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Conserved domains on  [gi|446709226|ref|WP_000786572|]
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MULTISPECIES: J domain-containing protein [Enterobacteriaceae]

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

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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];
1-51 5.78e-06

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: 44.71  E-value: 5.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446709226   1 MKNCWKILDIEETTDVDIIRRAYLALLPSFHPETDP-------QGFKQLRQAYEEALR 51
Cdd:COG2214    4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGelkalaeELFQRLNEAYEVLSD 61
 
Name Accession Description Interval E-value
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1-51 5.78e-06

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 44.71  E-value: 5.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446709226   1 MKNCWKILDIEETTDVDIIRRAYLALLPSFHPETDP-------QGFKQLRQAYEEALR 51
Cdd:COG2214    4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGelkalaeELFQRLNEAYEVLSD 61
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-47 5.98e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 43.76  E-value: 5.98e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 446709226     2 KNCWKILDIEETTDVDIIRRAYLALLPSFHPETDP-------QGFKQLRQAYE 47
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPgdkeeaeEKFKEINEAYE 53
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 3-47 1.38e-03

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: 36.75  E-value: 1.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446709226   3 NCWKILDIEETTDVDIIRRAY--LALLpsFHP------ETDPQGFKQLRQAYE 47
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYrkLALK--YHPdknpddPEAEEKFKEINEAYE 51
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 3-47 2.60e-03

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: 36.30  E-value: 2.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446709226    3 NCWKILDIEETTDVDIIRRAY--LALLpsFHPET---DPQG---FKQLRQAYE 47
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYrkLALK--YHPDKnpgDPEAeekFKEINEAYE 51
 
Name Accession Description Interval E-value
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1-51 5.78e-06

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 44.71  E-value: 5.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446709226   1 MKNCWKILDIEETTDVDIIRRAYLALLPSFHPETDP-------QGFKQLRQAYEEALR 51
Cdd:COG2214    4 LKDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGelkalaeELFQRLNEAYEVLSD 61
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-47 5.98e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 43.76  E-value: 5.98e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 446709226     2 KNCWKILDIEETTDVDIIRRAYLALLPSFHPETDP-------QGFKQLRQAYE 47
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPgdkeeaeEKFKEINEAYE 53
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 3-47 1.38e-03

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: 36.75  E-value: 1.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446709226   3 NCWKILDIEETTDVDIIRRAY--LALLpsFHP------ETDPQGFKQLRQAYE 47
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYrkLALK--YHPdknpddPEAEEKFKEINEAYE 51
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 3-47 2.60e-03

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: 36.30  E-value: 2.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446709226    3 NCWKILDIEETTDVDIIRRAY--LALLpsFHPET---DPQG---FKQLRQAYE 47
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYrkLALK--YHPDKnpgDPEAeekFKEINEAYE 51
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 3-47 3.13e-03

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: 38.14  E-value: 3.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446709226   3 NCWKILDIEETTDVDIIRRAYLALLPSFHPETDPQG------FKQLRQAYE 47
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDpeaeekFKEINEAYE 51
 
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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