ID   SYFA_THESM              Reviewed;         503 AA.
AC   C6A236;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00282};
DE   AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282};
DE            Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00282};
GN   Name=pheS {ECO:0000255|HAMAP-Rule:MF_00282}; OrderedLocusNames=TSIB_0616;
OS   Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12597 / MM 739;
RX   PubMed=19447963; DOI=10.1128/aem.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT   sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT   analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(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         Evidence={ECO:0000255|HAMAP-Rule:MF_00282};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00282};
CC       Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_00282};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00282}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Phe-tRNA synthetase alpha subunit type 2 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00282}.
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; CP001463; ACS89681.1; -; Genomic_DNA.
DR   RefSeq; WP_015848901.1; NC_012883.1.
DR   AlphaFoldDB; C6A236; -.
DR   SMR; C6A236; -.
DR   STRING; 604354.TSIB_0616; -.
DR   EnsemblBacteria; ACS89681; ACS89681; TSIB_0616.
DR   GeneID; 8095604; -.
DR   KEGG; tsi:TSIB_0616; -.
DR   eggNOG; arCOG00410; Archaea.
DR   HOGENOM; CLU_025086_2_2_2; -.
DR   OMA; QIEGWVM; -.
DR   OrthoDB; 22747at2157; -.
DR   Proteomes; UP000009079; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00282; Phe_tRNA_synth_alpha2; 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; IPR022917; Phe_tRNA_ligase_alpha_bac/arc.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF46785; SSF46785; 2.
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..503
FT                   /note="Phenylalanine--tRNA ligase alpha subunit"
FT                   /id="PRO_1000204841"
FT   BINDING         346
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         385..387
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         426
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         428
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="shared with beta subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
FT   BINDING         451
FT                   /ligand="L-phenylalanine"
FT                   /ligand_id="ChEBI:CHEBI:58095"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00282"
SQ   SEQUENCE   503 AA;  58155 MW;  5C45DF0AF6894490 CRC64;
     MELSYQEKVT LIKLRELKKA SFDELVKETG LDQVAVMRAI LWLQSKGLAK LHEKQKRVVK
     ITELGEKYAK IGLPERRALK LLVEKGKVTL EDLREVLSED ELRPIIGILR KEGWATVRKE
     DDVLTLELTE KGKEALTKER PIDIALKVLA EKREVEAREI EELLSLKELK TRKIGEEDAK
     AEREVEITDE GLRIASEGLE LKEEVSILTP ELIKSGGWKN VEFKHFNIHA PVKRLYPGKK
     QPYRTFLDKI RRKLIEMGFI EMTVESLIET QFWNFDALFQ PQNHPARDWT DTYQLKYPKY
     GFLPDETLVE RVKASHEHGW ITGSRGWGYK WDPRTAMLLM PRAHATALSA RQLGKGVQIP
     GKYFAIQRVF RPDVLDRTHL IEFNQVDGFV VGETLTFKHL LGILKRFAVE IAGAKKVKFL
     PDYYPFTEPS VQMSAYHEEL GWVEFGGAGV FREEMTKPLG IDVPVIAWGI GIDRLAMFKL
     GIDDIRYLFS YDLKWLREAK LVW