A0A977PTQ9 · A0A977PTQ9_9ACAR
- ProteinSignal recognition particle 54 kDa protein
- GeneSrp54k
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids464 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER).
Catalytic activity
- GTP + H2O = GDP + phosphate + H+This reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | signal recognition particle, endoplasmic reticulum targeting | |
Molecular Function | 7S RNA binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | endoplasmic reticulum signal peptide binding | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Biological Process | SRP-dependent cotranslational protein targeting to membrane, translocation |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSignal recognition particle 54 kDa protein
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Acariformes > Sarcoptiformes > Oribatida > Brachypylina > Ameronothroidea > Fortuyniidae > Fortuynia
Accessions
- Primary accessionA0A977PTQ9
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 262-275 | SRP54-type proteins GTP-binding | ||||
Sequence: PISFIGTGEHMDDF |
Domain
The M domain binds the 7SL RNA in presence of SRP19 and binds the signal sequence of presecretory proteins.
The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which binds GTP and forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the SRP receptor subunit SRPRA. The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another. SRP receptor compaction upon binding with cargo-loaded SRP and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.
Sequence similarities
Belongs to the GTP-binding SRP family. SRP54 subfamily.
Family and domain databases
Sequence
- Sequence statusFragment
- Length464
- Mass (Da)51,115
- Last updated2023-02-22 v1
- Checksum9C4841EEF82EEF42
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: R | ||||||
Non-terminal residue | 464 | |||||
Sequence: L |