mitochondrial import inner membrane translocase subunit TIM16 [Homo sapiens]
mitochondrial import inner membrane translocase subunit TIM16( domain architecture ID 10508427)
mitochondrial import inner membrane translocase subunit TIM16 regulates ATP-dependent protein translocation into the mitochondrial matrix
List of domain hits
Name | Accession | Description | Interval | E-value | |||
Pam16 | pfam03656 | Pam16; The Pam16 protein is the fifth essential subunit of the pre-sequence ... |
1-125 | 3.39e-56 | |||
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: 170.91 E-value: 3.39e-56
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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 ... |
1-125 | 3.39e-56 | |||
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: 170.91 E-value: 3.39e-56
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PTZ00100 | PTZ00100 | DnaJ chaperone protein; Provisional |
50-105 | 4.52e-05 | |||
DnaJ chaperone protein; Provisional Pssm-ID: 240265 Cd Length: 116 Bit Score: 39.83 E-value: 4.52e-05
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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 ... |
1-125 | 3.39e-56 | |||
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: 170.91 E-value: 3.39e-56
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PTZ00100 | PTZ00100 | DnaJ chaperone protein; Provisional |
50-105 | 4.52e-05 | |||
DnaJ chaperone protein; Provisional Pssm-ID: 240265 Cd Length: 116 Bit Score: 39.83 E-value: 4.52e-05
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Blast search parameters | ||||
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