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A0A0K9NN98 · A0A0K9NN98_ZOSMR

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.

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 site599Zn2+ (UniProtKB | ChEBI)
Binding site603Zn2+ (UniProtKB | ChEBI)
Binding site718Zn2+ (UniProtKB | ChEBI)
Binding site722Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast
Cellular Componentmitochondrion
Molecular Functionalanine-tRNA ligase activity
Molecular Functionaminoacyl-tRNA editing activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-tRNA aminoacylation
Biological Processmitochondrial alanyl-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

    • ORF names
      ZOSMA_85G00250

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Finnish
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Zosteraceae > Zostera

Accessions

  • Primary accession
    A0A0K9NN98

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-761Alanyl-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. Alax-L subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    952
  • Mass (Da)
    105,161
  • Last updated
    2015-11-11 v1
  • MD5 Checksum
    E8725FD24F084CF225FE215EF7F773ED
MTTTSEAIEWPARKVRQTFIDFFVNNKSHKNWLSSPVVPHDDPTLLFANAGMNQYKPIFLGTVDPTNPLGKLVRACNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFNNQAIEWAWELLTEVYKLPKDNLYATYFGGDEKAHLPPDFEARDKWLTFLPASHVLPFGCKDNFWEMGDTGPCGPCTEIHFDRIGNRDASSLVNNDDPTCIEIWNLVFIQFNRESDSSLKMLPSKHVDTGMGFERLTSILQKKMSNYDTDVFLPIFDAIQKVTNAPHPYSGKLGEDDIGNVDMAYRVVADHIRTISFAVADGSRPGNDGREYVLRRILRRAVRYGKEILKAEEGFFSRLVNTVVHVMGDTFPELKHNEKKIKDIIEEEEASFGRTLLKGIEKFKRAARDVRDNKLNGQDAFLLWDTYGFPLDLTQLMAEESGLTVDVDGFNSAMNEAREKARSARNKFGGDSIAMDADATSELHKRRVATTNDSSKYIWNKDHGSVVKAIYSGSGFLETVSAGLDVGLVLESTSFYAEQGGQIYDTGFLEGPFGSFKVNNVQIFGGYILHIGSLNSGPSSLSIGASIVCKVDYARRSLIAPNHTCTHMLNFALKEVLGDHIDQKGSIVLPEKLRFDFSHGKPIHPEDLRKIESIVNLQIDDELEVYASEASLTDARNIVGLRAVFGEVYPDPVRVVSIGQKVEDLLSDPTKKQWLSISTEFCGGTHISNTREAKAFALLSEEGIAKGIRRVTAVTTASAISAQELAKSLDDEITEASKSEGSSLEKSVASLKSRLDAAIIPAARKADLRSRISKLQEQIMIAQKLVGKQNIEKAIQTATGIADAAVSEGRPFCVGSVDVGLDTTAIREAVCKVMQEKRLPIMLFSREEVSNKAVVYVGIPNNDKNGMATKWLKSALVPINGKGGGKGGVAQGQGTDGSRIDEAIAFAEKFAQMELK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LFYR01002060
EMBL· GenBank· DDBJ
KMZ57465.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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