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Conserved domains on  [gi|2269529892|gb|UTH33218|]
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DnaJ domain-containing protein [Ectopseudomonas hydrolytica]

Protein Classification

DNA-J related domain-containing protein( domain architecture ID 10574576)

DNA-J related domain-containing protein consists of an N-terminal DNA-J related domain and C-terminal J domain (also known as DnaJ domain); 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|9585179|10542335
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DNAJ_related pfam12339
DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino ...
 15-132 2.79e-55

DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino acids in length. The family is found in association with pfam00226. There is a conserved YYLD sequence motif. Mostof the sequences in this family are annotated as DNA-J related proteins but there is little publication to back this up.


:

Pssm-ID: 432489  Cd Length: 120  Bit Score: 171.25  E-value: 2.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269529892  15 VLELLLAAPEGLAEYQLIQQLKQRHSGHIPNLPLTDKLVLFRTHFLLFNALYRLRERLWQDGSHLLQISPLCIQLLP--Y 92
Cdd:pfam12339   1 LLELLRAHPEGIKEHTLIKELKERPYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWGQLQIHALDIRLLPpaP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2269529892  93 QAGSAELSERDGLRDYYLDMDNLRDTDERDVERLLASFWT 132
Cdd:pfam12339  81 TSADAALDEADPLREYYLDWSNYEDTDEADVERLLDSFWT 120
DnaJ smart00271
DnaJ molecular chaperone homology domain;
146-193 2.91e-07

DnaJ molecular chaperone homology domain;


:

Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 45.69  E-value: 2.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2269529892  146 LFELDEQAplDLARIKHRYRQLVSQHHPDRGGS-----TERLQSINKAMEILE 193
Cdd:smart00271   6 ILGVPRDA--SLDEIKKAYRKLALKYHPDKNPGdkeeaEEKFKEINEAYEVLS 56
 
Name Accession Description Interval E-value
DNAJ_related pfam12339
DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino ...
 15-132 2.79e-55

DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino acids in length. The family is found in association with pfam00226. There is a conserved YYLD sequence motif. Mostof the sequences in this family are annotated as DNA-J related proteins but there is little publication to back this up.


Pssm-ID: 432489  Cd Length: 120  Bit Score: 171.25  E-value: 2.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269529892  15 VLELLLAAPEGLAEYQLIQQLKQRHSGHIPNLPLTDKLVLFRTHFLLFNALYRLRERLWQDGSHLLQISPLCIQLLP--Y 92
Cdd:pfam12339   1 LLELLRAHPEGIKEHTLIKELKERPYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWGQLQIHALDIRLLPpaP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2269529892  93 QAGSAELSERDGLRDYYLDMDNLRDTDERDVERLLASFWT 132
Cdd:pfam12339  81 TSADAALDEADPLREYYLDWSNYEDTDEADVERLLDSFWT 120
DnaJ smart00271
DnaJ molecular chaperone homology domain;
146-193 2.91e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 45.69  E-value: 2.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2269529892  146 LFELDEQAplDLARIKHRYRQLVSQHHPDRGGS-----TERLQSINKAMEILE 193
Cdd:smart00271   6 ILGVPRDA--SLDEIKKAYRKLALKYHPDKNPGdkeeaEEKFKEINEAYEVLS 56
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
146-194 4.03e-07

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 45.94  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2269529892 146 LFELDEQAplDLARIKHRYRQLVSQHHPDR---GGS-------TERLQSINKAMEILER 194
Cdd:COG1076     9 LLGLPPDA--DDAELKRAYRKLQREHHPDRlaaGLPeeeqrlaLQKAAAINEAYETLKD 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 146-192 3.89e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 46.35  E-value: 3.89e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2269529892 146 LFELDEQAPLDlaRIKHRYRQLVSQHHPDRGGSTERLQSINKAMEIL 192
Cdd:PTZ00037   33 VLNLSKDCTTS--EIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVL 77
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 146-194 6.17e-06

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: 42.15  E-value: 6.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2269529892 146 LFELDEQAplDLARIKHRYRQLVSQHHPDRG----GSTERLQSINKAMEILER 194
Cdd:cd06257     5 ILGVPPDA--SDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYEVLSD 55
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 160-192 3.34e-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: 37.45  E-value: 3.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2269529892 160 IKHRYRQLVSQHHPDRG----GSTERLQSINKAMEIL 192
Cdd:pfam00226  17 IKKAYRKLALKYHPDKNpgdpEAEEKFKEINEAYEVL 53
 
Name Accession Description Interval E-value
DNAJ_related pfam12339
DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino ...
 15-132 2.79e-55

DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino acids in length. The family is found in association with pfam00226. There is a conserved YYLD sequence motif. Mostof the sequences in this family are annotated as DNA-J related proteins but there is little publication to back this up.


Pssm-ID: 432489  Cd Length: 120  Bit Score: 171.25  E-value: 2.79e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269529892  15 VLELLLAAPEGLAEYQLIQQLKQRHSGHIPNLPLTDKLVLFRTHFLLFNALYRLRERLWQDGSHLLQISPLCIQLLP--Y 92
Cdd:pfam12339   1 LLELLRAHPEGIKEHTLIKELKERPYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWGQLQIHALDIRLLPpaP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2269529892  93 QAGSAELSERDGLRDYYLDMDNLRDTDERDVERLLASFWT 132
Cdd:pfam12339  81 TSADAALDEADPLREYYLDWSNYEDTDEADVERLLDSFWT 120
DnaJ smart00271
DnaJ molecular chaperone homology domain;
146-193 2.91e-07

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 45.69  E-value: 2.91e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2269529892  146 LFELDEQAplDLARIKHRYRQLVSQHHPDRGGS-----TERLQSINKAMEILE 193
Cdd:smart00271   6 ILGVPRDA--SLDEIKKAYRKLALKYHPDKNPGdkeeaEEKFKEINEAYEVLS 56
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
146-194 4.03e-07

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 45.94  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2269529892 146 LFELDEQAplDLARIKHRYRQLVSQHHPDR---GGS-------TERLQSINKAMEILER 194
Cdd:COG1076     9 LLGLPPDA--DDAELKRAYRKLQREHHPDRlaaGLPeeeqrlaLQKAAAINEAYETLKD 65
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 146-192 3.89e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 46.35  E-value: 3.89e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2269529892 146 LFELDEQAPLDlaRIKHRYRQLVSQHHPDRGGSTERLQSINKAMEIL 192
Cdd:PTZ00037   33 VLNLSKDCTTS--EIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVL 77
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 146-194 6.17e-06

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: 42.15  E-value: 6.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2269529892 146 LFELDEQAplDLARIKHRYRQLVSQHHPDRG----GSTERLQSINKAMEILER 194
Cdd:cd06257     5 ILGVPPDA--SDEEIKKAYRKLALKYHPDKNpddpEAEEKFKEINEAYEVLSD 55
PHA03102 PHA03102
Small T antigen; Reviewed
 138-195 6.91e-06

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 44.28  E-value: 6.91e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2269529892 138 EEKQAALGLFELDEQAPLDLARIKHRYRQLVSQHHPDRGGSTERLQSINKAMEILERY 195
Cdd:PHA03102    2 EESKELMDLLGLPRSAWGNLPLMRKAYLRKCLEFHPDKGGDEEKMKELNTLYKKFRES 59
PHA02624 PHA02624
large T antigen; Provisional
 138-195 3.20e-05

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 43.82  E-value: 3.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2269529892 138 EEKQAALGLFELDEQAPLDLARIKHRYRQLVSQHHPDRGGSTERLQSINKAMEILERY 195
Cdd:PHA02624    8 EESKELMDLLGLPMAAWGNLPLMRKAYLRKCKEYHPDKGGDEEKMKRLNSLYKKLQEG 65
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
156-192 4.72e-05

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 40.47  E-value: 4.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2269529892 156 DLARIKHRYRQLVSQHHPDRGG-----STERLQSINKAMEIL 192
Cdd:COG2214    18 SLEEIRQAYRRLAKLLHPDRGGelkalAEELFQRLNEAYEVL 59
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 156-192 1.86e-04

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: 40.07  E-value: 1.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2269529892 156 DLARIKHRYRQLVSQHHPDRGGS----TERLQSINKAMEIL 192
Cdd:COG0484    13 SAEEIKKAYRKLAKKYHPDRNPGdpeaEEKFKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 160-192 3.34e-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: 37.45  E-value: 3.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2269529892 160 IKHRYRQLVSQHHPDRG----GSTERLQSINKAMEIL 192
Cdd:pfam00226  17 IKKAYRKLALKYHPDKNpgdpEAEEKFKEINEAYEVL 53
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 158-192 4.09e-04

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 38.68  E-value: 4.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2269529892 158 ARIKHRYRQLVSQHHPDRGGSTERLQSINKAMEIL 192
Cdd:PTZ00100   80 ERIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
PRK14293 PRK14293
molecular chaperone DnaJ;
160-192 9.67e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 39.20  E-value: 9.67e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2269529892 160 IKHRYRQLVSQHHPD---RGGSTERLQSINKAMEIL 192
Cdd:PRK14293   20 LKRAYRRLARKYHPDvnkEPGAEDRFKEINRAYEVL 55
 
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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