A0A1F1QZJ4 · A0A1F1QZJ4_9MICC
- ProteinProline--tRNA ligase
- GeneproS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids605 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
Catalytic activity
- tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + diphosphate
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aminoacyl-tRNA editing activity | |
Molecular Function | ATP binding | |
Molecular Function | proline-tRNA ligase activity | |
Biological Process | prolyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProline--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Rothia
Accessions
- Primary accessionA0A1F1QZJ4
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-503 | Aminoacyl-transfer RNA synthetases class-II family profile | ||||
Sequence: RRAAPGVYTWLPLGLKVLRKVENIVREEMNAIGAQEVLFPALLPREPYEATNRWEEYGDNLFRLQDRKGADMLLAPTHEEMFTLLVKDLYSSYKDLPLYIYQIQNKYRDEARPRSGLLRGREFVMKDSYSFTVDDEGLNEAYEAHRAAYQRIFNRLGLDTVIVTAQSGAMGGSRSEEFLHPTPVGEDTFVRSAGGYAANVEAVTTVVPADIDFTDTPAAIVLDTPESPTIETLVAQMNDLHPQVTGGELTAEQTLKCFVGAVITPAGERKLFAVGVPGDREVDLGRVEVNIGALMGIGGEIEVEAASEEDLKKFPQLVKGYIGPGLTLDQPMLGENTEERQTATGIPFFVDPRVVRGTSWVTGANEHGKHVANLVYGRDFNADGTLEACEVREGDPAPDGSGPLIAARGVEMGHIFQLGRKYAEALGLKVLDQNGKLQTVTMGSYGIGVTRALAAIAEGNHDEKGLIWP |
Domain
Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain.
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length605
- Mass (Da)66,135
- Last updated2017-02-15 v1
- ChecksumCC978B64F6C3F750