signal recognition particle (SRP) subunit SRP68 family protein similar to SRP subunit SRP68 that is part of the SRP complex that has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane
RNA-binding domain of signal recognition particle subunit 68; Signal recognition particles ...
1-259
6.25e-60
RNA-binding domain of signal recognition particle subunit 68; Signal recognition particles (SRPs) are ribonucleoprotein complexes that target particular nascent pre-secretory proteins to the endoplasmic reticulum. SRP68 is one of the two largest proteins found in SRPs (the other being SRP72), and it forms a heterodimer with SRP72. Heterodimer formation is essential for SRP function. This model characterizes the N-terminal RNA-binding domain SRP68-RBD, a tetratricopeptide-like module. Interactions between SRP68-RBD and SRP RNA (7SL RNA) are thought to facilitate a conformation of SRP RNA that is required for interactions with ribosomal RNA.
The actual alignment was detected with superfamily member pfam16969:
Pssm-ID: 473954 Cd Length: 562 Bit Score: 199.44 E-value: 6.25e-60
RNA-binding signal recognition particle 68; SRP68 is a family that is part of the SRP or ...
1-259
6.25e-60
RNA-binding signal recognition particle 68; SRP68 is a family that is part of the SRP or signal recognition particle complex. This complex, consisting of six proteins and a 7SL-RNA is necessary for guiding the emerging proteins designed for the membrane towards the translocation pore. SRP68 forms a stable heterodimer with SRP72, a protein with a TPR repeat. Specific RNA-binding of SRP68 is mediated by the N-terminal domain of approximately 200 residues of this family.
Pssm-ID: 465323 Cd Length: 562 Bit Score: 199.44 E-value: 6.25e-60
RNA-binding signal recognition particle 68; SRP68 is a family that is part of the SRP or ...
1-259
6.25e-60
RNA-binding signal recognition particle 68; SRP68 is a family that is part of the SRP or signal recognition particle complex. This complex, consisting of six proteins and a 7SL-RNA is necessary for guiding the emerging proteins designed for the membrane towards the translocation pore. SRP68 forms a stable heterodimer with SRP72, a protein with a TPR repeat. Specific RNA-binding of SRP68 is mediated by the N-terminal domain of approximately 200 residues of this family.
Pssm-ID: 465323 Cd Length: 562 Bit Score: 199.44 E-value: 6.25e-60
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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