SYFA_YEAST
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 03-AUG-2022, entry version 197.
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; 110.
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; P15625; -.
DR PRIDE; P15625; -.
DR TopDownProteomics; P15625; -.
DR EnsemblFungi; YFL022C_mRNA; YFL022C; YFL022C.
DR GeneID; 850522; -.
DR KEGG; sce:YFL022C; -.
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 BioCyc; YEAST:G3O-30438-MON; -.
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: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 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; IPR040586; PheRS_DBD2.
DR InterPro; IPR040725; PheRS_DBD3.
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 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
