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Conserved domains on  [gi|15228699|ref|NP_191778|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

J domain-containing protein( domain architecture ID 10644999)

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

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List of domain hits

 Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
9-65 3.02e-11

DnaJ molecular chaperone homology domain;


:

Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 54.93  E-value: 3.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228699      9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlVAESKFKSISEAYSCLESGD 65
Cdd:smart00271   6 ILGVPRDA--SLDEIKKAYRKLALKYHPDKNPGDKE-EAEEKFKEINEAYEVLSDPE 59
 
Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
9-65 3.02e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 54.93  E-value: 3.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228699      9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlVAESKFKSISEAYSCLESGD 65
Cdd:smart00271   6 ILGVPRDA--SLDEIKKAYRKLALKYHPDKNPGDKE-EAEEKFKEINEAYEVLSDPE 59
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 9-61 1.55e-10

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: 55.09  E-value: 1.55e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15228699   9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCL 61
Cdd:COG0484   5 ILGVSRDA--SAEEIKKAYRKLAKKYHPDRNPGDPE--AEEKFKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 9-71 4.14e-10

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: 52.09  E-value: 4.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228699     9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLeSGDVKGQWY 71
Cdd:pfam00226   5 ILGVSPDA--SDEEIKKAYRKLALKYHPDKNPGDPE--AEEKFKEINEAYEVL-SDPEKRAIY 62
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 9-61 9.87e-10

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: 51.01  E-value: 9.87e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15228699   9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCL 61
Cdd:cd06257   5 ILGVPPDA--SDEEIKKAYRKLALKYHPDKNPDDPE--AEEKFKEINEAYEVL 53
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 19-61 3.24e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 53.61  E-value: 3.24e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15228699   19 DPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCL 61
Cdd:PRK10767  17 SEDEIKKAYRKLAMKYHPDRNPGDKE--AEEKFKEIKEAYEVL 57
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 10-75 5.21e-08

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: 49.91  E-value: 5.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228699    10 LGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCLeSGDVKGQWYYRAG 75
Cdd:TIGR02349   6 LGVSKDA--SEEEIKKAYRKLAKKYHPDRNKDKE---AEEKFKEINEAYEVL-SDPEKRAQYDQFG 65
 
Name Accession Description Interval E-value
DnaJ smart00271
DnaJ molecular chaperone homology domain;
9-65 3.02e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 54.93  E-value: 3.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228699      9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlVAESKFKSISEAYSCLESGD 65
Cdd:smart00271   6 ILGVPRDA--SLDEIKKAYRKLALKYHPDKNPGDKE-EAEEKFKEINEAYEVLSDPE 59
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 9-61 1.55e-10

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: 55.09  E-value: 1.55e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15228699   9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCL 61
Cdd:COG0484   5 ILGVSRDA--SAEEIKKAYRKLAKKYHPDRNPGDPE--AEEKFKEINEAYEVL 53
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 9-71 4.14e-10

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: 52.09  E-value: 4.14e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15228699     9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLeSGDVKGQWY 71
Cdd:pfam00226   5 ILGVSPDA--SDEEIKKAYRKLALKYHPDKNPGDPE--AEEKFKEINEAYEVL-SDPEKRAIY 62
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 10-69 4.49e-10

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 51.92  E-value: 4.49e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228699  10 LGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLESGDVKGQ 69
Cdd:COG5407   6 LGVAKTASAD--EIKKAYRKLAKKYHPDRNKGDPK--AEERFKEINEAYELLSDAEKRAR 61
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
9-94 8.44e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 52.03  E-value: 8.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228699   9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKLvAESKFKSISEAYSCLeSGDVKGQWYYRAGVYSRvvKTGVPRP 88
Cdd:COG2214  10 VLGVPPDA--SLEEIRQAYRRLAKLLHPDRGGELKAL-AEELFQRLNEAYEVL-SDPERRAEYDRELGQSG--KGSASQP 83


                ....*.
gi 15228699  89 YSSAKR 94
Cdd:COG2214  84 SAAAQR 89
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 9-61 9.87e-10

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: 51.01  E-value: 9.87e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15228699   9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCL 61
Cdd:cd06257   5 ILGVPPDA--SDEEIKKAYRKLALKYHPDKNPDDPE--AEEKFKEINEAYEVL 53
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 19-61 3.24e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 53.61  E-value: 3.24e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15228699   19 DPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCL 61
Cdd:PRK10767  17 SEDEIKKAYRKLAMKYHPDRNPGDKE--AEEKFKEIKEAYEVL 57
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
9-58 2.79e-08

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 47.48  E-value: 2.79e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15228699   9 LLGFPPNSrpDPSQVKAAYRKKVWESHPDLF----PDDQKLVAESKFKSISEAY 58
Cdd:COG1076   9 LLGLPPDA--DDAELKRAYRKLQREHHPDRLaaglPEEEQRLALQKAAAINEAY 60
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 9-61 3.00e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 50.95  E-value: 3.00e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQKLvAESKFKSISEAYSCL 61
Cdd:PRK14282   9 ILGVSRNATQE--EIKRAYKRLVKEWHPDRHPENRKE-AEQKFKEIQEAYEVL 58
PRK14279 PRK14279
molecular chaperone DnaJ;
16-71 3.15e-08

