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Conserved domains on  [gi|25152096|ref|NP_496072|]
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DnaJ homolog dnj-20 [Caenorhabditis elegans]

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 ...
 1-54 6.59e-10

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: 51.66  E-value: 6.59e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 25152096   1 MEIQHLDGhIVKVQRDKVTWPGARLRKKDEGMPSLeDNNKKGMLVVTFDVEFPK 54
Cdd:cd10747 105 IEVPTLGG-KVKLKIPPGTQPGTVLRLKGKGMPRL-RGGGRGDLYVEVKVEFPK 156
 
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 ...
 1-54 6.59e-10

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: 51.66  E-value: 6.59e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 25152096   1 MEIQHLDGhIVKVQRDKVTWPGARLRKKDEGMPSLeDNNKKGMLVVTFDVEFPK 54
Cdd:cd10747 105 IEVPTLGG-KVKLKIPPGTQPGTVLRLKGKGMPRL-RGGGRGDLYVEVKVEFPK 156
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 2-80 2.68e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 51.75  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152096    2 EIQHLDGHIVKVQ--RDKVTWPGARLRKKDEGMPSLEDNNKKGMLVVTFDVEFPKTE-LSDEQKAQIIEILQQNTVKPKA 78
Cdd:PTZ00037 294 YITHLDGRKLLVNtpPGEVVKPGDIKVINNEGMPTYKSPFKKGNLYVTFEVIFPVDRkFTNEEKEILKSLFPQNPEEKKD 373


                 ..
gi 25152096   79 YN 80
Cdd:PTZ00037 374 LE 375
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 2-53 1.53e-07

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: 46.09  E-value: 1.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 25152096     2 EIQHLDGHiVKVQRDKVTWPGARLRKKDEGMPSLeDNNKKGMLVVTFDVEFP 53
Cdd:pfam01556 164 EVPTLDGK-VKLKIPAGTQPGTVLRLKGKGMPRL-KGGGRGDLYVTVKVEVP 213
 
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 ...
 1-54 6.59e-10

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: 51.66  E-value: 6.59e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 25152096   1 MEIQHLDGhIVKVQRDKVTWPGARLRKKDEGMPSLeDNNKKGMLVVTFDVEFPK 54
Cdd:cd10747 105 IEVPTLGG-KVKLKIPPGTQPGTVLRLKGKGMPRL-RGGGRGDLYVEVKVEFPK 156
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 2-80 2.68e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 51.75  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152096    2 EIQHLDGHIVKVQ--RDKVTWPGARLRKKDEGMPSLEDNNKKGMLVVTFDVEFPKTE-LSDEQKAQIIEILQQNTVKPKA 78
Cdd:PTZ00037 294 YITHLDGRKLLVNtpPGEVVKPGDIKVINNEGMPTYKSPFKKGNLYVTFEVIFPVDRkFTNEEKEILKSLFPQNPEEKKD 373


                 ..
gi 25152096   79 YN 80
Cdd:PTZ00037 374 LE 375
DnaJ_C pfam01556
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ...
 2-53 1.53e-07

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: 46.09  E-value: 1.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 25152096     2 EIQHLDGHiVKVQRDKVTWPGARLRKKDEGMPSLeDNNKKGMLVVTFDVEFP 53
Cdd:pfam01556 164 EVPTLDGK-VKLKIPAGTQPGTVLRLKGKGMPRL-KGGGRGDLYVTVKVEVP 213
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 1-77 2.17e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 34.75  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25152096    1 MEIQHLDGHIVKVQRDKVTWPGARLRKKDEGMPSLEDNNkKGMLVVTFDVEFPKTE-----LSDEQKAQ-IIEILQQNTV 74
Cdd:PRK14291 294 LEVPLLDGKKEKVKIPPGTKEGDKIRVPGKGMPRLKGSG-YGDLVVRVHIDVPKISmlsklMGDGKKAKkLLKELDKLLP 372


                 ...
gi 25152096   75 KPK 77
Cdd:PRK14291 373 EPE 375
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 1-75 2.46e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 34.74  E-value: 2.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25152096    1 MEIQHLDG-HIVKVQRDkvTWPGARLRKKDEGMPSLEDNNkKGMLVVTFDVEFPkTELSDEQKAQIIEILQQNTVK 75
Cdd:PRK14294 283 IEVPTLEGeRELKIPKG--TQPGDIFRFKGKGIPSLRGGG-RGDQIIEVEVKVP-TRLTKKQEELLTEFARLESEK 354
 
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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