LSM14 family protein having an Sm fold consisting of a five-stranded beta-sheet and an alpha-helix at the N-terminus, may be involved in essential RNA-processing tasks
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of ...
14-88
7.90e-40
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of Sm-like proteins that 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, that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm14 has an uncharacterized C-terminal domain containing a conserved DFDF box. In Xenopus laevis, LSm14 is an oocyte-specific constituent of ribonucleoprotein particles.
:
Pssm-ID: 212483 Cd Length: 74 Bit Score: 139.65 E-value: 7.90e-40
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
459-554
1.68e-32
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.
:
Pssm-ID: 430668 Cd Length: 104 Bit Score: 120.64 E-value: 1.68e-32
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of ...
14-88
7.90e-40
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of Sm-like proteins that 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, that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm14 has an uncharacterized C-terminal domain containing a conserved DFDF box. In Xenopus laevis, LSm14 is an oocyte-specific constituent of ribonucleoprotein particles.
Pssm-ID: 212483 Cd Length: 74 Bit Score: 139.65 E-value: 7.90e-40
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from ...
16-88
4.86e-39
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from the newt Pleurodeles walt, and its orthologs from fungi, animals, plants and apicomplexans. The domain is also found in Dcp3p and the human EDC3/FLJ21128 protein where it is fused to the the Rossmanoid YjeF-N domain. In addition both EDC3 and Scd6p are found fused to the FDF domain.
Pssm-ID: 463675 Cd Length: 75 Bit Score: 137.63 E-value: 4.86e-39
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
459-554
1.68e-32
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.
Pssm-ID: 430668 Cd Length: 104 Bit Score: 120.64 E-value: 1.68e-32
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of ...
14-88
7.90e-40
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of Sm-like proteins that 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, that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm14 has an uncharacterized C-terminal domain containing a conserved DFDF box. In Xenopus laevis, LSm14 is an oocyte-specific constituent of ribonucleoprotein particles.
Pssm-ID: 212483 Cd Length: 74 Bit Score: 139.65 E-value: 7.90e-40
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from ...
16-88
4.86e-39
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from the newt Pleurodeles walt, and its orthologs from fungi, animals, plants and apicomplexans. The domain is also found in Dcp3p and the human EDC3/FLJ21128 protein where it is fused to the the Rossmanoid YjeF-N domain. In addition both EDC3 and Scd6p are found fused to the FDF domain.
Pssm-ID: 463675 Cd Length: 75 Bit Score: 137.63 E-value: 4.86e-39
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
459-554
1.68e-32
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.
Pssm-ID: 430668 Cd Length: 104 Bit Score: 120.64 E-value: 1.68e-32
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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