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Conserved domains on  [gi|25147027|ref|NP_741015|]
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DnaJ homolog dnj-5 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 748-840 1.91e-45

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


:

Pssm-ID: 464360  Cd Length: 92  Bit Score: 157.90  E-value: 1.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147027   748 RNTIFC-DCENTHFRVATSISPSQARSCKRCGVKHPAKQNDIWVEKRHLGLTSTYYTCTDNVVYDITSWATCKSQRamLK 826
Cdd:pfam14901   1 ANTIRCtKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGDS--LM 78

                          90
                  ....*....|....
gi 25147027   827 NMRAHTHNVQYRLL 840
Cdd:pfam14901  79 HCRPNTHRVQYRIN 92
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 659-708 9.03e-10

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


:

Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 54.86  E-value: 9.03e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 25147027 659 DAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDA-ADQVYELVDVAFS 708
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPeAEEKFKEINEAYE 51
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 748-840 1.91e-45

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 157.90  E-value: 1.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147027   748 RNTIFC-DCENTHFRVATSISPSQARSCKRCGVKHPAKQNDIWVEKRHLGLTSTYYTCTDNVVYDITSWATCKSQRamLK 826
Cdd:pfam14901   1 ANTIRCtKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGDS--LM 78

                          90
                  ....*....|....
gi 25147027   827 NMRAHTHNVQYRLL 840
Cdd:pfam14901  79 HCRPNTHRVQYRIN 92
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 659-708 9.03e-10

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 54.86  E-value: 9.03e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 25147027 659 DAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDA-ADQVYELVDVAFS 708
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPeAEEKFKEINEAYE 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
658-715 5.91e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 53.01  E-value: 5.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147027    658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTID--AADQVYELVDVAFSAIGYKDS 715
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkeEAEEKFKEINEAYEVLSDPEK 60
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 659-719 7.35e-08

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 49.78  E-value: 7.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147027   659 DAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDA-ADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPeAEEKFKEINEAYEVLSDPEKRAIY 62
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
657-722 1.22e-06

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 47.41  E-value: 1.22e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25147027 657 IRDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTID--AADQVYELVDVAFSAIGYKDSRSEYTLE 722
Cdd:COG2214   4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkaLAEELFQRLNEAYEVLSDPERRAEYDRE 71
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 656-719 8.37e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 49.08  E-value: 8.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25147027  656 TIRDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDAADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:PRK14298   3 TTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQY 66
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 748-840 1.91e-45

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 157.90  E-value: 1.91e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147027   748 RNTIFC-DCENTHFRVATSISPSQARSCKRCGVKHPAKQNDIWVEKRHLGLTSTYYTCTDNVVYDITSWATCKSQRamLK 826
Cdd:pfam14901   1 ANTIRCtKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLWRYYACMDGKVYDITEWAICQGDS--LM 78

                          90
                  ....*....|....
gi 25147027   827 NMRAHTHNVQYRLL 840
Cdd:pfam14901  79 HCRPNTHRVQYRIN 92
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 659-708 9.03e-10

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 54.86  E-value: 9.03e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 25147027 659 DAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDA-ADQVYELVDVAFS 708
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPeAEEKFKEINEAYE 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
658-715 5.91e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 53.01  E-value: 5.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25147027    658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTID--AADQVYELVDVAFSAIGYKDS 715
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDkeEAEEKFKEINEAYEVLSDPEK 60
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 659-719 7.35e-08

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 49.78  E-value: 7.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147027   659 DAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDA-ADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPeAEEKFKEINEAYEVLSDPEKRAIY 62
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
657-722 1.22e-06

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 47.41  E-value: 1.22e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25147027 657 IRDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTID--AADQVYELVDVAFSAIGYKDSRSEYTLE 722
Cdd:COG2214   4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkaLAEELFQRLNEAYEVLSDPERRAEYDRE 71
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 656-719 8.37e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 49.08  E-value: 8.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25147027  656 TIRDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDAADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:PRK14298   3 TTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQY 66
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
658-690 2.15e-05

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 43.25  E-value: 2.15e-05
                        10        20        30
                ....*....|....*....|....*....|...
gi 25147027 658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDK 690
Cdd:COG1076   4 DDAFELLGLPPDADDAELKRAYRKLQREHHPDR 36
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 659-719 2.85e-05

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 44.69  E-value: 2.85e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147027 659 DAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTID-AADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDpEAEEKFKEINEAYEVLSDPEKRAAY 62
PRK14279 PRK14279
molecular chaperone DnaJ;
658-719 1.69e-04

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 45.11  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25147027  658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTID-AADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:PRK14279   9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDpAAEERFKAVSEAHDVLSDPAKRKEY 71
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 658-719 2.81e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 44.31  E-value: 2.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25147027  658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDAADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:PRK14276   4 TEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAY 65
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 658-689 1.86e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 41.58  E-value: 1.86e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 25147027  658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPD 689
Cdd:PRK14278   3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPD 34
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 658-719 5.79e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 40.11  E-value: 5.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25147027  658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDA-ADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:PRK14301   4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPeAEQKFKEAAEAYEVLRDAEKRARY 66
PRK14297 PRK14297
molecular chaperone DnaJ;
658-719 5.90e-03

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 40.15  E-value: 5.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25147027  658 RDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDKCTIDA-ADQVYELVDVAFSAIGYKDSRSEY 719
Cdd:PRK14297   4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKeAEEKFKEINEAYQVLSDPQKKAQY 66
djlA PRK09430
co-chaperone DjlA;
653-690 6.06e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 39.41  E-value: 6.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 25147027  653 SRETIRDAYSVFGLRSDCSDDDIKRNYKRLAALVSPDK 690
Cdd:PRK09430 195 RGPTLEDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
 
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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