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Conserved domains on  [gi|1622860766|ref|XP_028688665|]
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dnaJ homolog subfamily C member 4 isoform X6 [Macaca mulatta]

Protein Classification

J domain-containing protein( domain architecture ID 10446266)

J domain-containing protein containing a similar domain as DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70.

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 31-67 2.30e-12

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: 59.41  E-value: 2.30e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:pfam00226  27 KYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 31-67 2.30e-12

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: 59.41  E-value: 2.30e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:pfam00226  27 KYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 31-68 1.31e-11

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: 59.72  E-value: 1.31e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYDA 68
Cdd:COG0484    27 KYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 31-67 1.31e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 53.61  E-value: 1.31e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK10767   31 KYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 31-59 4.11e-06

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: 42.53  E-value: 4.11e-06
                          10        20
                  ....*....|....*....|....*....
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSR 59
Cdd:cd06257    27 KYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
31-62 1.16e-04

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 38.75  E-value: 1.16e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622860766   31 QLHPDRDPGNPSL-HSRFVELSEAYRVLSREQS 62
Cdd:smart00271  28 KYHPDKNPGDKEEaEEKFKEINEAYEVLSDPEK 60
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 31-67 2.30e-12

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: 59.41  E-value: 2.30e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:pfam00226  27 KYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 31-68 1.31e-11

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: 59.72  E-value: 1.31e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYDA 68
Cdd:COG0484    27 KYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDR 64
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 31-67 1.31e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 53.61  E-value: 1.31e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK10767   31 KYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
31-83 1.55e-08

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 50.10  E-value: 1.55e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622860766  31 QLHPDRDPGNPSL-HSRFVELSEAYRVLSREQSRRRYDAQLRSGGPPKSPQTTA 83
Cdd:COG2214    32 LLHPDRGGELKALaEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGSASQPSA 85
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 31-67 6.09e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 51.73  E-value: 6.09e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14281   30 KYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14279 PRK14279
molecular chaperone DnaJ;
31-74 8.30e-08

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 51.27  E-value: 8.30e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD---AQLRSGG 74
Cdd:PRK14279   36 ELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDetrRLFAGGG 82
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 31-67 1.64e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 50.18  E-value: 1.64e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14277   32 KYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 31-67 3.12e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 49.46  E-value: 3.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14284   28 KYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14289 PRK14289
molecular chaperone DnaJ;
31-67 3.63e-07

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 49.44  E-value: 3.63e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14289   32 QYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 31-67 4.73e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 48.97  E-value: 4.73e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14301   31 QYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14295 PRK14295
molecular chaperone DnaJ;
31-67 1.19e-06

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 47.92  E-value: 1.19e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14295   36 EYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14297 PRK14297
molecular chaperone DnaJ;
33-67 1.80e-06

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 47.09  E-value: 1.80e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622860766  33 HPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14297   33 HPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYD 67
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 31-67 1.94e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 47.07  E-value: 1.94e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14294   31 KYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYD 67
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 31-59 4.11e-06

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: 42.53  E-value: 4.11e-06
                          10        20
                  ....*....|....*....|....*....
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSR 59
Cdd:cd06257    27 KYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 33-95 1.74e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 44.15  E-value: 1.74e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622860766  33 HPDRDPGN-PSLHSRFVELSEAYRVLSREQSRRRYDaqlrsggppkspQTTAHDKSAGQTHSSW 95
Cdd:PRK14290   32 HPDLHPGNkAEAEEKFKEISEAYEVLSDPQKRRQYD------------QTGTVDFGAGGSNFNW 83
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 31-67 7.27e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 42.47  E-value: 7.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622860766  31 QLHPDRDPGNPSL-HSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14282   31 EWHPDRHPENRKEaEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 31-67 9.02e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 42.06  E-value: 9.02e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPgNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14291   30 KYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYD 65
DnaJ smart00271
DnaJ molecular chaperone homology domain;
31-62 1.16e-04

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 38.75  E-value: 1.16e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622860766   31 QLHPDRDPGNPSL-HSRFVELSEAYRVLSREQS 62
Cdd:smart00271  28 KYHPDKNPGDKEEaEEKFKEINEAYEVLSDPEK 60
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 31-67 2.11e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 40.99  E-value: 2.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPgNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14298   32 KYHPDKNK-EPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14293 PRK14293
molecular chaperone DnaJ;
31-67 3.14e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 40.36  E-value: 3.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622860766  31 QLHPD--RDPGNpslHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14293   30 KYHPDvnKEPGA---EDRFKEINRAYEVLSDPETRARYD 65
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 33-73 6.12e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 39.59  E-value: 6.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622860766  33 HPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYDAQLRSG 73
Cdd:PRK14286   33 HPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAG 73
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 33-67 6.59e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 39.42  E-value: 6.59e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622860766  33 HPDRDPgNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14283   34 HPDVSE-EEGAEEKFKEISEAYAVLSDDEKRQRYD 67
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 33-67 8.54e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 39.20  E-value: 8.54e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622860766  33 HPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14285   32 HPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14280 PRK14280
molecular chaperone DnaJ;
31-67 2.48e-03

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 37.78  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1622860766  31 QLHPDRDPgNPSLHSRFVELSEAYRVLSREQSRRRYD 67
Cdd:PRK14280   31 KYHPDINK-EEGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 31-76 4.15e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 37.18  E-value: 4.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622860766  31 QLHPDRDPgNPSLHSRFVELSEAYRVLSREQSRRRYD--AQLRSGGPP 76
Cdd:PRK14292   29 KYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYDrfGTAPGAGMP 75
PRK14288 PRK14288
molecular chaperone DnaJ;
31-73 5.03e-03

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 36.98  E-value: 5.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622860766  31 QLHPDRDPGNPSLHSRFVELSEAYRVLSREQSRRRYDAQLRSG 73
Cdd:PRK14288   30 KYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKG 72
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 31-79 8.95e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 36.07  E-value: 8.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622860766  31 QLHPDRDPgNPSLHSRFVELSEAYRVLSREQSRRRYD------AQLRSGGPPKSP 79
Cdd:PRK14299   31 KYHPDVNK-SPGAEEKFKEINEAYTVLSDPEKRRIYDtygttaASAGWQGPPPGP 84
 
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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