular chaperone HslO;
1-88 1.01e-46

Hsp33 family molecular chaperone HslO;


The actual alignment was detected with superfamily member PRK00114:

Pssm-ID: 234643  Cd Length: 293  Bit Score: 150.31  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988744664   1 DYIVKALAFDGEIRAYAALTTETVQEAQTRHYTWPTASAAMGRTMTATAMMGAMLKGDQKLTVTVDGQGPIGRIIADANA 80
Cdd:PRK00114    3 DYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDANA 82


                  ....*...
gi 1988744664  81 KGEVRAYV 88
Cdd:PRK00114   83 DGQVRGYV 90
 
Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
1-88 1.01e-46

Hsp33 family molecular chaperone HslO;


Pssm-ID: 234643  Cd Length: 293  Bit Score: 150.31  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988744664   1 DYIVKALAFDGEIRAYAALTTETVQEAQTRHYTWPTASAAMGRTMTATAMMGAMLKGDQKLTVTVDGQGPIGRIIADANA 80
Cdd:PRK00114    3 DYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDANA 82


                  ....*...
gi 1988744664  81 KGEVRAYV 88
Cdd:PRK00114   83 DGQVRGYV 90
HslO COG1281
Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein ...
 1-88 8.75e-42

Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440892  Cd Length: 291  Bit Score: 137.59  E-value: 8.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988744664   1 DYIVKALAFDGEIRAYAALTTETVQEAQTRHYTWPTASAAMGRTMTATAMMGAMLKGDQKLTVTVDGQGPIGRIIADANA 80
Cdd:COG1281     2 DYLVRFLFEDGDVRGEAVRLTETVQEALARHDYPPPVTALLGEALAAAALLGATLKFDGRLTLQIQGDGPLGLLVADADS 81


                  ....*...
gi 1988744664  81 KGEVRAYV 88
Cdd:COG1281    82 DGEVRGYA 89
HSP33 pfam01430
Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones ...
 7-88 1.49e-37

Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.


Pssm-ID: 460209  Cd Length: 271  Bit Score: 126.10  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988744664   7 LAFDGEIRAYAALTTETVQEAQTRHYTWPTASAAMGRTMTATAMMGAMLKGD-QKLTVTVDGQGPIGRIIADANAKGEVR 85
Cdd:pfam01430   1 LAEDGNVRGFAVRLTELVEEALARHDYPPVATAALGRALAAAALLGATLKFEdGRLTLQIQGDGPLGLLVADADSDGNVR 80


                  ...
gi 1988744664  86 AYV 88
Cdd:pfam01430  81 GYV 83
 
Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
1-88 1.01e-46

Hsp33 family molecular chaperone HslO;


Pssm-ID: 234643  Cd Length: 293  Bit Score: 150.31  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988744664   1 DYIVKALAFDGEIRAYAALTTETVQEAQTRHYTWPTASAAMGRTMTATAMMGAMLKGDQKLTVTVDGQGPIGRIIADANA 80
Cdd:PRK00114    3 DYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDANA 82


                  ....*...
gi 1988744664  81 KGEVRAYV 88
Cdd:PRK00114   83 DGQVRGYV 90
HslO COG1281
Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein ...
 1-88 8.75e-42

Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440892  Cd Length: 291  Bit Score: 137.59  E-value: 8.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988744664   1 DYIVKALAFDGEIRAYAALTTETVQEAQTRHYTWPTASAAMGRTMTATAMMGAMLKGDQKLTVTVDGQGPIGRIIADANA 80
Cdd:COG1281     2 DYLVRFLFEDGDVRGEAVRLTETVQEALARHDYPPPVTALLGEALAAAALLGATLKFDGRLTLQIQGDGPLGLLVADADS 81


                  ....*...
gi 1988744664  81 KGEVRAYV 88
Cdd:COG1281    82 DGEVRGYA 89
HSP33 pfam01430
Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones ...
 7-88 1.49e-37

Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.


Pssm-ID: 460209  Cd Length: 271  Bit Score: 126.10  E-value: 1.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988744664   7 LAFDGEIRAYAALTTETVQEAQTRHYTWPTASAAMGRTMTATAMMGAMLKGD-QKLTVTVDGQGPIGRIIADANAKGEVR 85
Cdd:pfam01430   1 LAEDGNVRGFAVRLTELVEEALARHDYPPVATAALGRALAAAALLGATLKFEdGRLTLQIQGDGPLGLLVADADSDGNVR 80


                  ...
gi 1988744664  86 AYV 88
Cdd:pfam01430  81 GYV 83
hslO PRK01402
Hsp33-like chaperonin; Reviewed
 22-87 6.98e-03

Hsp33-like chaperonin; Reviewed


Pssm-ID: 234952  Cd Length: 328  Bit Score: 33.76  E-value: 6.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988744664  22 ETVQEAQTRH-YTWPTAsAAMGRTMTATAMMGAMLKGDQKLTVTVDGQGPIGRIIADANAKGEVRAY 87
Cdd:PRK01402   38 PALDEILTRHdYPEPVA-RLLGEAVVLTVLLGSSLKFEGRFILQTQGDGPVDMLVVDFSTPDRLRAY 103
 
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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