A0A2G6BP93 · A0A2G6BP93_UNCCC

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 Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site557Zn2+ (UniProtKB | ChEBI)
Binding site561Zn2+ (UniProtKB | ChEBI)
Binding site659Zn2+ (UniProtKB | ChEBI)
Binding site663Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alanine--tRNA ligase
  • EC number
  • Alternative names
    • Alanyl-tRNA synthetase
      (AlaRS
      )

Gene names

    • Name
      alaS
    • ORF names
      CSB55_09160

Organism names

Accessions

  • Primary accession
    A0A2G6BP93

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain2-702Alanyl-transfer RNA synthetases family profile

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 status
    Complete
  • Length
    868
  • Mass (Da)
    97,675
  • Last updated
    2018-01-31 v1
  • Checksum
    EBB7041091468BFB
MLTSKEIRQSFIDFFVEKQHKSIKSAPVVPHTDPTLLFTIAGMTQFKDIFLGLKDPDTPRAVNSQKCIRAGGKHNDLEEVGKDGYHHTFFEMLGNWSFADYYKEEAIVWAWELVTKVWKLPKDKLYATVYKDDDEAFEIWKNKTDIANDHIQYHGDKSNFWEMGDTGPCGPCSEIHIDMGEERCAWQDKEDHVCGVNIDCHRFIELWNLVFIQYNRDENGKLHPLKNKYIDTGAGLERICQVLQGVNSNYETDLFMPLIEKTVELSGVPYSKGKDGTPHRVIADHLRTLCFAVSDGGFPSNEGRGYVLRRILRRASRFGRLINLKEPFMFKLVDTVTDVMGHYYTELAENKKLITSVIKSEEERFNLTLDKGLIRFEEIVNRSEHGLISGNDAFVLYDTYGFPLDLTRLLAEEKNMTIDEDGFHIEMEQQRIRARNAGNFKQTESILKEMGVASSTNTGFYGYDELSKEVRILYSKNLDDNKIILILDNTPFYAESGGQVADRGMITGENGEFEVYDVQKESDVILHYAEVKNLKSTEGVFIARVDREYRKNISRNHTATHLLHAGLKSLLGDHVKQKGSLVRADCLRFDFTHFNRVTPEELRKLEETVNEEVRKCTPVVTSEMSIEEAQKSGATALFGEKYGETVRVVDVPGFSKELCGGIHLNFTGEIGLIKIISESSVASGIRRIEAVTGVFAEKKVREEEDFIEKIKNTINVPQNKVLEKIEKIMAENVELHKKLEAGKMKSAGNLLDDLIAEADTVNGIKFVAADLGEKNSGDLRKIGDTLRDKIGKGIGVLFAVNGGKASVLVTVTKDLTSDYKAGIIVNKVASYLGGKGGGRPDMAMAGGKEIKNIPTALKKVKEILAEIN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PDOO01000046
EMBL· GenBank· DDBJ
PID27111.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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