ID   SYFA_YEAST              Reviewed;         503 AA.
AC   P15625; D6VTK8;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE            Short=PheRS;
GN   Name=FRS2; OrderedLocusNames=YFL022C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3049607; DOI=10.1016/s0021-9258(19)37603-3;
RA   Sanni A., Mirande M., Ebel J.-P., Boulanger Y., Waller J.-P., Fasiolo F.;
RT   "Structure and expression of the genes encoding the alpha and beta subunits
RT   of yeast phenylalanyl-tRNA synthetase.";
RL   J. Biol. Chem. 263:15407-15415(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE, AND DOMAIN TRNA-BINDING.
RX   PubMed=2644133; DOI=10.1016/0014-5793(89)80500-9;
RA   Fasiolo F., Sanni A., Potier S., Ebel J.-P., Boulanger Y.;
RT   "Identification of the major tRNA(Phe) binding domain in the tetrameric
RT   structure of cytoplasmic phenylalanyl-tRNA synthetase from baker's yeast.";
RL   FEBS Lett. 242:351-356(1989).
RN   [5]
RP   ACETYLATION AT SER-2.
RX   PubMed=9298649; DOI=10.1002/elps.1150180810;
RA   Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA   Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA   Payne W.E.;
RT   "Proteome studies of Saccharomyces cerevisiae: identification and
RT   characterization of abundant proteins.";
RL   Electrophoresis 18:1347-1360(1997).
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.
CC   -!- INTERACTION:
CC       P15625; P15624: FRS1; NbExp=2; IntAct=EBI-18678, EBI-18684;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally erroneously assigned as a beta subunit.
CC       {ECO:0000305|PubMed:3049607}.
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DR   EMBL; J03965; AAA35152.1; -; Genomic_DNA.
DR   EMBL; D50617; BAA09216.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12418.1; -; Genomic_DNA.
DR   PIR; S56232; YFBYAC.
DR   RefSeq; NP_116631.1; NM_001179944.2.
DR   AlphaFoldDB; P15625; -.
DR   SMR; P15625; -.
DR   BioGRID; 31124; 116.
DR   ComplexPortal; CPX-1738; Phenylalanyl-tRNA synthetase complex.
DR   DIP; DIP-5428N; -.
DR   IntAct; P15625; 11.
DR   MINT; P15625; -.
DR   STRING; 4932.YFL022C; -.
DR   iPTMnet; P15625; -.
DR   MaxQB; P15625; -.
DR   PaxDb; 4932-YFL022C; -.
DR   PeptideAtlas; P15625; -.
DR   TopDownProteomics; P15625; -.
DR   EnsemblFungi; YFL022C_mRNA; YFL022C; YFL022C.
DR   GeneID; 850522; -.
DR   KEGG; sce:YFL022C; -.
DR   AGR; SGD:S000001872; -.
DR   SGD; S000001872; FRS2.
DR   VEuPathDB; FungiDB:YFL022C; -.
DR   eggNOG; KOG2784; Eukaryota.
DR   GeneTree; ENSGT00390000006387; -.
DR   HOGENOM; CLU_025086_2_0_1; -.
DR   InParanoid; P15625; -.
DR   OMA; QIEGWVM; -.
DR   OrthoDB; 4619at2759; -.
DR   BioCyc; YEAST:G3O-30438-MONOMER; -.
DR   BioGRID-ORCS; 850522; 6 hits in 10 CRISPR screens.
DR   PRO; PR:P15625; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P15625; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IDA:SGD.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IMP:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
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; IDA:SGD.
DR   CDD; cd00496; PheRS_alpha_core; 1.
DR   Gene3D; 1.10.10.2320; -; 1.
DR   Gene3D; 1.10.10.2330; -; 1.
DR   Gene3D; 3.30.1370.240; -; 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; IPR040586; PheRS_DBD2.
DR   InterPro; IPR040725; PheRS_DBD3.
DR   NCBIfam; TIGR00468; pheS; 1.
DR   PANTHER; PTHR11538:SF40; PHENYLALANINE--TRNA LIGASE ALPHA SUBUNIT; 1.
DR   PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF18554; PheRS_DBD2; 1.
DR   Pfam; PF18553; PheRS_DBD3; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298649"
FT   CHAIN           2..503
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_0000126828"
FT   REGION          2..173
FT                   /note="Contains the major tRNA-Phe binding sites"
FT   BINDING         333
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         374..376
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         414
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   BINDING         416
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         440
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y285"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:9298649"
FT   CONFLICT        177
FT                   /note="N -> S (in Ref. 1; AAA35152)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289
FT                   /note="D -> E (in Ref. 1; AAA35152)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  57511 MW;  50B7EAC675AB559B CRC64;
     MSDFQLEILK KLDELDEIKS TLATFPQHGS QDVLSALNSL KAHNKLEFSK VDTVTYDLTK
     EGAQILNEGS YEIKLVKLIQ ELGQLQIKDV MSKLGPQVGK VGQARAFKNG WIAKNASNEL
     ELSAKLQNTD LNELTDETQS ILAQIKNNSH LDSIDAKILN DLKKRKLIAQ GKITDFNVTK
     GPEFSTDLTK LETDLTSDMV STNAYKDLKF KPYNFNSQGV QISSGALHPL NKVREEFRQI
     FFSMGFTEMP SNQYVETGFW NFDALYVPQQ HPARDLQDTF YIKDPLTADL PDDKTYMDNI
     KAVHEQGRFG SIGYRYNWKP EECQKLVLRT HSTAISARML HDLAKDPKPT RLFSIDRVFR
     NEAVDATHLA EFHQVEGVLA DYNITLGDLI KFMEEFFERM GVTGLRFKPT YNPYTEPSME
     IFSWHEGLQK WVEIGNSGMF RPEMLESMGL PKDLRVLGWG LSLERPTMIK YKVQNIRELL
     GHKVSLDFIE TNPAARLDED LYE
//