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Conserved domains on  [gi|115532478|ref|NP_001040754|]
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Thioredoxin domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 55-166 2.04e-49

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


:

Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 168.71  E-value: 2.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532478  55 SVFEYKYRMSYQQYQFKILEESNTKPYIVYIYSNYCQMCYRFHPQWKRVIADLEPLGYGIATVNGNREQNLMEKMRISHV 134
Cdd:cd02963    1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115532478 135 PALVAIVEGRiIPMRIDSSFSDRSIVAFAQKV 166
Cdd:cd02963   81 PAIVGIINGQ-VTFYHDSSFTKQHVVDFVRKL 111
DnaJ_bact super family cl37091
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 2-23 2.62e-05

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


The actual alignment was detected with superfamily member TIGR02349:

Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 47.21  E-value: 2.62e-05
                          10        20
                  ....*....|....*....|..
gi 115532478    2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:TIGR02349  44 EINEAYEVLSDPEKRAQYDQFG 65
 
Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 55-166 2.04e-49

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 168.71  E-value: 2.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532478  55 SVFEYKYRMSYQQYQFKILEESNTKPYIVYIYSNYCQMCYRFHPQWKRVIADLEPLGYGIATVNGNREQNLMEKMRISHV 134
Cdd:cd02963    1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115532478 135 PALVAIVEGRiIPMRIDSSFSDRSIVAFAQKV 166
Cdd:cd02963   81 PAIVGIINGQ-VTFYHDSSFTKQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 2-23 2.62e-05

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 47.21  E-value: 2.62e-05
                          10        20
                  ....*....|....*....|..
gi 115532478    2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:TIGR02349  44 EINEAYEVLSDPEKRAQYDQFG 65
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 2-75 3.38e-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: 44.31  E-value: 3.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGTFDDVKQFEDNAERARSFYGFGGFGGFGFDESVFEYKYRMSYQQYQFKILEE 75
Cdd:COG0484   45 EINEAYEVLSDPEKRAAYDRFGHAAELLLATELAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLL 118
PRK14297 PRK14297
molecular chaperone DnaJ;
2-26 5.56e-05

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 46.31  E-value: 5.56e-05
                         10        20
                 ....*....|....*....|....*
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGTFD 26
Cdd:PRK14297  49 EINEAYQVLSDPQKKAQYDQFGTAD 73
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
2-28 1.54e-04

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 44.81  E-value: 1.54e-04
                         10        20
                 ....*....|....*....|....*..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGtFDDV 28
Cdd:NF037946  49 EINEAYEVLSNPEKRANYDKYG-HDGV 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1-20 1.12e-03

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: 37.84  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|
gi 115532478    1 MEIAEAYEVLSDPLRKERYD 20
Cdd:pfam00226  44 KEINEAYEVLSDPEKRAIYD 63
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 76-145 2.57e-03

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 39.99  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532478  76 SNTKPYIVYIYSNYCQMCYRFHPQWKRVIADLEPLgYGIATVNGNREQNLMEKMRISHVPALVAIVEGRI 145
Cdd:PTZ00443  50 ATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQ-VNVADLDATRALNLAKRFAIKGYPTLLLFDKGKM 118
 
Name Accession Description Interval E-value
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 55-166 2.04e-49

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 168.71  E-value: 2.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532478  55 SVFEYKYRMSYQQYQFKILEESNTKPYIVYIYSNYCQMCYRFHPQWKRVIADLEPLGYGIATVNGNREQNLMEKMRISHV 134
Cdd:cd02963    1 DSFDYKYSLTFSQYENEIVPKSFKKPYLIKITSDWCFSCIHIEPVWKEVIQELEPLGVGIATVNAGHERRLARKLGAHSV 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115532478 135 PALVAIVEGRiIPMRIDSSFSDRSIVAFAQKV 166
Cdd:cd02963   81 PAIVGIINGQ-VTFYHDSSFTKQHVVDFVRKL 111
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 2-23 2.62e-05

