ID   SYFA_ENCCU              Reviewed;         475 AA.
AC   Q8SRG9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable phenylalanine--tRNA ligase alpha subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE            Short=PheRS;
GN   OrderedLocusNames=ECU07_1660;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A5K9S0};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL590447; CAD25697.1; -; Genomic_DNA.
DR   RefSeq; NP_586093.1; NM_001041715.1.
DR   AlphaFoldDB; Q8SRG9; -.
DR   SMR; Q8SRG9; -.
DR   STRING; 284813.Q8SRG9; -.
DR   GeneID; 859527; -.
DR   KEGG; ecu:ECU07_1660; -.
DR   VEuPathDB; MicrosporidiaDB:ECU07_1660; -.
DR   HOGENOM; CLU_025086_2_2_1; -.
DR   InParanoid; Q8SRG9; -.
DR   OMA; QIEGWVM; -.
DR   OrthoDB; 733355at2759; -.
DR   Proteomes; UP000000819; Chromosome VII.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
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; IPR040725; PheRS_DBD3.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..475
FT                   /note="Probable phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000388407"
FT   REGION          2..151
FT                   /note="Contains the major tRNA-Phe binding sites"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         351..353
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         391
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         393
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000250|UniProtKB:A5K9S0"
FT   BINDING         417
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
SQ   SEQUENCE   475 AA;  54685 MW;  2B219D395F8E4618 CRC64;
     MTAVAQKIIE NLKMQDEVRS SDIDAPYSEI HGALISLESR GICNVKMEES YEEVLTPEGE
     EVERSGSQEY LLLESIGEDG MSIEELERHS LGKMNAFRNK WIRREGNRVF RNVESIEDTV
     RNMVISMKRG TASAEEVEAL RKRKLVSRRK KIVFIATKGP MFFDNTSYVT ELTSEMVLDG
     SYRDLSFKHY NFNAEGNAPQ CGSIHPLMKI REDFRRIFIE LGFSEMATNQ YVESSFWNFD
     ALFQPQNHPS RDAHDTFFLL NPELSTDFPS DYLKEVGETH RGGKYNSLGY MSNWDIKEAQ
     KNILRTHTTS VSARNLYRLA KKEFKPAKLF SIDKVFRNET VDATHLAEFH QVEGLVVGKG
     LNLTHLMGIL REFFNRLGMG DIRFKPAFNP YTEPSMEVFG YHKGMDRWIE VGNSGVFRPE
     MLRPMGFDSD VSVVAWGLSL ERPAMIKYGL KNIRELVGHK VDIEFSRKSE ICFFD