NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|66472920|ref|NP_037370|]
View 

dnaJ homolog subfamily C member 15 [Homo sapiens]

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 ...
 41-144 1.32e-26

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: 96.46  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472920   41 IAVGLGVaalaFAGRYAFRIWKplEQVITETAKKISTPS---------FSSYYKGGFEQKMSRREAGLILGVSPSAGKAK 111
Cdd:PTZ00100   8 LTFGGGV----LAVRYGYRYLK--NQKIFGSNNMSFPLSgfnpslgslFLKNDLKGFENPMSKSEAYKILNISPTASKER 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 66472920  112 IRTAHRRVMILNHPDKGGSPYVAAKINEAKDLL 144
Cdd:PTZ00100  82 IREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 41-144 1.32e-26

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 96.46  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472920   41 IAVGLGVaalaFAGRYAFRIWKplEQVITETAKKISTPS---------FSSYYKGGFEQKMSRREAGLILGVSPSAGKAK 111
Cdd:PTZ00100   8 LTFGGGV----LAVRYGYRYLK--NQKIFGSNNMSFPLSgfnpslgslFLKNDLKGFENPMSKSEAYKILNISPTASKER 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 66472920  112 IRTAHRRVMILNHPDKGGSPYVAAKINEAKDLL 144
Cdd:PTZ00100  82 IREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
DnaJ smart00271
DnaJ molecular chaperone homology domain;
100-149 4.26e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 49.54  E-value: 4.26e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 66472920    100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAA-----KINEAKDLLETTTK 149
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLSDPEK 60
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
100-144 7.72e-09

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 49.72  E-value: 7.72e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 66472920 100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAA-----KINEAKDLL 144
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAeelfqRLNEAYEVL 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 100-144 3.59e-08

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: 47.15  E-value: 3.59e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66472920 100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVA----AKINEAKDLL 144
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeekfKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 100-144 6.65e-06

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: 6.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 66472920   100 ILGVSPSAGKAKIRTAHRRVMILNHPDK-GGSPYVAAK---INEAKDLL 144
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVL 53
 
Name Accession Description Interval E-value
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 41-144 1.32e-26

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 96.46  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472920   41 IAVGLGVaalaFAGRYAFRIWKplEQVITETAKKISTPS---------FSSYYKGGFEQKMSRREAGLILGVSPSAGKAK 111
Cdd:PTZ00100   8 LTFGGGV----LAVRYGYRYLK--NQKIFGSNNMSFPLSgfnpslgslFLKNDLKGFENPMSKSEAYKILNISPTASKER 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 66472920  112 IRTAHRRVMILNHPDKGGSPYVAAKINEAKDLL 144
Cdd:PTZ00100  82 IREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
DnaJ smart00271
DnaJ molecular chaperone homology domain;
100-149 4.26e-09

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 49.54  E-value: 4.26e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 66472920    100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAA-----KINEAKDLLETTTK 149
Cdd:smart00271   6 ILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAeekfkEINEAYEVLSDPEK 60
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
100-144 7.72e-09

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 49.72  E-value: 7.72e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 66472920 100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAA-----KINEAKDLL 144
Cdd:COG2214  10 VLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAeelfqRLNEAYEVL 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 100-144 3.59e-08

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: 47.15  E-value: 3.59e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66472920 100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVA----AKINEAKDLL 144
Cdd:cd06257   5 ILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAeekfKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 100-144 6.65e-06

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: 6.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 66472920   100 ILGVSPSAGKAKIRTAHRRVMILNHPDK-GGSPYVAAK---INEAKDLL 144
Cdd:pfam00226   5 ILGVSPDASDEEIKKAYRKLALKYHPDKnPGDPEAEEKfkeINEAYEVL 53
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 100-144 1.29e-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: 42.38  E-value: 1.29e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 66472920 100 ILGVSPSAGKAKIRTAHRRVMILNHPDK-GGSPYVAAK---INEAKDLL 144
Cdd:COG0484   5 ILGVSRDASAEEIKKAYRKLAKKYHPDRnPGDPEAEEKfkeINEAYEVL 53
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 80-149 2.94e-05