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 47.21  E-value: 2.62e-05
                          10        20
                  ....*....|....*....|..
gi 115532478    2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:TIGR02349  44 EINEAYEVLSDPEKRAQYDQFG 65
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 2-75 3.38e-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: 44.31  E-value: 3.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGTFDDVKQFEDNAERARSFYGFGGFGGFGFDESVFEYKYRMSYQQYQFKILEE 75
Cdd:COG0484   45 EINEAYEVLSDPEKRAAYDRFGHAAELLLATELAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLL 118
PRK14297 PRK14297
molecular chaperone DnaJ;
2-26 5.56e-05

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 46.31  E-value: 5.56e-05
                         10        20
                 ....*....|....*....|....*
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGTFD 26
Cdd:PRK14297  49 EINEAYQVLSDPQKKAQYDQFGTAD 73
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
2-28 1.54e-04

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 44.81  E-value: 1.54e-04
                         10        20
                 ....*....|....*....|....*..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGtFDDV 28
Cdd:NF037946  49 EINEAYEVLSNPEKRANYDKYG-HDGV 74
PRK14293 PRK14293
molecular chaperone DnaJ;
2-23 1.72e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 44.60  E-value: 1.72e-04
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK14293  47 EINRAYEVLSDPETRARYDQFG 68
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 2-33 2.50e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 44.01  E-value: 2.50e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG----------------TFDDV-KQFED 33
Cdd:PRK14282  50 EIQEAYEVLSDPQKRAMYDRFGyvgeqppyqetesgggFFEDIfKDFEN 98
PRK14280 PRK14280
molecular chaperone DnaJ;
2-30 3.68e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 43.56  E-value: 3.68e-04
                         10        20
                 ....*....|....*....|....*....
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGtFDDVKQ 30
Cdd:PRK14280  48 EISEAYEVLSDDQKRAQYDQFG-HAGPNQ 75
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 2-23 3.89e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 43.59  E-value: 3.89e-04
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK10767  49 EIKEAYEVLSDPQKRAAYDQYG 70
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 2-23 4.78e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 43.25  E-value: 4.78e-04
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK14277  50 EINEAYEILSDPQKRAQYDQFG 71
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1-20 1.12e-03

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: 37.84  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|
gi 115532478    1 MEIAEAYEVLSDPLRKERYD 20
Cdd:pfam00226  44 KEINEAYEVLSDPEKRAIYD 63
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 2-26 1.22e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 41.84  E-value: 1.22e-03
                         10        20
                 ....*....|....*....|....*
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFGTFD 26
Cdd:PRK14290  49 EISEAYEVLSDPQKRRQYDQTGTVD 73
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 2-23 1.26e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 41.75  E-value: 1.26e-03
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK14284  46 EVSEAYEVLSDAQKRESYDRYG 67
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 2-23 1.47e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 41.65  E-value: 1.47e-03
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK14301  49 EAAEAYEVLRDAEKRARYDRFG 70
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 2-23 2.19e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 40.99  E-value: 2.19e-03
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK14298  49 EISEAYAVLSDAEKRAQYDRFG 70
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 76-145 2.57e-03

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 39.99  E-value: 2.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115532478  76 SNTKPYIVYIYSNYCQMCYRFHPQWKRVIADLEPLgYGIATVNGNREQNLMEKMRISHVPALVAIVEGRI 145
Cdd:PTZ00443  50 ATTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQ-VNVADLDATRALNLAKRFAIKGYPTLLLFDKGKM 118
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 2-23 6.79e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 39.42  E-value: 6.79e-03
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK14283  49 EISEAYAVLSDDEKRQRYDQFG 70
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 2-23 8.19e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 39.36  E-value: 8.19e-03
                         10        20
                 ....*....|....*....|..
gi 115532478   2 EIAEAYEVLSDPLRKERYDRFG 23
Cdd:PRK14294  49 EAAEAYEVLSDPKKRGIYDQYG 70
 
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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