ID   SYFAA_XENLA             Reviewed;         498 AA.
AC   Q6AZG6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit A;
DE            EC=6.1.1.20 {ECO:0000250|UniProtKB:Q9Y285};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit A;
DE            Short=PheRS;
GN   Name=farsa-a; Synonyms=farsla-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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) +
CC         L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668,
CC         Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y285};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19414;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y285};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A5K9S0};
CC   -!- SUBUNIT: Heterotetramer; dimer of two heterodimers formed by alpha and
CC       beta subunits. {ECO:0000250|UniProtKB:Q9Y285}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q505J8}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
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DR   EMBL; BC078035; AAH78035.1; -; mRNA.
DR   RefSeq; NP_001087130.1; NM_001093661.1.
DR   AlphaFoldDB; Q6AZG6; -.
DR   SMR; Q6AZG6; -.
DR   BioGRID; 103879; 1.
DR   IntAct; Q6AZG6; 1.
DR   DNASU; 447019; -.
DR   GeneID; 447019; -.
DR   KEGG; xla:447019; -.
DR   CTD; 447019; -.
DR   Xenbase; XB-GENE-946398; farsa.S.
DR   OrthoDB; 733355at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 447019; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; ISS:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; ISS:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; ISS:UniProtKB.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR040724; PheRS_DBD1.
DR   InterPro; IPR040586; PheRS_DBD2.
DR   InterPro; IPR040725; PheRS_DBD3.
DR   Pfam; PF18552; PheRS_DBD1; 1.
DR   Pfam; PF18554; PheRS_DBD2; 1.
DR   Pfam; PF18553; PheRS_DBD3; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00468; pheS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   2: Evidence at transcript level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..498
FT                   /note="Phenylalanine--tRNA ligase alpha subunit A"
FT                   /id="PRO_0000280452"
FT   BINDING         330
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         373..375
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         413
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with heterodimeric partner"
FT                   /evidence="ECO:0000250|UniProtKB:A5K9S0"
FT   BINDING         439
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
SQ   SEQUENCE   498 AA;  56753 MW;  88609B0FFC25C2DF CRC64;
     MADNSVSEQL LQRLQDGGSK GVDSLELAAL LGVEHQQVVG AVKSLQCLGE IIQAEQRSSK
     KWELSSEGEE IGREGSHEAR VFQTLPKEGL LQAQLMKQPF SKVGFSKAMS NKWIRLDKAA
     EGGPRIYRVV DSIEDTVKEK LQLILKGRAD DVNEKDRNEL KKRKLVNEVT VKSYWVTKGS
     GFSTSITKQE TDLTPEMIAS GSWREKQFKG YNFDALGVMP ECGHLHPLLK VRTQFRQIFL
     EMGFTEMPTN NFIESSFWNF DALFQPQQHP ARDQHDTFFL QDPALATEFP MEYLERVKKV
     HSEGGYGSQG YKYDWSIHEA QKNILRTHTT AVSARMLYKL ALQKDFTPVK YFSIDRVFRN
     ETLDATHLAE FHQIEGVVAD RGLTLGNLMG VLKEFFHKLG ITKLRFKPAY NPYTEPSMEV
     FSYHEGLKKW VEVGNSGLFR PELLLPMGLP EDVNVLGWGL SLERPTMIRY GIKNIRELVG
     HKVNLQMVYD SPICRLDA