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Conserved domains on  [gi|19113862|ref|NP_592950|]
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TIM23 translocase complex subunit Tim15 [Schizosaccharomyces pombe]

Protein Classification

DNL-type zinc finger protein( domain architecture ID 10524414)

DNL-type zinc finger protein similar to Saccharomyces cerevisiae mitochondrial protein import protein ZIM17 that acts as an Hsp70-specific chaperone that prevents self-aggregation of the matrix Hsp70 chaperones SSC1 and SSQ1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-DNL pfam05180
DNL zinc finger; The domain is named after a short C-terminal motif of D(N/H)L. This domain is ...
 78-140 9.94e-40

DNL zinc finger; The domain is named after a short C-terminal motif of D(N/H)L. This domain is a novel zinc-finger protein essential for protein import into mitochondria.


:

Pssm-ID: 461571  Cd Length: 64  Bit Score: 128.84  E-value: 9.94e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113862    78 VSFTCTVCNTRSNHNFSKQAYHNGTVLVQCPKCKNRHLMADHLKIFSEERVTIEDILAKKGET 140
Cdd:pfam05180   2 LTFTCKVCNTRSTKTFSKQAYHKGVVIIQCPGCKNRHLIADNLGWFGDKKKNIEDILAEKGEK 64
 
Name Accession Description Interval E-value
zf-DNL pfam05180
DNL zinc finger; The domain is named after a short C-terminal motif of D(N/H)L. This domain is ...
 78-140 9.94e-40

DNL zinc finger; The domain is named after a short C-terminal motif of D(N/H)L. This domain is a novel zinc-finger protein essential for protein import into mitochondria.


Pssm-ID: 461571  Cd Length: 64  Bit Score: 128.84  E-value: 9.94e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113862    78 VSFTCTVCNTRSNHNFSKQAYHNGTVLVQCPKCKNRHLMADHLKIFSEERVTIEDILAKKGET 140
Cdd:pfam05180   2 LTFTCKVCNTRSTKTFSKQAYHKGVVIIQCPGCKNRHLIADNLGWFGDKKKNIEDILAEKGEK 64
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
 104-150 3.52e-03

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 37.03  E-value: 3.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 19113862  104 LVQCPKCKNRHlMADHLkifseervtIEDILAKKGETFKKGYGQVIN 150
Cdd:PRK04173  86 LVECKKCKKRY-RADHL---------IEELGIDAEGLSNEELKELIR 122
 
Name Accession Description Interval E-value
zf-DNL pfam05180
DNL zinc finger; The domain is named after a short C-terminal motif of D(N/H)L. This domain is ...
 78-140 9.94e-40

DNL zinc finger; The domain is named after a short C-terminal motif of D(N/H)L. This domain is a novel zinc-finger protein essential for protein import into mitochondria.


Pssm-ID: 461571  Cd Length: 64  Bit Score: 128.84  E-value: 9.94e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113862    78 VSFTCTVCNTRSNHNFSKQAYHNGTVLVQCPKCKNRHLMADHLKIFSEERVTIEDILAKKGET 140
Cdd:pfam05180   2 LTFTCKVCNTRSTKTFSKQAYHKGVVIIQCPGCKNRHLIADNLGWFGDKKKNIEDILAEKGEK 64
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
 104-150 3.52e-03

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 37.03  E-value: 3.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 19113862  104 LVQCPKCKNRHlMADHLkifseervtIEDILAKKGETFKKGYGQVIN 150
Cdd:PRK04173  86 LVECKKCKKRY-RADHL---------IEELGIDAEGLSNEELKELIR 122
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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