dnaJ homolog subfamily A member 4 isoform 6 [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DnaJ_bact super family | cl37091 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
7-114 | 8.81e-40 | |||
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. The actual alignment was detected with superfamily member TIGR02349: Pssm-ID: 274090 [Multi-domain] Cd Length: 354 Bit Score: 138.89 E-value: 8.81e-40
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DnaJ_C super family | cl47019 | C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ... |
106-144 | 1.93e-03 | |||
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70. The actual alignment was detected with superfamily member cd10747: Pssm-ID: 199909 [Multi-domain] Cd Length: 158 Bit Score: 37.40 E-value: 1.93e-03
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Name | Accession | Description | Interval | E-value | |||
DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
7-114 | 8.81e-40 | |||
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: 138.89 E-value: 8.81e-40
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
7-114 | 3.02e-34 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 124.87 E-value: 3.02e-34
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
7-65 | 2.17e-33 | |||
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: 114.11 E-value: 2.17e-33
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
7-74 | 2.07e-32 | |||
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: 114.03 E-value: 2.07e-32
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
5-60 | 2.49e-26 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 95.76 E-value: 2.49e-26
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
7-57 | 4.72e-26 | |||
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: 94.92 E-value: 4.72e-26
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DnaJ_C | cd10747 | C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ... |
106-144 | 1.93e-03 | |||
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70. Pssm-ID: 199909 [Multi-domain] Cd Length: 158 Bit Score: 37.40 E-value: 1.93e-03
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DnaJ_C | pfam01556 | DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
106-142 | 1.96e-03 | |||
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: 38.00 E-value: 1.96e-03
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Name | Accession | Description | Interval | E-value | |||
DnaJ_bact | TIGR02349 | chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ... |
7-114 | 8.81e-40 | |||
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: 138.89 E-value: 8.81e-40
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PRK10767 | PRK10767 | chaperone protein DnaJ; Provisional |
7-114 | 3.02e-34 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 236757 [Multi-domain] Cd Length: 371 Bit Score: 124.87 E-value: 3.02e-34
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
1-114 | 8.88e-34 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 123.81 E-value: 8.88e-34
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DnaJ | pfam00226 | DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ... |
7-65 | 2.17e-33 | |||
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: 114.11 E-value: 2.17e-33
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DnaJ | COG0484 | DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ... |
7-74 | 2.07e-32 | |||
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: 114.03 E-value: 2.07e-32
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
5-107 | 2.59e-32 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 119.77 E-value: 2.59e-32
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
7-114 | 3.43e-30 | |||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 114.32 E-value: 3.43e-30
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PRK14280 | PRK14280 | molecular chaperone DnaJ; |
7-98 | 3.65e-30 | |||
molecular chaperone DnaJ; Pssm-ID: 237656 [Multi-domain] Cd Length: 376 Bit Score: 114.05 E-value: 3.65e-30
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
7-114 | 1.54e-29 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 112.17 E-value: 1.54e-29
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
2-108 | 4.09e-29 | |||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 111.84 E-value: 4.09e-29
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PRK14276 | PRK14276 | chaperone protein DnaJ; Provisional |
4-99 | 8.08e-29 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237653 [Multi-domain] Cd Length: 380 Bit Score: 110.56 E-value: 8.08e-29
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PRK14297 | PRK14297 | molecular chaperone DnaJ; |
7-113 | 1.17e-28 | |||
molecular chaperone DnaJ; Pssm-ID: 184611 [Multi-domain] Cd Length: 380 Bit Score: 110.26 E-value: 1.17e-28
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
1-114 | 1.22e-27 | |||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 107.61 E-value: 1.22e-27
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PRK14281 | PRK14281 | chaperone protein DnaJ; Provisional |
7-122 | 6.95e-27 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237657 [Multi-domain] Cd Length: 397 Bit Score: 105.66 E-value: 6.95e-27
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
7-104 | 2.22e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 104.08 E-value: 2.22e-26
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DnaJ | smart00271 | DnaJ molecular chaperone homology domain; |
5-60 | 2.49e-26 | |||
DnaJ molecular chaperone homology domain; Pssm-ID: 197617 [Multi-domain] Cd Length: 60 Bit Score: 95.76 E-value: 2.49e-26
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DnaJ | cd06257 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
7-57 | 4.72e-26 | |||
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: 94.92 E-value: 4.72e-26
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PRK14284 | PRK14284 | chaperone protein DnaJ; Provisional |
5-97 | 6.28e-26 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237658 [Multi-domain] Cd Length: 391 Bit Score: 103.00 E-value: 6.28e-26
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
2-110 | 1.06e-25 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 101.99 E-value: 1.06e-25
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
1-108 | 1.76e-25 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 101.44 E-value: 1.76e-25
