DnaJ, partial [Aeromonas sp. MJ-61]
molecular chaperone DnaJ( domain architecture ID 1000952)
molecular chaperone DnaJ, part of the DnaK-DnaJ-GrpE system, prevents the aggregation of unfolded substrate and acts primarily by stimulating the ATPase activity of Hsp70
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PRK10767 super family | cl35946 | chaperone protein DnaJ; Provisional |
2-83 | 1.37e-55 | |||
chaperone protein DnaJ; Provisional The actual alignment was detected with superfamily member PRK10767: Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 174.95 E-value: 1.37e-55
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Name | Accession | Description | Interval | E-value | |||
PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
2-83 | 1.37e-55 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 174.95 E-value: 1.37e-55
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
1-83 | 1.26e-36 | |||
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: 125.41 E-value: 1.26e-36
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DnaJ_C | pfam01556 | DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
1-83 | 2.60e-25 | |||
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region. Pssm-ID: 460251 [Multi-domain] Cd Length: 213 Bit Score: 93.09 E-value: 2.60e-25
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DnaJ_zf | cd10719 | Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ... |
12-72 | 5.50e-21 | |||
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ 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 chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding. Pssm-ID: 199908 [Multi-domain] Cd Length: 65 Bit Score: 78.07 E-value: 5.50e-21
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Name | Accession | Description | Interval | E-value | |||
PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
2-83 | 1.37e-55 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 174.95 E-value: 1.37e-55
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
1-83 | 1.26e-36 | |||
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: 125.41 E-value: 1.26e-36
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
2-83 | 9.61e-31 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 110.24 E-value: 9.61e-31
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
3-83 | 1.43e-28 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 104.82 E-value: 1.43e-28
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
3-83 | 2.63e-28 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 103.92 E-value: 2.63e-28
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
2-83 | 3.54e-28 | |||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 103.65 E-value: 3.54e-28
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
2-82 | 6.93e-28 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 102.96 E-value: 6.93e-28
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
2-82 | 2.37e-27 | |||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 101.61 E-value: 2.37e-27
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
1-83 | 3.85e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 98.36 E-value: 3.85e-26
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
2-82 | 6.46e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 97.78 E-value: 6.46e-26
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
2-83 | 8.62e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 97.47 E-value: 8.62e-26
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
2-83 | 2.15e-25 | |||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 96.39 E-value: 2.15e-25
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DnaJ_C | pfam01556 | DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
1-83 | 2.60e-25 | |||
DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It is always found associated with pfam00226 and pfam00684. DnaJ is a chaperone associated with the Hsp70 heat-shock system involved in protein folding and renaturation after stress. The two C-terminal domains CTDI and CTDII, both incorporated in this family are necessary for maintaining the J-domains in their specific relative positions. Structural analysis of PDB:1nlt shows that PF00684 is nested within this DnaJ C-terminal region. Pssm-ID: 460251 [Multi-domain] Cd Length: 213 Bit Score: 93.09 E-value: 2.60e-25
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
2-83 | 2.03e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 91.06 E-value: 2.03e-23
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
3-83 | 2.36e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 90.98 E-value: 2.36e-23
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
1-83 | 2.42e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 90.88 E-value: 2.42e-23
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
2-82 | 5.19e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 89.87 E-value: 5.19e-23
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
2-82 | 6.07e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 89.90 E-value: 6.07e-23
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DnaJ_CXXCXGXG | pfam00684 | DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ... |
12-72 | 1.19e-22 | |||
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found. Pssm-ID: 459904 [Multi-domain] Cd Length: 65 Bit Score: 82.22 E-value: 1.19e-22
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PRK14279 | PRK14279 | molecular chaperone DnaJ; |
12-83 | 2.67e-22 | |||
molecular chaperone DnaJ; Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 87.87 E-value: 2.67e-22
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
2-72 | 7.61e-22 | |||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 86.81 E-value: 7.61e-22
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
1-83 | 8.75e-22 | |||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 86.44 E-value: 8.75e-22
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DnaJ_zf | cd10719 | Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ... |
12-72 | 5.50e-21 | |||
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ 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 chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding. Pssm-ID: 199908 [Multi-domain] Cd Length: 65 Bit Score: 78.07 E-value: 5.50e-21
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
2-82 | 9.05e-20 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 81.15 E-value: 9.05e-20
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
3-83 | 2.30e-19 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 79.93 E-value: 2.30e-19
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
12-83 | 9.49e-19 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 78.11 E-value: 9.49e-19
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
1-83 | 2.28e-18 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 76.89 E-value: 2.28e-18
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
3-83 | 8.63e-18 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 75.43 E-value: 8.63e-18
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
2-71 | 5.75e-17 | |||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 73.18 E-value: 5.75e-17
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
12-83 | 9.25e-17 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 72.52 E-value: 9.25e-17
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
12-82 | 1.12e-09 | |||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 52.90 E-value: 1.12e-09
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phage_xxxx | TIGR02642 | uncharacterized phage protein; This uncharacterized protein is found in prophage regions of ... |
27-62 | 1.83e-04 | |||
uncharacterized phage protein; This uncharacterized protein is found in prophage regions of Shewanella oneidensis MR-1, Vibrio vulnificus YJ016, Yersinia pseudotuberculosis IP 32953, and Aeromonas hydrophila ATCC7966. It appears to have regions of sequence similarity to phage lambda antitermination protein Q. [Mobile and extrachromosomal element functions, Prophage functions] Pssm-ID: 274243 [Multi-domain] Cd Length: 186 Bit Score: 37.55 E-value: 1.83e-04
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anti-TRAP | cd10748 | anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT ... |
47-72 | 8.20e-03 | |||
anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT binds to the TRAP protein, (tryptophan-activated trp RNA-binding attenuation protein), effectively disrupting interaction of TRAP with mRNAs. Upon binding of tryptophan, TRAP (which forms a complex of 11 identical subunits) interacts with a specific location in the leader RNA and blocks translation of the tryptophan biosynthetic operon. AT, in turn, recognizes the tryptophan-activated TRAP complex and prevents RNA binding. AT is expressed in response to high levels of uncharged tryptophan tRNA. AT contains a zinc-binding motif that closely resembles the zinc-binding motifs in the zinc-finger region of DnaJ/Hsp40. AT has been shown to form homo-dodecameric assemblies, and can actually do that in two different relative orientations, resulting in two different dodecamers. Recent data suggest that the trimeric form of AT may be the biologically relevant active complex. Pssm-ID: 199910 [Multi-domain] Cd Length: 52 Bit Score: 31.44 E-value: 8.20e-03
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Blast search parameters | ||||
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