ID   SYFA_CAMJE              Reviewed;         330 AA.
AC   Q9PP34; Q0PA01;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Phenylalanyl-tRNA synthetase alpha chain;
DE            EC=6.1.1.20;
DE   AltName: Full=Phenylalanine--tRNA ligase alpha chain;
DE            Short=PheRS;
GN   Name=pheS; OrderedLocusNames=Cj0897;
OS   Campylobacter jejuni.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 11168 / Serotype O:2;
RX   MEDLINE=20150912; PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W.,
RA   Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA   Whitehead S., Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer (By similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha chain type 1 subfamily.
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DR   EMBL; AL111168; CAL35018.1; -; Genomic_DNA.
DR   PIR; A81363; A81363.
DR   RefSeq; YP_002344296.1; -.
DR   HSSP; P27001; 1JJC.
DR   IntAct; Q9PP34; 12.
DR   GeneID; 905193; -.
DR   GenomeReviews; AL111168_GR; Cj0897.
DR   OMA; Q9PP34; FRASYFP.
DR   BioCyc; CJEJ192222:CJ0897C-MON; -.
DR   BRENDA; 6.1.1.20; 255835.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00281; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR002319; Phe-tRNA-synth_IIc-rel.
DR   InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR018157; Phe-tRNA-synth_IIc_C.
DR   InterPro; IPR004188; Phe-tRNA_synth_II_N.
DR   PANTHER; PTHR11538; tRNA-synt_2d; 1.
DR   Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 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; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    330       Phenylalanyl-tRNA synthetase alpha chain.
FT                                /FTId=PRO_0000126681.
FT   METAL       246    246       Magnesium (By similarity).
SQ   SEQUENCE   330 AA;  37987 MW;  02013BD56B6AEAF2 CRC64;
     MQNFIEQIQK CENLNDLEAI RISVLGKKGI LTEGFTKLKE LEDEAKKEFA AKLNAQKEIF
     NEAYLAKFKD LENLALEERM KQDALNFNYF DESITTGALH PVMSTMDKII EYFIALNFSI
     EKGPLIEDDF HNFEALNLPK SHPARDMQDT FYFDDKRLLR TQTSPVQIRT MLAQKPPIRM
     IAPGAVFRRD FDITHTPMFH QVEGLVVEEG QKVSFANLKS VLEDFLRYMF GDVKVRFRPS
     FFPFTEPSAE VDISCVFCKG KGCRVCKHTG WLEVLGCGIV DPNVYNFVGY ENVSGYAFGL
     GVERFAMLLH QIPDLRSLFE GDLRLLEQFR
//