RecName: Full=Mitochondrial import inner membrane translocase subunit Tim16; AltName: Full=Protein black pearl
J domain-containing protein( domain architecture ID 84)
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
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DnaJ super family | cl02542 | DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ... |
1-117 | 3.76e-33 | |||
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. The actual alignment was detected with superfamily member pfam03656: Pssm-ID: 413365 Cd Length: 127 Bit Score: 113.13 E-value: 3.76e-33
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Name | Accession | Description | Interval | E-value | |||
Pam16 | pfam03656 | Pam16; The Pam16 protein is the fifth essential subunit of the pre-sequence ... |
1-117 | 3.76e-33 | |||
Pam16; The Pam16 protein is the fifth essential subunit of the pre-sequence translocase-associated protein import motor (PAM). In Saccharomyces cerevisiae, Pam16 is required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane. Pam16 has a degenerate J domain. J-domain proteins play important regulatory roles as co-chaperones, recruiting Hsp70 partners and accelerating the ATP-hydrolysis step of the chaperone cycle. Pam16's J-like domain strongly interacts with Pam18's J domain, leading to a productive interaction of Pam18 with mtHsp70 at the mitochondria import channel. Pam18 stimulates the ATPase activity of mtHsp70. Pssm-ID: 252088 Cd Length: 127 Bit Score: 113.13 E-value: 3.76e-33
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PTZ00100 | PTZ00100 | DnaJ chaperone protein; Provisional |
56-108 | 4.21e-06 | |||
DnaJ chaperone protein; Provisional Pssm-ID: 240265 Cd Length: 116 Bit Score: 42.92 E-value: 4.21e-06
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Name | Accession | Description | Interval | E-value | |||
Pam16 | pfam03656 | Pam16; The Pam16 protein is the fifth essential subunit of the pre-sequence ... |
1-117 | 3.76e-33 | |||
Pam16; The Pam16 protein is the fifth essential subunit of the pre-sequence translocase-associated protein import motor (PAM). In Saccharomyces cerevisiae, Pam16 is required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane. Pam16 has a degenerate J domain. J-domain proteins play important regulatory roles as co-chaperones, recruiting Hsp70 partners and accelerating the ATP-hydrolysis step of the chaperone cycle. Pam16's J-like domain strongly interacts with Pam18's J domain, leading to a productive interaction of Pam18 with mtHsp70 at the mitochondria import channel. Pam18 stimulates the ATPase activity of mtHsp70. Pssm-ID: 252088 Cd Length: 127 Bit Score: 113.13 E-value: 3.76e-33
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PTZ00100 | PTZ00100 | DnaJ chaperone protein; Provisional |
56-108 | 4.21e-06 | |||
DnaJ chaperone protein; Provisional Pssm-ID: 240265 Cd Length: 116 Bit Score: 42.92 E-value: 4.21e-06
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Blast search parameters | ||||
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