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 50.89  E-value: 3.15e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228699   16 SRPDPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLeSGDVKGQWY 71
Cdd:PRK14279  19 SDASAEEIKKAYRKLARELHPDANPGDPA--AEERFKAVSEAHDVL-SDPAKRKEY 71
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 10-75 5.21e-08

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: 49.91  E-value: 5.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15228699    10 LGFPPNSrpDPSQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCLeSGDVKGQWYYRAG 75
Cdd:TIGR02349   6 LGVSKDA--SEEEIKKAYRKLAKKYHPDRNKDKE---AEEKFKEINEAYEVL-SDPEKRAQYDQFG 65
PRK14295 PRK14295
molecular chaperone DnaJ;
9-67 1.04e-07

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 49.46  E-value: 1.04e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLesGDVK 67
Cdd:PRK14295  14 VLGVPKDATEA--EIKKAYRKLAREYHPDANKGDAK--AEERFKEISEAYDVL--SDEK 66
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 22-75 1.23e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 48.97  E-value: 1.23e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15228699   22 QVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLESGDVKGQwYYRAG 75
Cdd:PRK14301  20 EIKKAYRKLALQYHPDRNPDNPE--AEQKFKEAAEAYEVLRDAEKRAR-YDRFG 70
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 9-75 1.26e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 49.07  E-value: 1.26e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLeSGDVKGQWYYRAG 75
Cdd:PRK14284   6 ILGVSKTASPE--EIKKAYRKLAVKYHPDKNPGDAE--AEKRFKEVSEAYEVL-SDAQKRESYDRYG 67
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 19-86 4.24e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 47.50  E-value: 4.24e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228699   19 DPSQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLESGDVKGQW--YYRAGVYSRVVKTGVP 86
Cdd:PRK14281  16 DKDEIKKAYRKLALKYHPDKNPDNKE--AEEHFKEVNEAYEVLSNDDKRRRYdqFGHAGVGSSAASGGGP 83
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 19-75 5.91e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 47.13  E-value: 5.91e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15228699   19 DPSQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCLeSGDVKGQWYYRAG 75
Cdd:PRK14283  18 DKKEIKKAYRKLARKYHPDVSEEEG---AEEKFKEISEAYAVL-SDDEKRQRYDQFG 70
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 9-70 7.25e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 46.72  E-value: 7.25e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLESGDVKGQW 70
Cdd:PRK14277  10 ILGVDRNATEE--EIKKAYRRLAKKYHPDLNPGDKE--AEQKFKEINEAYEILSDPQKRAQY 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 9-91 7.83e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 46.77  E-value: 7.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCLESGDVKGQwyyragvYSRVVKTGVPRP 88
Cdd:PRK14298  10 ILGLSKDASVE--DIKKAYRKLAMKYHPDKNKEPD---AEEKFKEISEAYAVLSDAEKRAQ-------YDRFGHAGIDNQ 77


                 ...
gi 15228699   89 YSS 91
Cdd:PRK14298  78 YSA 80
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 9-61 8.22e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 46.69  E-value: 8.22e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCL 61
Cdd:PRK14291   8 ILGVSRNATQE--EIKKAYRRLARKYHPDFNKNPE---AEEKFKEINEAYQVL 55
PRK14289 PRK14289
molecular chaperone DnaJ;
9-76 1.58e-06

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 45.98  E-value: 1.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLESGDVKGQW--YYRAGV 76
Cdd:PRK14289  10 VLGVSKTATVD--EIKKAYRKKAIQYHPDKNPGDKE--AEEKFKEAAEAYDVLSDPDKRSRYdqFGHAGV 75
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 9-61 6.43e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 44.15  E-value: 6.43e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDqKLVAESKFKSISEAYSCL 61
Cdd:PRK14290   8 ILGVDRNASQE--DIKKAFRELAKKWHPDLHPGN-KAEAEEKFKEISEAYEVL 57
PRK14297 PRK14297
molecular chaperone DnaJ;
22-70 6.93e-06

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 44.00  E-value: 6.93e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 15228699   22 QVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLESGDVKGQW 70
Cdd:PRK14297  20 EIKKAFRKLAIKYHPDKNKGNKE--AEEKFKEINEAYQVLSDPQKKAQY 66
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 21-61 8.25e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 43.89  E-value: 8.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15228699   21 SQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCL 61
Cdd:PRK14278  18 AEIKRAYRKLARELHPDVNPDEE---AQEKFKEISVAYEVL 55
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 17-72 2.65e-05

