A0A5A7R291 · A0A5A7R291_STRAF
- ProteinAlanine--tRNA ligase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1145 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Catalytic activity
- ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | alanine-tRNA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | mitochondrial alanyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlanine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > lamiids > Lamiales > Orobanchaceae > Buchnereae > Striga
Accessions
- Primary accessionA0A5A7R291
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 60-950 | Alanyl-transfer RNA synthetases family profile | ||||
Sequence: WPASRVRETFIKFFEGKSHVNFRSSPVVPHNDPTLLFANAGMNQFKPIFLGTADPNTELSKLRRACNTQKCIRAGGKHNDLDDVYGLPDDRIYATYFGGDEKLGLPADNEAKDHWLRFLPPSRVLPFGCKDNFWEMGDTGPCGPCTEIHFDRIGGRDAASFVNNDDPTVIEIWNLVFIQFNREADGSLKSLPAKHVDTGMGFERLTSILQNKMSNYDTDIFFPIFDAIQQATGAHPYSGKVGSDDVDNVDMAYRVVADHIRTISFAIADGSRPGNEGREYVLRRILRRAVRYGTEVLKAQQGFFHGLVQVVLEVMGDVFPELKEHALKIREIIADEETSFGRTLTKGYEQALEADGVMVGALEAGAARAAHRFLISFGASEAGVASGCISGEMSKRMSKESERGVGSGIGMHRSAPNASHAVAACGTAITAILFSNLACWFVKIIHAIPAMALPLAPFGNTGANYLILVGVKKNPSELDARKESRMSGIEKFKKAAQEVQGRDAFDLWDTYGFPLDLTQLMADERGLTVDVEGFNIAMDKARERSRKAQNKVMSYLTADISRQSATFKNLIALNQAGGTIGMDADATASLHKRGVAVTDDSVKYTWFQDHASVIKAVYTGSEFLESAGPGEEVGIILETTSFYAEQGALPPYYGGFAMAVAKSMASTEIFDTGIIEGSDGIFEVSNVQIYGGFVLHIGSFSGKTGRLYIGDKVVCKVNYDRRMLIAPNHTCTHILNYALREVLGNHVDQKGSIVLPEKLRFDFSHGKPVKPEELKKIELIVNEQIESKLNVYSKETKLEDAKRINGLRAVFGEVYPDPVRVVAIGRKVEDLLANPDNEEWLSISAELCGGTHISNTMDAKGFVLLSEEGIAKGIRRVTGVTMDCAFKALEL |
Domain
Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,145
- Mass (Da)124,744
- Last updated2019-11-13 v1
- ChecksumBBAFED4FD1E9AFEA
Keywords
- Technical term