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
7-105 | 1.88e-25 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 101.50 E-value: 1.88e-25
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
1-71 | 1.49e-24 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 99.10 E-value: 1.49e-24
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SEC63 | COG5407 | Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ... |
7-61 | 2.62e-24 | |||
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 444165 [Multi-domain] Cd Length: 61 Bit Score: 90.83 E-value: 2.62e-24
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
4-109 | 2.93e-24 | |||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 98.38 E-value: 2.93e-24
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PRK14279 | PRK14279 | molecular chaperone DnaJ; |
4-66 | 1.41e-23 | |||
molecular chaperone DnaJ; Pssm-ID: 237655 [Multi-domain] Cd Length: 392 Bit Score: 96.34 E-value: 1.41e-23
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CbpA | COG2214 | Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; |
1-71 | 2.19e-23 | |||
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription]; Pssm-ID: 441816 [Multi-domain] Cd Length: 91 Bit Score: 89.39 E-value: 2.19e-23
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
7-104 | 6.84e-23 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 94.42 E-value: 6.84e-23
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PRK14287 | PRK14287 | chaperone protein DnaJ; Provisional |
7-97 | 1.06e-22 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237659 [Multi-domain] Cd Length: 371 Bit Score: 93.92 E-value: 1.06e-22
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
1-68 | 3.82e-22 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 92.30 E-value: 3.82e-22
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PRK14282 | PRK14282 | chaperone protein DnaJ; Provisional |
7-109 | 2.15e-21 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 184603 [Multi-domain] Cd Length: 369 Bit Score: 90.24 E-value: 2.15e-21
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PRK10266 | PRK10266 | curved DNA-binding protein; |
7-105 | 2.43e-21 | |||
curved DNA-binding protein; Pssm-ID: 182347 [Multi-domain] Cd Length: 306 Bit Score: 89.11 E-value: 2.43e-21
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
7-71 | 7.64e-21 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 87.69 E-value: 7.64e-21
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PRK14285 | PRK14285 | chaperone protein DnaJ; Provisional |
7-106 | 3.67e-19 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172773 [Multi-domain] Cd Length: 365 Bit Score: 84.27 E-value: 3.67e-19
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PRK14300 | PRK14300 | chaperone protein DnaJ; Provisional |
7-114 | 7.41e-17 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 172788 [Multi-domain] Cd Length: 372 Bit Score: 77.75 E-value: 7.41e-17
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PRK14296 | PRK14296 | chaperone protein DnaJ; Provisional |
2-103 | 2.94e-16 | |||
chaperone protein DnaJ; Provisional Pssm-ID: 237666 [Multi-domain] Cd Length: 372 Bit Score: 76.14 E-value: 2.94e-16
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PRK14288 | PRK14288 | molecular chaperone DnaJ; |
4-74 | 3.96e-16 | |||
molecular chaperone DnaJ; Pssm-ID: 172776 [Multi-domain] Cd Length: 369 Bit Score: 75.50 E-value: 3.96e-16
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DjlA | COG1076 | DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; |
7-63 | 2.06e-13 | |||
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440694 [Multi-domain] Cd Length: 75 Bit Score: 62.89 E-value: 2.06e-13
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PTZ00341 | PTZ00341 | Ring-infected erythrocyte surface antigen; Provisional |
2-74 | 6.24e-12 | |||
Ring-infected erythrocyte surface antigen; Provisional Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 64.04 E-value: 6.24e-12
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ZUO1 | COG5269 | Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
3-65 | 1.58e-09 | |||
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 56.58 E-value: 1.58e-09
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djlA | PRK09430 | co-chaperone DjlA; |
8-55 | 1.82e-08 | |||
co-chaperone DjlA; Pssm-ID: 236512 [Multi-domain] Cd Length: 267 Bit Score: 52.89 E-value: 1.82e-08
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PHA03102 | PHA03102 | Small T antigen; Reviewed |
9-70 | 2.70e-05 | |||
Small T antigen; Reviewed Pssm-ID: 222986 [Multi-domain] Cd Length: 153 Bit Score: 42.74 E-value: 2.70e-05
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PHA02624 | PHA02624 | large T antigen; Provisional |
9-61 | 5.88e-05 | |||
large T antigen; Provisional Pssm-ID: 222912 [Multi-domain] Cd Length: 647 Bit Score: 43.05 E-value: 5.88e-05
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PTZ00100 | PTZ00100 | DnaJ chaperone protein; Provisional |
5-36 | 3.63e-04 | |||
DnaJ chaperone protein; Provisional Pssm-ID: 240265 Cd Length: 116 Bit Score: 38.68 E-value: 3.63e-04
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hscB | PRK01356 | co-chaperone HscB; Provisional |
7-64 | 1.28e-03 | |||
co-chaperone HscB; Provisional Pssm-ID: 167217 [Multi-domain] Cd Length: 166 Bit Score: 37.93 E-value: 1.28e-03
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DnaJ_C | cd10747 | C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ... |
106-144 | 1.93e-03 | |||
C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 protein mediates oligomerization and binding to denatured polypeptide substrate. DnaJ/Hsp40 is a widely conserved heat-shock protein. It prevents the aggregation of unfolded substrate and forms a ternary complex with both substrate and DnaK/Hsp70; the N-terminal J-domain of DnaJ/Hsp40 stimulates the ATPase activity of DnaK/Hsp70. Pssm-ID: 199909 [Multi-domain] Cd Length: 158 Bit Score: 37.40 E-value: 1.93e-03
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DnaJ_C | pfam01556 | DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
106-142 | 1.96e-03 | |||
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: 38.00 E-value: 1.96e-03
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Blast search parameters | ||||
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