ID   SYFA_AYWBP              Reviewed;         343 AA.
AC   Q2NJZ3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=AYWB_133;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(2006).
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; CP000061; ABC65250.1; -; Genomic_DNA.
DR   RefSeq; YP_456329.1; -.
DR   GeneID; 3865826; -.
DR   GenomeReviews; CP000061_GR; AYWB_133.
DR   KEGG; ayw:AYWB_133; -.
DR   HOGENOM; Q2NJZ3; -.
DR   OMA; Q2NJZ3; FRASYFP.
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    343       Phenylalanyl-tRNA synthetase alpha chain.
FT                                /FTId=PRO_1000006797.
FT   METAL       256    256       Magnesium (By similarity).
SQ   SEQUENCE   343 AA;  39875 MW;  D1630DFA97EFBF6A CRC64;
     MQTKIKKLIA QFHTSLQKNK YDLDKLMILD KEFLGKKGIL FELTQELKNL PHAQKSVAGK
     LINFLKQEII FTLQKEKETL KRNQLNAKIL QEEIDPTLPA FNFCQGSTHP LNQIIEKIED
     LFLSLGYEIK EGNEIETLFY NFEMLNMGKG HPAREMQDSF YIDSQKLLRT HTSNIQVKEM
     KARQGKPLKI ISSGKVYRKD DDDATHSHQF MQLEGLVIDK NINFSVLKET LLLITKELFG
     NSQEIHLRPS YFPFTEPSIE VDLVITKKDG TKEYLEILGA GLVHPQVLKN ANYDPEKYQG
     FAFGIGIERI AMIKYQIENI RYFYANDIRF LKQFARNADN ENY
//