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 42.50  E-value: 2.94e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472920   80 FSSYYKGGFEQKMSRREAG-----LILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAAKINEAKDLLETTTK 149
Cdd:PTZ00037   8 FDGMPGGGFDGGRRKREVDneklyEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVLSDPEK 82
djlA PRK09430
co-chaperone DjlA;
28-127 6.64e-05

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 41.34  E-value: 6.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472920   28 DADVDQQ-RLVRSLIAVGLGVAALAFAGRYAFriWKpleqvitetakkiSTPSFSSYYKGGFEQKMSRR----EAGLILG 102
Cdd:PRK09430 143 DGSLHPNeRQVLYVIAEELGFSRFQFDQLLRM--MQ-------------AGFRFQQQQGGGGYQQAQRGptleDAYKVLG 207

                         90       100
                 ....*....|....*....|....*
gi 66472920  103 VSPSAGKAKIRTAHRRVMILNHPDK 127
Cdd:PRK09430 208 VSESDDDQEIKRAYRKLMSEHHPDK 232
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 92-145 2.10e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 39.97  E-value: 2.10e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 66472920   92 MSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDKG-GSPYVAAKINEAKDLLE 145
Cdd:PRK14286   1 MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNkGNKESEEKFKEATEAYE 55
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 92-144 3.19e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 39.54  E-value: 3.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 66472920   92 MSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAAK---INEAKDLL 144
Cdd:PRK14296   1 MKKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKmveINEAADVL 56
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
92-144 5.04e-04

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 36.70  E-value: 5.04e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66472920  92 MSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDK---GGSPYV-------AAKINEAKDLL 144
Cdd:COG1076   1 MQLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaaGLPEEEqrlalqkAAAINEAYETL 63
PHA02624 PHA02624
large T antigen; Provisional
 92-149 8.79e-04

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 38.43  E-value: 8.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66472920   92 MSRREAGLI---LGVSPSAGK--AKIRTAHRRVMILNHPDKGGSPYVAAKINEAKDLLETTTK 149
Cdd:PHA02624   5 LSREESKELmdlLGLPMAAWGnlPLMRKAYLRKCKEYHPDKGGDEEKMKRLNSLYKKLQEGVK 67
PRK14280 PRK14280
molecular chaperone DnaJ;
92-146 9.95e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 38.16  E-value: 9.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 66472920   92 MSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAAKINEAKDLLET 146
Cdd:PRK14280   1 MAKRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEV 55
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 100-149 1.01e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 37.95  E-value: 1.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 66472920  100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVA---AKINEAKDLLETTTK 149
Cdd:PRK14292   7 LLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAekfAQINEAYAVLSDAEK 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 92-145 3.08e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 36.64  E-value: 3.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 66472920   92 MSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDKG-GSPYVAAKINEAKDLLE 145
Cdd:PRK14301   1 MSQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNpDNPEAEQKFKEAAEAYE 55
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 100-149 3.94e-03

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 33.82  E-value: 3.94e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 66472920 100 ILGVSPSAGKAKIRTAHRRVMILNHPDKG-GSPYVAAK---INEAKDLLETTTK 149
Cdd:COG5407   5 VLGVAKTASADEIKKAYRKLAKKYHPDRNkGDPKAEERfkeINEAYELLSDAEK 58
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 92-146 4.18e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 36.14  E-value: 4.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 66472920   92 MSRREAGLILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVAAKINEAKDLLET 146
Cdd:PRK14287   1 MSKRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDT 55
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 100-149 6.86e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 35.55  E-value: 6.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 66472920  100 ILGVSPSAGKAKIRTAHRRVMILNHPDKGGSPYVA----AKINEAKDLLETTTK 149
Cdd:PRK14281   8 VLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAeehfKEVNEAYEVLSNDDK 61
PHA03102 PHA03102
Small T antigen; Reviewed
 101-139 8.90e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 34.65  E-value: 8.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 66472920  101 LGVSPSAGK--AKIRTAHRRVMILNHPDKGGSPYVAAKINE 139
Cdd:PHA03102  11 LGLPRSAWGnlPLMRKAYLRKCLEFHPDKGGDEEKMKELNT 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH