NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17509089|ref|NP_491662|]
View 

Mitochondrial import inner membrane translocase subunit TIM14 [Caenorhabditis elegans]

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 ...
 6-107 1.19e-24

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: 89.91  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509089    6 IVAGLGLAAVGFGARYvLRNQALIKKGMEAIPVAG------GAFSNYYRGGFDQKMSRAEAAKILGVAPSAKPAKIKEAH 79
Cdd:PTZ00100   8 LTFGGGVLAVRYGYRY-LKNQKIFGSNNMSFPLSGfnpslgSLFLKNDLKGFENPMSKSEAYKILNISPTASKERIREAH 86

                         90       100
                 ....*....|....*....|....*...
gi 17509089   80 KKVMIVNHPDRGGSPYLAAKINEAKDLM 107
Cdd:PTZ00100  87 KQLMLRNHPDNGGSTYIASKVNEAKDLL 114
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 6-107 1.19e-24

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 89.91  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509089    6 IVAGLGLAAVGFGARYvLRNQALIKKGMEAIPVAG------GAFSNYYRGGFDQKMSRAEAAKILGVAPSAKPAKIKEAH 79
Cdd:PTZ00100   8 LTFGGGVLAVRYGYRY-LKNQKIFGSNNMSFPLSGfnpslgSLFLKNDLKGFENPMSKSEAYKILNISPTASKERIREAH 86

                         90       100
                 ....*....|....*....|....*...
gi 17509089   80 KKVMIVNHPDRGGSPYLAAKINEAKDLM 107
Cdd:PTZ00100  87 KQLMLRNHPDNGGSTYIASKVNEAKDLL 114
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
63-105 4.86e-09

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 49.33  E-value: 4.86e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17509089  63 ILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSP-----YLAAKINEAKD 105
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkalaeELFQRLNEAYE 57
DnaJ smart00271
DnaJ molecular chaperone homology domain;
62-112 9.04e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.00  E-value: 9.04e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17509089     62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSPYLAA-----KINEAKDLMESSKS 112
Cdd:smart00271   5 EILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 62-105 1.65e-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: 44.46  E-value: 1.65e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17509089  62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRG----GSPYLAAKINEAKD 105
Cdd:cd06257   4 DILGVPPDASDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYE 51
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 62-103 2.26e-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: 36.30  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 17509089    62 KILGVAPSAKPAKIKEAHKKVMIVNHPDR-GGSPYLAAK---INEA 103
Cdd:pfam00226   4 EILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEA 49
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 6-107 1.19e-24

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 89.91  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17509089    6 IVAGLGLAAVGFGARYvLRNQALIKKGMEAIPVAG------GAFSNYYRGGFDQKMSRAEAAKILGVAPSAKPAKIKEAH 79
Cdd:PTZ00100   8 LTFGGGVLAVRYGYRY-LKNQKIFGSNNMSFPLSGfnpslgSLFLKNDLKGFENPMSKSEAYKILNISPTASKERIREAH 86

                         90       100
                 ....*....|....*....|....*...
gi 17509089   80 KKVMIVNHPDRGGSPYLAAKINEAKDLM 107
Cdd:PTZ00100  87 KQLMLRNHPDNGGSTYIASKVNEAKDLL 114
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
63-105 4.86e-09

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 49.33  E-value: 4.86e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17509089  63 ILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSP-----YLAAKINEAKD 105
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELkalaeELFQRLNEAYE 57
DnaJ smart00271
DnaJ molecular chaperone homology domain;
62-112 9.04e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 48.00  E-value: 9.04e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 17509089     62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSPYLAA-----KINEAKDLMESSKS 112
Cdd:smart00271   5 EILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 62-105 1.65e-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: 44.46  E-value: 1.65e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17509089  62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRG----GSPYLAAKINEAKD 105
Cdd:cd06257   4 DILGVPPDASDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYE 51
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 62-103 1.06e-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: 41.61  E-value: 1.06e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 17509089  62 KILGVAPSAKPAKIKEAHKKVMIVNHPDR-GGSPYLAAK---INEA 103
Cdd:COG0484   4 EILGVSRDASAEEIKKAYRKLAKKYHPDRnPGDPEAEEKfkeINEA 49
djlA PRK09430
co-chaperone DjlA;
39-99 1.91e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 41.72  E-value: 1.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17509089   39 AGGAFSNYYRGGFDQKMSRA----EAAKILGVAPSAKPAKIKEAHKKVMIVNHPDRggspyLAAK 99
Cdd:PRK09430 177 AGFRFQQQQGGGGYQQAQRGptleDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK-----LVAK 236
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 62-103 2.26e-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: 36.30  E-value: 2.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 17509089    62 KILGVAPSAKPAKIKEAHKKVMIVNHPDR-GGSPYLAAK---INEA 103
Cdd:pfam00226   4 EILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEA 49
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
55-103 2.62e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 36.70  E-value: 2.62e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17509089  55 MSRAEAAKILGVAPSAKPAKIKEAHKKVMIVNHPDR---GGSPY-------LAAKINEA 103
Cdd:COG1076   1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaGLPEEeqrlalqKAAAINEA 59
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 62-107 3.26e-04

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 38.26  E-value: 3.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 17509089   62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSPYLAAKINEAKDLM 107
Cdd:PTZ00037  32 EVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVL 77
PHA02624 PHA02624
large T antigen; Provisional
 52-112 4.49e-04

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 38.04  E-value: 4.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17509089   52 DQKMSRAEAAKI---LGVAPSAKP--AKIKEAHKKVMIVNHPDRGGSPYLAAKINEAKDLMESSKS 112
Cdd:PHA02624   2 DKTLSREESKELmdlLGLPMAAWGnlPLMRKAYLRKCKEYHPDKGGDEEKMKRLNSLYKKLQEGVK 67
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 62-108 1.16e-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: 1.16e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 17509089  62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSPYLAA----KINEAKDLME 108
Cdd:COG5407   4 EVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEerfkEINEAYELLS 54
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 55-108 1.46e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 36.64  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17509089   55 MSRAEAAKILGVAPSAKPAKIKEAHKKVMIVNHPDRG-GSPYLAAKINEAKDLME 108
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYE 55
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 62-103 2.15e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 36.02  E-value: 2.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 17509089   62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSPYLA---AKINEA 103
Cdd:PRK14292   6 ELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAekfAQINEA 50
PRK14295 PRK14295
molecular chaperone DnaJ;
62-111 6.72e-03

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 34.44  E-value: 6.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17509089   62 KILGVAPSAKPAKIKEAHKKVMIVNHPD-RGGSPYLAAK---INEAKDLMESSK 111
Cdd:PRK14295  13 KVLGVPKDATEAEIKKAYRKLAREYHPDaNKGDAKAEERfkeISEAYDVLSDEK 66
PRK14279 PRK14279
molecular chaperone DnaJ;
62-107 7.37e-03

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 34.32  E-value: 7.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 17509089   62 KILGVAPSAKPAKIKEAHKKVMIVNHPDRGGSPYLAA----KINEAKDLM 107
Cdd:PRK14279  13 KELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEerfkAVSEAHDVL 62
 
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