NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|559767237|ref|NP_001273901|]
View 

mitochondrial import inner membrane translocase subunit TIM14 isoform3 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 55-94 1.01e-14

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: 65.26  E-value: 1.01e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 559767237  55 EPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG 94
Cdd:PTZ00100  59 ENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNG 98
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 55-94 1.01e-14

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 65.26  E-value: 1.01e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 559767237  55 EPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG 94
Cdd:PTZ00100  59 ENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNG 98
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
66-97 1.64e-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: 1.64e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 559767237  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGKQL 97
Cdd:COG2214   10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGEL 41
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-96 3.20e-07

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: 44.07  E-value: 3.20e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 559767237  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGKQ 96
Cdd:cd06257    5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPD 35
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-95 3.78e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 44.15  E-value: 3.78e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 559767237    66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGK 95
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNP 35
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-93 1.08e-05

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: 40.53  E-value: 1.08e-05
                          10        20
                  ....*....|....*....|....*...
gi 559767237   66 ILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDK 32
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 55-94 1.01e-14

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 65.26  E-value: 1.01e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 559767237  55 EPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG 94
Cdd:PTZ00100  59 ENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNG 98
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
66-97 1.64e-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: 1.64e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 559767237  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGKQL 97
Cdd:COG2214   10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGEL 41
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-96 3.20e-07

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: 44.07  E-value: 3.20e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 559767237  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGKQ 96
Cdd:cd06257    5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPD 35
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-95 3.78e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 44.15  E-value: 3.78e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 559767237    66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGK 95
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNP 35
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-93 1.08e-05

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: 40.53  E-value: 1.08e-05
                          10        20
                  ....*....|....*....|....*...
gi 559767237   66 ILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDK 32
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-95 3.92e-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: 40.46  E-value: 3.92e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 559767237  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGK 95
Cdd:COG0484    5 ILGVSRDASAEEIKKAYRKLAKKYHPDRNP 34
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
58-93 2.57e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.08  E-value: 2.57e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 559767237  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:COG1076    1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDR 36
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 59-93 2.73e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 39.02  E-value: 2.73e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 559767237  59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:PRK14281   1 MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDK 35
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 58-95 3.36e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 38.82  E-value: 3.36e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 559767237  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGK 95
Cdd:PRK14286   1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNK 38
djlA PRK09430
co-chaperone DjlA;
66-93 5.03e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 38.25  E-value: 5.03e-04
                         10        20
                 ....*....|....*....|....*...
gi 559767237  66 ILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:PRK09430 205 VLGVSESDDDQEIKRAYRKLMSEHHPDK 232
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 59-96 9.07e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 37.52  E-value: 9.07e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 559767237  59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGKQ 96
Cdd:PRK14298   3 TTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE 40
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 66-96 1.22e-03

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 34.98  E-value: 1.22e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 559767237  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGKQ 96
Cdd:COG5407    5 VLGVAKTASADEIKKAYRKLAKKYHPDRNKG 35
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 60-95 1.32e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 37.28  E-value: 1.32e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 559767237  60 KREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGK 95
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNK 37
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 58-96 1.91e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 36.85  E-value: 1.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 559767237  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGKQ 96
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKS 39
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 58-93 2.33e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 36.64  E-value: 2.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 559767237  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDR 36
PRK14280 PRK14280
molecular chaperone DnaJ;
58-96 3.01e-03

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 36.24  E-value: 3.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 559767237  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGKQ 96
Cdd:PRK14280   1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE 39
 
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