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Conserved domains on  [gi|2569148888|gb|WMI01661|]
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dnaJ-5, partial [Graphium agamemnon]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ_C super family cl47019
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ...
 1-63 2.95e-12

C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70.


The actual alignment was detected with superfamily member cd10747:

Pssm-ID: 199909 [Multi-domain]  Cd Length: 158  Bit Score: 57.44  E-value: 2.95e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569148888   1 ALCGTVITVPTmSGEKLTVNLQgEVVKPHTVKRFPGYGLPFPKePTRNGDLLVAFDIKFPERL 63
Cdd:cd10747    99 ALLGGEIEVPT-LGGKVKLKIP-PGTQPGTVLRLKGKGMPRLR-GGGRGDLYVEVKVEFPKKL 158
 
Name Accession Description Interval E-value
DnaJ_C cd10747
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ...
 1-63 2.95e-12

C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70.


Pssm-ID: 199909 [Multi-domain]  Cd Length: 158  Bit Score: 57.44  E-value: 2.95e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569148888   1 ALCGTVITVPTmSGEKLTVNLQgEVVKPHTVKRFPGYGLPFPKePTRNGDLLVAFDIKFPERL 63
Cdd:cd10747    99 ALLGGEIEVPT-LGGKVKLKIP-PGTQPGTVLRLKGKGMPRLR-GGGRGDLYVEVKVEFPKKL 158
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 1-60 5.90e-10

DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region.


Pssm-ID: 460251 [Multi-domain]  Cd Length: 213  Bit Score: 52.26  E-value: 5.90e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569148888   1 ALCGTVITVPTMSGE-KLTVNlqgEVVKPHTVKRFPGYGLPFPKePTRNGDLLVAFDIKFP 60
Cdd:pfam01556 157 ALLGGTIEVPTLDGKvKLKIP---AGTQPGTVLRLKGKGMPRLK-GGGRGDLYVTVKVEVP 213
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 1-71 4.99e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 47.51  E-value: 4.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569148888   1 ALCGTVITVPTMSGEKLTVNLQ-GEVVKPHTVKRFPGYGLPFPKEPTRNGDLLVAFDIKFP--ERLNTGVKEIL 71
Cdd:PTZ00037  287 ALTGFVFYITHLDGRKLLVNTPpGEVVKPGDIKVINNEGMPTYKSPFKKGNLYVTFEVIFPvdRKFTNEEKEIL 360
 
Name Accession Description Interval E-value
DnaJ_C cd10747
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ...
 1-63 2.95e-12

C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70.


Pssm-ID: 199909 [Multi-domain]  Cd Length: 158  Bit Score: 57.44  E-value: 2.95e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569148888   1 ALCGTVITVPTmSGEKLTVNLQgEVVKPHTVKRFPGYGLPFPKePTRNGDLLVAFDIKFPERL 63
Cdd:cd10747    99 ALLGGEIEVPT-LGGKVKLKIP-PGTQPGTVLRLKGKGMPRLR-GGGRGDLYVEVKVEFPKKL 158
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 1-60 5.90e-10

DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region.


Pssm-ID: 460251 [Multi-domain]  Cd Length: 213  Bit Score: 52.26  E-value: 5.90e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569148888   1 ALCGTVITVPTMSGE-KLTVNlqgEVVKPHTVKRFPGYGLPFPKePTRNGDLLVAFDIKFP 60
Cdd:pfam01556 157 ALLGGTIEVPTLDGKvKLKIP---AGTQPGTVLRLKGKGMPRLK-GGGRGDLYVTVKVEVP 213
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 1-71 4.99e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 47.51  E-value: 4.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569148888   1 ALCGTVITVPTMSGEKLTVNLQ-GEVVKPHTVKRFPGYGLPFPKEPTRNGDLLVAFDIKFP--ERLNTGVKEIL 71
Cdd:PTZ00037  287 ALTGFVFYITHLDGRKLLVNTPpGEVVKPGDIKVINNEGMPTYKSPFKKGNLYVTFEVIFPvdRKFTNEEKEIL 360
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 1-60 3.91e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 36.67  E-value: 3.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569148888   1 ALCGTVITVPTMSGEKLTVNLQGEvVKPHTVKRFPGYGLPFPKEPTRnGDLLVAFDIKFP 60
Cdd:PRK14291  288 AVLGTELEVPLLDGKKEKVKIPPG-TKEGDKIRVPGKGMPRLKGSGY-GDLVVRVHIDVP 345
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 1-71 3.31e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 33.97  E-value: 3.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569148888   1 ALCGTVITVPTMSGE-KLTVNlQGevVKPHTVKRFPGYGLPFPKEPTRnGDLLVAFDIKFPERLNTGVKEIL 71
Cdd:PRK14294  277 AALGAQIEVPTLEGErELKIP-KG--TQPGDIFRFKGKGIPSLRGGGR-GDQIIEVEVKVPTRLTKKQEELL 344
 
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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