NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1373810410|ref|WP_107125765|]
View 

MULTISPECIES: J domain-containing protein [unclassified Sphingobium]

Protein Classification

J domain-containing protein( domain architecture ID 10644999)

J domain-containing protein similar to molecular chaperone 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CbpA super family cl34431
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
150-201 6.84e-07

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


The actual alignment was detected with superfamily member COG2214:

Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 45.86  E-value: 6.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1373810410 150 RVMELDIDADRKALRMRYTALLRRYHPDHNGGDRSH-ERALQAVIEAYGHLKK 201
Cdd:COG2214     9 AVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALaEELFQRLNEAYEVLSD 61
 
Name Accession Description Interval E-value
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
150-201 6.84e-07

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 45.86  E-value: 6.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1373810410 150 RVMELDIDADRKALRMRYTALLRRYHPDHNGGDRSH-ERALQAVIEAYGHLKK 201
Cdd:COG2214     9 AVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALaEELFQRLNEAYEVLSD 61
DnaJ smart00271
DnaJ molecular chaperone homology domain;
151-201 1.48e-05

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 41.07  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1373810410  151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSH-ERALQAVIEAYGHLKK 201
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEaEEKFKEINEAYEVLSD 57
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 151-196 4.54e-05

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: 39.84  E-value: 4.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1373810410 151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAY 196
Cdd:cd06257     5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAY 50
PRK14288 PRK14288
molecular chaperone DnaJ;
151-205 2.65e-04

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 40.83  E-value: 2.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1373810410 151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAYGHL---KKAAVF 205
Cdd:PRK14288    8 ILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLsdeKKRALY 65
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 151-196 3.41e-04

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: 37.45  E-value: 3.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1373810410 151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAY 196
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAY 50
 
Name Accession Description Interval E-value
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
150-201 6.84e-07

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 45.86  E-value: 6.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1373810410 150 RVMELDIDADRKALRMRYTALLRRYHPDHNGGDRSH-ERALQAVIEAYGHLKK 201
Cdd:COG2214     9 AVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALaEELFQRLNEAYEVLSD 61
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 150-196 5.35e-06

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: 44.31  E-value: 5.35e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1373810410 150 RVMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAY 196
Cdd:COG0484     4 EILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAY 50
DnaJ smart00271
DnaJ molecular chaperone homology domain;
151-201 1.48e-05

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 41.07  E-value: 1.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1373810410  151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSH-ERALQAVIEAYGHLKK 201
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEaEEKFKEINEAYEVLSD 57
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 151-196 4.54e-05

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: 39.84  E-value: 4.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1373810410 151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAY 196
Cdd:cd06257     5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAY 50
PRK14288 PRK14288
molecular chaperone DnaJ;
151-205 2.65e-04

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 40.83  E-value: 2.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1373810410 151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAYGHL---KKAAVF 205
Cdd:PRK14288    8 ILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLsdeKKRALY 65
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 151-196 3.41e-04

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: 37.45  E-value: 3.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1373810410 151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAY 196
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAY 50
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 144-199 3.42e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 37.50  E-value: 3.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1373810410 144 EDRKALRVMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERaLQAVIEAYGHL 199
Cdd:PRK14283    3 EKRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEK-FKEISEAYAVL 57
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 151-196 5.10e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 37.09  E-value: 5.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1373810410 151 VMELDIDADRKALRMRYTALLRRYHPDHNGGDRSHERALQAVIEAY 196
Cdd:PRK14277   10 ILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAY 55
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH