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Conserved domains on  [gi|1027768989|ref|WP_063700695|]
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MULTISPECIES: DNA-J related domain-containing protein [Pseudoalteromonas]

Protein Classification

DNA-J related domain-containing protein( domain architecture ID 10322655)

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:  15170475|35729039|9644977|8016869|9585179|10542335
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DNAJ_related super family cl13736
DNA-J related protein; This domain family is found in bacteria, and is approximately 130 amino ...
 9-119 1.88e-35

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.


The actual alignment was detected with superfamily member pfam12339:

Pssm-ID: 432489  Cd Length: 120  Bit Score: 120.79  E-value: 1.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027768989   9 IFYLLLEQPT-WKVHTLASALSE--SGKIEPLDADPQKDLFKRNFLVMNGLYQLQTQLAPEQQ--LQIASLHIELVNEQI 83
Cdd:pfam12339   1 LLELLRAHPEgIKEHTLIKELKErpYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWgqLQIHALDIRLLPPAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027768989  84 ---SNALESHDPLRDYYLDWQNF-DTSSEEIDALLTDFWQ 119
Cdd:pfam12339  81 tsaDAALDEADPLREYYLDWSNYeDTDEADVERLLDSFWT 120
DnaJ smart00271
DnaJ molecular chaperone homology domain;
152-189 1.92e-06

DnaJ molecular chaperone homology domain;


:

Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 43.38  E-value: 1.92e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1027768989  152 SLKELQKRWRQLALKHHPDRQGCAIE-----FKKIQLEYEQLK 189
Cdd:smart00271  14 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 ...
 9-119 1.88e-35

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: 120.79  E-value: 1.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027768989   9 IFYLLLEQPT-WKVHTLASALSE--SGKIEPLDADPQKDLFKRNFLVMNGLYQLQTQLAPEQQ--LQIASLHIELVNEQI 83
Cdd:pfam12339   1 LLELLRAHPEgIKEHTLIKELKErpYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWgqLQIHALDIRLLPPAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027768989  84 ---SNALESHDPLRDYYLDWQNF-DTSSEEIDALLTDFWQ 119
Cdd:pfam12339  81 tsaDAALDEADPLREYYLDWSNYeDTDEADVERLLDSFWT 120
DnaJ smart00271
DnaJ molecular chaperone homology domain;
152-189 1.92e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 43.38  E-value: 1.92e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1027768989  152 SLKELQKRWRQLALKHHPDRQGCAIE-----FKKIQLEYEQLK 189
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEeaeekFKEINEAYEVLS 56
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 148-189 1.17e-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: 1.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1027768989 148 PVGFSLKELQKRWRQLALKHHPDR----QGCAIEFKKIQLEYEQLK 189
Cdd:pfam00226   9 SPDASDEEIKKAYRKLALKYHPDKnpgdPEAEEKFKEINEAYEVLS 54
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 148-189 1.51e-05

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: 40.99  E-value: 1.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1027768989 148 PVGFSLKELQKRWRQLALKHHPDR----QGCAIEFKKIQLEYEQLK 189
Cdd:cd06257     9 PPDASDEEIKKAYRKLALKYHPDKnpddPEAEEKFKEINEAYEVLS 54
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 152-188 1.92e-05

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 44.04  E-value: 1.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1027768989 152 SLKELQKRWRQLALKHHPDRQGCAIEFKKIQLEYEQL 188
Cdd:PTZ00037   41 TTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVL 77
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
148-189 2.28e-04

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 38.55  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1027768989 148 PVGFSLKELQKRWRQLALKHHPDRQGC-----AIEFKKIQLEYEQLK 189
Cdd:COG2214    14 PPDASLEEIRQAYRRLAKLLHPDRGGElkalaEELFQRLNEAYEVLS 60
 
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 ...
 9-119 1.88e-35

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: 120.79  E-value: 1.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1027768989   9 IFYLLLEQPT-WKVHTLASALSE--SGKIEPLDADPQKDLFKRNFLVMNGLYQLQTQLAPEQQ--LQIASLHIELVNEQI 83
Cdd:pfam12339   1 LLELLRAHPEgIKEHTLIKELKErpYGLFPPLDLSPPLDLFRTHFLLFHALYRLQERLWPEGWgqLQIHALDIRLLPPAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1027768989  84 ---SNALESHDPLRDYYLDWQNF-DTSSEEIDALLTDFWQ 119
Cdd:pfam12339  81 tsaDAALDEADPLREYYLDWSNYeDTDEADVERLLDSFWT 120
DnaJ smart00271
DnaJ molecular chaperone homology domain;
152-189 1.92e-06

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 43.38  E-value: 1.92e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1027768989  152 SLKELQKRWRQLALKHHPDRQGCAIE-----FKKIQLEYEQLK 189
Cdd:smart00271  14 SLDEIKKAYRKLALKYHPDKNPGDKEeaeekFKEINEAYEVLS 56
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 148-189 1.17e-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: 1.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1027768989 148 PVGFSLKELQKRWRQLALKHHPDR----QGCAIEFKKIQLEYEQLK 189
Cdd:pfam00226   9 SPDASDEEIKKAYRKLALKYHPDKnpgdPEAEEKFKEINEAYEVLS 54
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 148-189 1.51e-05

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: 40.99  E-value: 1.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1027768989 148 PVGFSLKELQKRWRQLALKHHPDR----QGCAIEFKKIQLEYEQLK 189
Cdd:cd06257     9 PPDASDEEIKKAYRKLALKYHPDKnpddPEAEEKFKEINEAYEVLS 54
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 152-188 1.92e-05

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 44.04  E-value: 1.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1027768989 152 SLKELQKRWRQLALKHHPDRQGCAIEFKKIQLEYEQL 188
Cdd:PTZ00037   41 TTSEIKKAYRKLAIKHHPDKGGDPEKFKEISRAYEVL 77
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 154-189 3.10e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 43.59  E-value: 3.10e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1027768989 154 KELQKRWRQLALKHHPDR-QGCA---IEFKKIQLEYEQLK 189
Cdd:PRK10767   19 DEIKKAYRKLAMKYHPDRnPGDKeaeEKFKEIKEAYEVLS 58
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
148-189 2.28e-04

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 38.55  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1027768989 148 PVGFSLKELQKRWRQLALKHHPDRQGC-----AIEFKKIQLEYEQLK 189
Cdd:COG2214    14 PPDASLEEIRQAYRRLAKLLHPDRGGElkalaEELFQRLNEAYEVLS 60
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 152-189 3.67e-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: 38.92  E-value: 3.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1027768989 152 SLKELQKRWRQLALKHHPDR----QGCAIEFKKIQLEYEQLK 189
Cdd:COG0484    13 SAEEIKKAYRKLAKKYHPDRnpgdPEAEEKFKEINEAYEVLS 54
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
148-171 1.92e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 35.54  E-value: 1.92e-03
                          10        20
                  ....*....|....*....|....
gi 1027768989 148 PVGFSLKELQKRWRQLALKHHPDR 171
Cdd:COG1076    13 PPDADDAELKRAYRKLQREHHPDR 36
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 152-171 8.74e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 36.28  E-value: 8.74e-03
                          10        20
                  ....*....|....*....|
gi 1027768989 152 SLKELQKRWRQLALKHHPDR 171
Cdd:PRK14294   17 SEEEIKKSYRKLAMKYHPDR 36
 
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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