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 42.33  E-value: 2.65e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15228699  17 RPDPSQVKAAYRKKVWESHPDLFPDDQKLVAESKFKSISEAYSCLesGDVKGQWYY 72
Cdd:COG5269  57 KAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKLIQKAREVL--GDRKLRLQY 110
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 22-75 2.77e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 42.44  E-value: 2.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15228699   22 QVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLeSGDVKGQWYYRAG 75
Cdd:PRK14294  20 EIKKSYRKLAMKYHPDRNPGDKE--AEELFKEAAEAYEVL-SDPKKRGIYDQYG 70
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 9-88 3.17e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 41.85  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCLeSGDVKGQWYYRAGVYSRVVKTGVPRP 88
Cdd:PRK14299   9 ILGVPKNASQD--EIKKAFKKLARKYHPDVNKSPG---AEEKFKEINEAYTVL-SDPEKRRIYDTYGTTAASAGWQGPPP 82
PRK14280 PRK14280
molecular chaperone DnaJ;
22-75 1.67e-04

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 40.09  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15228699   22 QVKAAYRKKVWESHPDLfpdDQKLVAESKFKSISEAYSCLeSGDVKGQWYYRAG 75
Cdd:PRK14280  20 EIKKAYRKLSKKYHPDI---NKEEGADEKFKEISEAYEVL-SDDQKRAQYDQFG 69
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 19-61 2.59e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 39.49  E-value: 2.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15228699   19 DPSQVKAAYRKKVWESHPDLFPDDQklvAESKFKSISEAYSCL 61
Cdd:PRK14292  15 SADEIKSAYRKLALKYHPDRNKEKG---AAEKFAQINEAYAVL 54
PRK10266 PRK10266
curved DNA-binding protein;
1-70 5.37e-04

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 38.65  E-value: 5.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15228699    1 MEVEEAKILLGFPPNSrpDPSQVKAAYRKKVWESHPDLF--PDdqklvAESKFKSISEAYSCLESGDVKGQW 70
Cdd:PRK10266   1 MELKDYYAIMGVKPTD--DLKTIKTAYRRLARKYHPDVSkePD-----AEARFKEVAEAWEVLSDEQRRAEY 65
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 9-70 8.32e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 38.07  E-value: 8.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDL--FPDdqklvAESKFKSISEAYSCLESGDVKGQW 70
Cdd:PRK14287   9 VLGVDRNASVD--EVKKAYRKLARKYHPDVnkAPD-----AEDKFKEVKEAYDTLSDPQKKAHY 65
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 19-61 8.63e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 37.76  E-value: 8.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 15228699   19 DPSQ--VKAAYRKKVWESHPDLfpdDQKLVAESKFKSISEAYSCL 61
Cdd:PRK14276  15 DASQdeIKKAYRKLSKKYHPDI---NKEPGAEEKYKEVQEAYETL 56
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 9-75 1.29e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 37.28  E-value: 1.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15228699    9 LLGFPPNSRPDpsQVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLESGDVKGQwYYRAG 75
Cdd:PRK14285   8 ILGLSKGASKD--EIKKAYRKIAIKYHPDKNKGNKE--AESIFKEATEAYEVLIDDNKRAQ-YDRFG 69
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 22-70 1.36e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 37.23  E-value: 1.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 15228699   22 QVKAAYRKKVWESHPDLfpdDQKLVAESKFKSISEAYSCLESGDVKGQW 70
Cdd:PRK14296  20 EIRQAYRKLAKQYHPDL---NKSPDAHDKMVEINEAADVLLDKDKRKQY 65
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 22-76 1.41e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 37.28  E-value: 1.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228699   22 QVKAAYRKKVWESHPDLFPDDQKlvAESKFKSISEAYSCLEsgDVKGQWYY----RAGV 76
Cdd:PRK14286  20 EIKSAYRKLAIKYHPDKNKGNKE--SEEKFKEATEAYEILR--DPKKRQAYdqfgKAGV 74
hscB PRK00294
co-chaperone HscB; Provisional
 9-63 4.10e-03

co-chaperone HscB; Provisional


Pssm-ID: 166894 [Multi-domain]  Cd Length: 173  Bit Score: 35.60  E-value: 4.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15228699    9 LLGFPPNSRPDPSQVKAAYRKKVWESHPDLFPD----DQKLVAEsKFKSISEAYSCLES 63
Cdd:PRK00294   9 LFDLQPSFRLDLDQLATRYRELAREVHPDRFADaperEQRLALE-RSASLNEAYQTLKS 66
PRK14293 PRK14293
molecular chaperone DnaJ;
19-76 4.20e-03

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 35.74  E-value: 4.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15228699   19 DPSQVKAAYRKKVWESHPDLfpdDQKLVAESKFKSISEAYSCLESGDVKGQW--YYRAGV 76
Cdd:PRK14293  16 DKDELKRAYRRLARKYHPDV---NKEPGAEDRFKEINRAYEVLSDPETRARYdqFGEAGV 72
 
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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