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Conserved domains on  [gi|197381799|ref|NP_001128112|]
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mitochondrial import inner membrane translocase subunit TIM14 [Rattus norvegicus]

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 ...
 53-94 1.91e-16

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: 71.04  E-value: 1.91e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 197381799  53 GFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG 94
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNG 98
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 53-94 1.91e-16

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 71.04  E-value: 1.91e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 197381799  53 GFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG 94
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNG 98
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
66-96 1.65e-07

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 47.02  E-value: 1.65e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 197381799  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGPL 96
Cdd:COG2214   10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGE 40
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-99 3.13e-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: 45.23  E-value: 3.13e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 197381799  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGPLVEE 99
Cdd:cd06257    5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPE 38
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-95 4.22e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 44.92  E-value: 4.22e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 197381799    66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNP 35
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-95 1.22e-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: 41.30  E-value: 1.22e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 197381799   66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKNP 34
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 53-94 1.91e-16

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 71.04  E-value: 1.91e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 197381799  53 GFEPKMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG 94
Cdd:PTZ00100  57 GFENPMSKSEAYKILNISPTASKERIREAHKQLMLRNHPDNG 98
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
66-96 1.65e-07

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 47.02  E-value: 1.65e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 197381799  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGPL 96
Cdd:COG2214   10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGE 40
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 66-99 3.13e-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: 45.23  E-value: 3.13e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 197381799  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGPLVEE 99
Cdd:cd06257    5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPE 38
DnaJ smart00271
DnaJ molecular chaperone homology domain;
66-95 4.22e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 44.92  E-value: 4.22e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 197381799    66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNP 35
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 66-95 1.22e-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: 41.30  E-value: 1.22e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 197381799   66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKNP 34
djlA PRK09430
co-chaperone DjlA;
45-103 1.55e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 43.65  E-value: 1.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 197381799  45 FSGGYYRGGFEP---KMTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKgpLVEEGLKP 103
Cdd:PRK09430 181 FQQQQGGGGYQQaqrGPTLEDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK--LVAKGLPP 240
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 66-95 2.55e-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: 42.00  E-value: 2.55e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 197381799  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:COG0484    5 ILGVSRDASAEEIKKAYRKLAKKYHPDRNP 34
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 59-95 7.90e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 42.10  E-value: 7.90e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 197381799  59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:PRK14281   1 MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNP 37
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
58-93 5.19e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 37.08  E-value: 5.19e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 197381799  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDK 93
Cdd:COG1076    1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDR 36
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 58-95 7.31e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 38.95  E-value: 7.31e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 197381799  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNP 38
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 59-104 1.12e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 38.68  E-value: 1.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 197381799  59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKG--PLVEEGLKPI 104
Cdd:PRK14298   3 TTRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNkePDAEEKFKEI 50
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 58-104 1.79e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 38.00  E-value: 1.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 197381799  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPD--KGPLVEEGLKPI 104
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDlnKSPDAHDKMVEI 49
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 59-104 2.72e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 37.44  E-value: 2.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 197381799  59 TKREAALILGVSPTANKGKIRDAHRRIMLLNHPD--KGPLVEEGLKPI 104
Cdd:PRK14291   1 AKKDYYEILGVSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEKFKEI 48
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 66-95 3.15e-03

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 34.59  E-value: 3.15e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 197381799  66 ILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:COG5407    5 VLGVAKTASADEIKKAYRKLAKKYHPDRNK 34
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 58-95 4.24e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 36.67  E-value: 4.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 197381799  58 MTKREAALILGVSPTANKGKIRDAHRRIMLLNHPDKGP 95
Cdd:PRK14294   1 MVKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNP 38
 
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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