ID   SYFA_NOSCE              Reviewed;         474 AA.
AC   C4V6K5;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 54.
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   ORFNames=NCER_100038;
OS   Nosema ceranae (strain BRL01) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae; Nosema.
OX   NCBI_TaxID=578460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRL01;
RX   PubMed=19503607; DOI=10.1371/journal.ppat.1000466;
RA   Cornman R.S., Chen Y.P., Schatz M.C., Street C., Zhao Y., Desany B.,
RA   Egholm M., Hutchison S., Pettis J.S., Lipkin W.I., Evans J.D.;
RT   "Genomic analyses of the microsporidian Nosema ceranae, an emergent
RT   pathogen of honey bees.";
RL   PLoS Pathog. 5:E1000466-E1000466(2009).
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}.
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DR   EMBL; ACOL01000001; EEQ83176.1; -; Genomic_DNA.
DR   RefSeq; XP_002996847.1; XM_002996801.1.
DR   AlphaFoldDB; C4V6K5; -.
DR   SMR; C4V6K5; -.
DR   STRING; 578460.C4V6K5; -.
DR   EnsemblFungi; EEQ83176; EEQ83176; NCER_100038.
DR   KEGG; nce:NCER_100038; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_100038; -.
DR   HOGENOM; CLU_025086_2_2_1; -.
DR   InParanoid; C4V6K5; -.
DR   OMA; QIEGWVM; -.
DR   Proteomes; UP000009082; Unassembled WGS sequence.
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..474
FT                   /note="Probable phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000388409"
FT   REGION          1..150
FT                   /note="Contains the major tRNA-Phe binding sites"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         350..352
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         390
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         392
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         416
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
SQ   SEQUENCE   474 AA;  54686 MW;  3A7E000DA753532D CRC64;
     MSLSQKILEL LKNTETIKST DIDVRSNELY PVLLSLASKE IISFTFKEQI IYKLTEEGES
     ILKNGSYEFN LYNSIGDNGM ELLEVDKYNL GKVNAFKNKW IKKVGDKVYK SADNVEDNVK
     NMLNNVTNKI YQKEEISLLK KRKLIYQAKE VVYFIKKGPL YGKDSDNITE LISKMVISGE
     YKHLNFKPYN FNTKGNIQSQ GALHPLMKVR EEIRKIFLEM GFNEMTTNKF VESSFWNFDT
     LFQPQNHPSR DAHDTFFMKT PSTTSYIPID YMKMIKKIHS VGDFDSDGHF SDWDIKEAEK
     NILRSHTTAC STRTMLEIAK GEFISAKLFS IDRVFRNEAL DATHLAEFNQ VEGLIVAKGL
     TLGNLMGYLK RFFEKLGITD IKFKPAYNPY TEPSMEVFGY HKGLKKWIEV GNSGMFRPEV
     LRPMGFDKDV RAIGFGLSLE RPTMIKYGIS NIRDLIGPKV DIEFIKKSEM CFFN