diphthamide biosynthesis 4, isoform B [Drosophila melanogaster]
diphthamide biosynthesis protein 4( domain architecture ID 10446362)
diphthamide biosynthesis protein 4 (DPH4) is a J domain-containing CSL-type zinc finger protein that is required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue
List of domain hits
Name | Accession | Description | Interval | E-value | ||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
3-72 | 2.42e-21 | ||
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: 82.52 E-value: 2.42e-21
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zf-CSL | pfam05207 | CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ... |
138-179 | 4.48e-09 | ||
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine. : Pssm-ID: 398744 Cd Length: 55 Bit Score: 50.32 E-value: 4.48e-09
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Name | Accession | Description | Interval | E-value | ||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
3-72 | 2.42e-21 | ||
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: 82.52 E-value: 2.42e-21
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
1-78 | 3.95e-18 | ||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 75.14 E-value: 3.95e-18
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
3-64 | 1.29e-16 | ||
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: 69.88 E-value: 1.29e-16
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
2-65 | 7.50e-15 | ||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 65.72 E-value: 7.50e-15
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
1-72 | 2.19e-14 | ||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 69.92 E-value: 2.19e-14
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
3-72 | 3.44e-13 | ||
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: 66.47 E-value: 3.44e-13
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zf-CSL | pfam05207 | CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ... |
138-179 | 4.48e-09 | ||
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine. Pssm-ID: 398744 Cd Length: 55 Bit Score: 50.32 E-value: 4.48e-09
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
3-72 | 4.10e-06 | ||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 45.97 E-value: 4.10e-06
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Name | Accession | Description | Interval | E-value | |||
DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
3-72 | 2.42e-21 | |||
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: 82.52 E-value: 2.42e-21
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
1-78 | 3.95e-18 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 75.14 E-value: 3.95e-18
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
3-73 | 9.24e-18 | |||
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: 75.51 E-value: 9.24e-18
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
3-64 | 1.29e-16 | |||
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: 69.88 E-value: 1.29e-16
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
2-65 | 7.50e-15 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 65.72 E-value: 7.50e-15
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
1-72 | 2.19e-14 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 69.92 E-value: 2.19e-14
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
3-72 | 1.78e-13 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 67.09 E-value: 1.78e-13
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DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
3-72 | 3.44e-13 | |||
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: 66.47 E-value: 3.44e-13
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
3-72 | 8.94e-13 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 65.18 E-value: 8.94e-13
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PRK14279 | PRK14279 | molecular chaperone DnaJ; |
3-72 | 1.85e-12 | |||
molecular chaperone DnaJ; Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 64.37 E-value: 1.85e-12
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
3-72 | 2.75e-12 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 64.05 E-value: 2.75e-12
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
3-72 | 5.70e-12 | |||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 62.94 E-value: 5.70e-12
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
3-72 | 1.02e-11 | |||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 62.16 E-value: 1.02e-11
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
3-72 | 1.21e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 61.49 E-value: 1.21e-11
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
1-65 | 2.19e-11 | |||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 56.73 E-value: 2.19e-11
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
3-72 | 3.22e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 60.63 E-value: 3.22e-11
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
3-72 | 4.39e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 60.59 E-value: 4.39e-11
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
3-72 | 4.44e-11 | |||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 60.57 E-value: 4.44e-11
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
3-72 | 6.89e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 59.78 E-value: 6.89e-11
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
3-72 | 9.32e-11 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 59.42 E-value: 9.32e-11
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
3-72 | 1.29e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 59.09 E-value: 1.29e-10
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
1-72 | 6.97e-10 | |||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 56.92 E-value: 6.97e-10
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
3-72 | 8.26e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 56.67 E-value: 8.26e-10
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
4-72 | 8.99e-10 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 56.54 E-value: 8.99e-10
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
3-72 | 2.17e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 55.40 E-value: 2.17e-09
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zf-CSL | pfam05207 | CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which ... |
138-179 | 4.48e-09 | |||
CSL zinc finger; This is a zinc binding motif which contains four cysteine residues which chelate zinc. This domain is often found associated with a pfam00226 domain. This domain is named after the conserved motif of the final cysteine. Pssm-ID: 398744 Cd Length: 55 Bit Score: 50.32 E-value: 4.48e-09
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
3-72 | 8.76e-09 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 53.52 E-value: 8.76e-09
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
3-72 | 4.27e-08 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 51.55 E-value: 4.27e-08
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
3-72 | 4.51e-08 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 51.63 E-value: 4.51e-08
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PRK10266 | PRK10266 | curved DNA-binding protein; |
3-85 | 8.01e-08 | |||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 50.59 E-value: 8.01e-08
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
3-72 | 1.10e-07 | |||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 50.49 E-value: 1.10e-07
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
3-72 | 1.48e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 49.93 E-value: 1.48e-07
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
3-72 | 2.05e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 49.60 E-value: 2.05e-07
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
4-72 | 4.14e-07 | |||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 49.05 E-value: 4.14e-07
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
3-72 | 8.55e-07 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 48.02 E-value: 8.55e-07
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
3-72 | 3.47e-06 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 45.97 E-value: 3.47e-06
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terminal_TopJ | NF037946 | terminal organelle assembly protein TopJ; |
3-72 | 4.10e-06 | |||
terminal organelle assembly protein TopJ; Pssm-ID: 468284 [Multi-domain] Cd Length: 440 Bit Score: 45.97 E-value: 4.10e-06
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
4-72 | 4.40e-05 | |||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 42.75 E-value: 4.40e-05
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PTZ00100 | PTZ00100 | DnaJ chaperone protein; Provisional |
5-33 | 5.21e-05 | |||
DnaJ chaperone protein; Provisional Pssm-ID: 240265 Cd Length: 116 Bit Score: 40.99 E-value: 5.21e-05
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hscB | TIGR00714 | Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ... |
23-108 | 2.99e-04 | |||
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization] Pssm-ID: 211601 [Multi-domain] Cd Length: 155 Bit Score: 39.48 E-value: 2.99e-04
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djlA | PRK09430 | co-chaperone DjlA; |
3-35 | 1.93e-03 | |||
co-chaperone DjlA; Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 37.87 E-value: 1.93e-03
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hscB | PRK05014 | co-chaperone HscB; Provisional |
3-71 | 4.96e-03 | |||
co-chaperone HscB; Provisional Pssm-ID: 179914 [Multi-domain] Cd Length: 171 Bit Score: 36.04 E-value: 4.96e-03
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Blast search parameters | ||||
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