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Conserved domains on  [gi|27363461|ref|NP_057153|]
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mitochondrial import inner membrane translocase subunit TIM16 [Homo sapiens]

Protein Classification

Pam16 domain-containing protein (domain architecture ID 10508427)

Pam16 domain-containing protein

Graphical summary

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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 2.89e-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: 2.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363461     1 MAKYLA-QIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAASNLSGLSLQEAQQILNVSK-LSPEEVQKNYE 78
Cdd:pfam03656   1 MAHRAAiQVIITGTQVVGKAFARAYRQEAAAQRVAAGAGTNASRRGTAKSNYGGISLDESCQILNVEEdLNMEEVNKRYE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 27363461    79 HLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREKGQMPHT 125
Cdd:pfam03656  81 HLFEVNDKSKGGSFYLQSKVYRAKERLDEELAIREKEAKAKAGDAST 127
 
Name Accession Description Interval E-value
Pam16 pfam03656
Pam16; The Pam16 protein is the fifth essential subunit of the pre-sequence ...
1-125 2.89e-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: 2.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363461     1 MAKYLA-QIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAASNLSGLSLQEAQQILNVSK-LSPEEVQKNYE 78
Cdd:pfam03656   1 MAHRAAiQVIITGTQVVGKAFARAYRQEAAAQRVAAGAGTNASRRGTAKSNYGGISLDESCQILNVEEdLNMEEVNKRYE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 27363461    79 HLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREKGQMPHT 125
Cdd:pfam03656  81 HLFEVNDKSKGGSFYLQSKVYRAKERLDEELAIREKEAKAKAGDAST 127
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
50-105 3.86e-05

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 39.83  E-value: 3.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27363461   50 NLSG----LSLQEAQQILNVSKLSPEE-VQKNYEHLFKVNDKSVGGSFYLQSKVVRAKERL 105
Cdd:PTZ00100  54 DLKGfenpMSKSEAYKILNISPTASKErIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
 
Name Accession Description Interval E-value
Pam16 pfam03656
Pam16; The Pam16 protein is the fifth essential subunit of the pre-sequence ...
1-125 2.89e-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: 2.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27363461     1 MAKYLA-QIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAASNLSGLSLQEAQQILNVSK-LSPEEVQKNYE 78
Cdd:pfam03656   1 MAHRAAiQVIITGTQVVGKAFARAYRQEAAAQRVAAGAGTNASRRGTAKSNYGGISLDESCQILNVEEdLNMEEVNKRYE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 27363461    79 HLFKVNDKSVGGSFYLQSKVVRAKERLDEELKIQAQEDREKGQMPHT 125
Cdd:pfam03656  81 HLFEVNDKSKGGSFYLQSKVYRAKERLDEELAIREKEAKAKAGDAST 127
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
50-105 3.86e-05

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 39.83  E-value: 3.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27363461   50 NLSG----LSLQEAQQILNVSKLSPEE-VQKNYEHLFKVNDKSVGGSFYLQSKVVRAKERL 105
Cdd:PTZ00100  54 DLKGfenpMSKSEAYKILNISPTASKErIREAHKQLMLRNHPDNGGSTYIASKVNEAKDLL 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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