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Conserved domains on  [gi|18398610|ref|NP_566352|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 84)

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
DnaJ super family cl02542
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 44-103 3.91e-19

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.


The actual alignment was detected with superfamily member PTZ00100:

Pssm-ID: 413365  Cd Length: 116  Bit Score: 76.04  E-value: 3.91e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398610   44 GFQATMNRREAALILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLASKINEAKDMMLG 103
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLLLK 116
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 44-103 3.91e-19

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 76.04  E-value: 3.91e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398610   44 GFQATMNRREAALILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLASKINEAKDMMLG 103
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLLLK 116
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
57-100 3.28e-05

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 39.32  E-value: 3.28e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18398610  57 ILGVRESVAAEKVKEAHRRVMVANHPDAGG-----SHYLASKINEAKDM 100
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGelkalAEELFQRLNEAYEV 58
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 57-99 2.80e-04

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: 35.98  E-value: 2.80e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18398610  57 ILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLA----SKINEAKD 99
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeekfKEINEAYE 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
57-99 1.53e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 34.13  E-value: 1.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 18398610     57 ILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLAS-----KINEAKD 99
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYE 53
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 44-103 3.91e-19

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 76.04  E-value: 3.91e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398610   44 GFQATMNRREAALILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLASKINEAKDMMLG 103
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLLLK 116
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
57-100 3.28e-05

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 39.32  E-value: 3.28e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 18398610  57 ILGVRESVAAEKVKEAHRRVMVANHPDAGG-----SHYLASKINEAKDM 100
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGelkalAEELFQRLNEAYEV 58
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 49-106 1.04e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 39.93  E-value: 1.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398610   49 MNRREAALILGVRESVAAEKVKEAHRRVMVANHPD---AGGSHYLASKINEAKDMMLGKTK 106
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDlnkSPDAHDKMVEINEAADVLLDKDK 61
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 57-99 2.80e-04

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: 35.98  E-value: 2.80e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18398610  57 ILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLA----SKINEAKD 99
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeekfKEINEAYE 51
DnaJ smart00271
DnaJ molecular chaperone homology domain;
57-99 1.53e-03

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 34.13  E-value: 1.53e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 18398610     57 ILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLAS-----KINEAKD 99
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYE 53
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 49-99 3.03e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 35.76  E-value: 3.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18398610   49 MNRREAALILGVRESVAAEKVKEAHRRVMVANHPDAGGSHYLASKINEAKD 99
Cdd:PRK14287   1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKE 51
djlA PRK09430
co-chaperone DjlA;
57-83 4.04e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 35.17  E-value: 4.04e-03
                         10        20
                 ....*....|....*....|....*..
gi 18398610   57 ILGVRESVAAEKVKEAHRRVMVANHPD 83
Cdd:PRK09430 205 VLGVSESDDDQEIKRAYRKLMSEHHPD 231
 
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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