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Conserved domains on  [gi|12859584|dbj|BAB31701|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10788 super family cl32577
periplasmic folding chaperone; Provisional
19-68 3.51e-03

periplasmic folding chaperone; Provisional


The actual alignment was detected with superfamily member PRK10788:

Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 33.83  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12859584   19 ESDTPLQQV--SIEEILEEQRVQQQTRLEAEKLKV--------QTLKDRGLSIPRADTLD 68
Cdd:PRK10788 476 EAVKPLAQVrdQVTELVKRQKAEQQAKVDAEKLLAalkagkgeEAMKAAGLSFGEPKTLS 535
Sm_like super family cl00259
Sm and related proteins; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to ...
1-14 8.10e-03

Sm and related proteins; The eukaryotic Sm and Sm-like (LSm) proteins associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet. Sm-like proteins exist in archaea as well as prokaryotes that form heptameric and hexameric ring structures similar to those found in eukaryotes.


The actual alignment was detected with superfamily member cd01728:

Pssm-ID: 469694  Cd Length: 74  Bit Score: 31.33  E-value: 8.10e-03
                       10
               ....*....|....
gi 12859584  1 FVVRGENVVLLGEI 14
Cdd:cd01728 61 FIIRGENVVLLGEI 74
 
Name Accession Description Interval E-value
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
19-68 3.51e-03

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 33.83  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12859584   19 ESDTPLQQV--SIEEILEEQRVQQQTRLEAEKLKV--------QTLKDRGLSIPRADTLD 68
Cdd:PRK10788 476 EAVKPLAQVrdQVTELVKRQKAEQQAKVDAEKLLAalkagkgeEAMKAAGLSFGEPKTLS 535
LSm1 cd01728
Like-Sm protein 1; The eukaryotic LSm proteins (LSm1-7) assemble into a hetero-heptameric ring ...
1-14 8.10e-03

Like-Sm protein 1; The eukaryotic LSm proteins (LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. Accumulation of uridylated RNAs in an lsm1 mutant suggests an involvement of the LSm1-7 complex in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm1-7, together with Pat1, are also called the decapping activator. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet.


Pssm-ID: 212475  Cd Length: 74  Bit Score: 31.33  E-value: 8.10e-03
                       10
               ....*....|....
gi 12859584  1 FVVRGENVVLLGEI 14
Cdd:cd01728 61 FIIRGENVVLLGEI 74
 
Name Accession Description Interval E-value
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
19-68 3.51e-03

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 33.83  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12859584   19 ESDTPLQQV--SIEEILEEQRVQQQTRLEAEKLKV--------QTLKDRGLSIPRADTLD 68
Cdd:PRK10788 476 EAVKPLAQVrdQVTELVKRQKAEQQAKVDAEKLLAalkagkgeEAMKAAGLSFGEPKTLS 535
LSm1 cd01728
Like-Sm protein 1; The eukaryotic LSm proteins (LSm1-7) assemble into a hetero-heptameric ring ...
1-14 8.10e-03

Like-Sm protein 1; The eukaryotic LSm proteins (LSm1-7) assemble into a hetero-heptameric ring around the 3'-terminus of the gamma-methyl triphosphate (gamma-m-P3) capped U6 snRNA. Accumulation of uridylated RNAs in an lsm1 mutant suggests an involvement of the LSm1-7 complex in recognition of the 3' uridylation tag and recruitment of the decapping machinery. LSm1-7, together with Pat1, are also called the decapping activator. Members of this family share a highly conserved Sm fold containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet.


Pssm-ID: 212475  Cd Length: 74  Bit Score: 31.33  E-value: 8.10e-03
                       10
               ....*....|....
gi 12859584  1 FVVRGENVVLLGEI 14
Cdd:cd01728 61 FIIRGENVVLLGEI 74
 
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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