ID   AASDA_XENLA             Reviewed;         412 AA.
AC   Q08B09;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Alanyl-tRNA editing protein Aarsd1-A;
DE   AltName: Full=Alanyl-tRNA synthetase domain-containing protein 1-A;
GN   Name=aarsd1-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC       incorrectly charged tRNA(Ala). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Alax-L subfamily. {ECO:0000305}.
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DR   EMBL; BC124925; AAI24926.1; -; mRNA.
DR   AlphaFoldDB; Q08B09; -.
DR   SMR; Q08B09; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF55186; SSF55186; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Protein biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..412
FT                   /note="Alanyl-tRNA editing protein Aarsd1-A"
FT                   /id="PRO_0000277469"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         112
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         208
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  45773 MW;  9DBA97F780A1FF00 CRC64;
     MAFHCQRDCY ATELLTEVVS CHPAQLKLEN GGKKNTVSGF NVLLKDTVLF PEGGGQPDDR
     GFIGEVPVLR VIRQGPDAVH FVASPLDPAT EVLVKIDWNR RFDHMQQHSG QHLVTAIADS
     LYGFKTTSWD LGRQRSVIEL DTPLVTTEQL EAIEKIANQK IREHVPVHVR LITVDDPEFD
     MVRSRGLPDD HAGPVRIIDI EGVDANMCCG THVRNLSDLQ MIKILGTEKG KKNKTNLIFL
     SGERVLKYVS RSYNTEKTLT SLLKNGPEEH IEAVDKLQKS VKALQKNNLT LLRDLAVLTA
     ENFKSKADRG KFFSLHRKEG DNEFMNIIAN VIGTEDTLLF LTIGDEKTSG LFLLAGPPGI
     VEKFGPRVCE ILDGKGAGKC GRFQGKANKM SQRAEVEVLL QKVISSVEIT QE