dnaJ homolog subfamily B member 13 isoform X7 [Homo sapiens]
J domain-containing protein( domain architecture ID 10180526)
J domain-containing protein similar to the N-terminal conserved domain (called J domain) of DnaJ-like proteins, which is involved in regulating the ATPase activity of heat shock protein 70 (Hsp70) by ATP hydrolysis
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DnaJ_C | cd10747 | C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ... |
35-161 | 6.80e-38 | |||
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: 127.54 E-value: 6.80e-38
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Name | Accession | Description | Interval | E-value | |||
DnaJ_C | cd10747 | C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ... |
35-161 | 6.80e-38 | |||
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: 127.54 E-value: 6.80e-38
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DnaJ_C | pfam01556 | DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
33-158 | 2.07e-36 | |||
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: 125.44 E-value: 2.07e-36
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
37-170 | 1.94e-32 | |||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 119.54 E-value: 1.94e-32
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Name | Accession | Description | Interval | E-value | ||||
DnaJ_C | cd10747 | C-terminal substrate binding domain of DnaJ and HSP40; The C-terminal region of the DnaJ/Hsp40 ... |
35-161 | 6.80e-38 | ||||
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: 127.54 E-value: 6.80e-38
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DnaJ_C | pfam01556 | DnaJ C terminal domain; This family consists of the C terminal region of the DnaJ protein. It ... |
33-158 | 2.07e-36 | ||||
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: 125.44 E-value: 2.07e-36
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PTZ00037 | PTZ00037 | DnaJ_C chaperone protein; Provisional |
37-170 | 1.94e-32 | ||||
DnaJ_C chaperone protein; Provisional Pssm-ID: 240236 [Multi-domain] Cd Length: 421 Bit Score: 119.54 E-value: 1.94e-32
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PRK14286 | PRK14286 | chaperone protein DnaJ; Provisional |
29-171 | 1.01e-14 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 172774 [Multi-domain] Cd Length: 372 Bit Score: 70.40 E-value: 1.01e-14
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PRK14299 | PRK14299 | chaperone protein DnaJ; Provisional |
33-171 | 1.70e-13 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237667 [Multi-domain] Cd Length: 291 Bit Score: 66.50 E-value: 1.70e-13
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PRK14278 | PRK14278 | chaperone protein DnaJ; Provisional |
39-171 | 1.72e-13 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237654 [Multi-domain] Cd Length: 378 Bit Score: 67.00 E-value: 1.72e-13
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PRK14283 | PRK14283 | chaperone protein DnaJ; Provisional |
35-171 | 6.00e-13 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 184604 [Multi-domain] Cd Length: 378 Bit Score: 65.62 E-value: 6.00e-13
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PRK14293 | PRK14293 | molecular chaperone DnaJ; |
37-171 | 1.43e-12 | ||||
molecular chaperone DnaJ; Pssm-ID: 237663 [Multi-domain] Cd Length: 374 Bit Score: 64.24 E-value: 1.43e-12
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PRK14298 | PRK14298 | chaperone protein DnaJ; Provisional |
35-171 | 7.45e-12 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 184612 [Multi-domain] Cd Length: 377 Bit Score: 62.56 E-value: 7.45e-12
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PRK14291 | PRK14291 | chaperone protein DnaJ; Provisional |
29-158 | 9.36e-12 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237661 [Multi-domain] Cd Length: 382 Bit Score: 62.09 E-value: 9.36e-12
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PRK14301 | PRK14301 | chaperone protein DnaJ; Provisional |
29-171 | 1.94e-10 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237668 [Multi-domain] Cd Length: 373 Bit Score: 58.21 E-value: 1.94e-10
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PRK14292 | PRK14292 | chaperone protein DnaJ; Provisional |
29-169 | 4.29e-10 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237662 [Multi-domain] Cd Length: 371 Bit Score: 57.21 E-value: 4.29e-10
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PRK14277 | PRK14277 | chaperone protein DnaJ; Provisional |
35-171 | 8.41e-10 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 184599 [Multi-domain] Cd Length: 386 Bit Score: 56.35 E-value: 8.41e-10
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PRK14289 | PRK14289 | molecular chaperone DnaJ; |
34-169 | 2.77e-09 | ||||
molecular chaperone DnaJ; Pssm-ID: 237660 [Multi-domain] Cd Length: 386 Bit Score: 54.84 E-value: 2.77e-09
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PRK14294 | PRK14294 | chaperone protein DnaJ; Provisional |
5-171 | 3.23e-09 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 237664 [Multi-domain] Cd Length: 366 Bit Score: 54.77 E-value: 3.23e-09
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PRK14290 | PRK14290 | chaperone protein DnaJ; Provisional |
28-171 | 2.64e-07 | ||||
chaperone protein DnaJ; Provisional Pssm-ID: 172778 [Multi-domain] Cd Length: 365 Bit Score: 49.16 E-value: 2.64e-07
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PRK14295 | PRK14295 | molecular chaperone DnaJ; |
40-169 | 6.12e-07 | ||||
molecular chaperone DnaJ; Pssm-ID: 237665 [Multi-domain] Cd Length: 389 Bit Score: 48.31 E-value: 6.12e-07
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Blast search parameters | ||||
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