ID   SYFA_THETH              Reviewed;         350 AA.
AC   P27001;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   24-NOV-2009, entry version 82.
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;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=99194858; PubMed=10092459; DOI=10.1006/jmbi.1999.2617;
RA   Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.;
RT   "Crystal structures of phenylalanyl-tRNA synthetase complexed with
RT   phenylalanine and a phenylalanyl-adenylate analogue.";
RL   J. Mol. Biol. 287:555-568(1999).
CC   -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC       diphosphate + L-phenylalanyl-tRNA(Phe).
CC   -!- COFACTOR: Binds 2 magnesium ions per tetramer.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Phe-tRNA synthetase alpha chain type 1 subfamily.
CC   -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC       1B70.
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DR   PDB; 1B70; X-ray; 2.70 A; A=1-350.
DR   PDB; 1B7Y; X-ray; 2.50 A; A=1-350.
DR   PDB; 2AKW; X-ray; 2.80 A; A=85-350.
DR   PDB; 2ALY; X-ray; 2.60 A; A=85-350.
DR   PDB; 2AMC; X-ray; 2.70 A; A=85-350.
DR   PDB; 2IY5; X-ray; 3.10 A; A=1-350.
DR   PDB; 3HFZ; X-ray; 2.90 A; A=1-350.
DR   PDBsum; 1B70; -.
DR   PDBsum; 1B7Y; -.
DR   PDBsum; 2AKW; -.
DR   PDBsum; 2ALY; -.
DR   PDBsum; 2AMC; -.
DR   PDBsum; 2IY5; -.
DR   PDBsum; 3HFZ; -.
DR   DisProt; DP00053; -.
DR   DIP; DIP:6104N; -.
DR   BRENDA; 6.1.1.20; 245.
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:0000049; F:tRNA binding; IEA:InterPro.
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; IPR004529; Phe-tRNA-synth_IIc_asu.
DR   InterPro; IPR004188; Phe-tRNA_synth_II_N.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase_acu.
DR   InterPro; IPR010978; tRNA_bd_arm.
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   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1    350       Phenylalanyl-tRNA synthetase alpha chain.
FT                                /FTId=PRO_0000126786.
FT   METAL       262    262       Magnesium.
FT   HELIX        16     31
FT   TURN         39     41
FT   HELIX        42     44
FT   HELIX        49     61
FT   HELIX        63     73
FT   HELIX        76     83
FT   HELIX       102    115
FT   TURN        116    118
FT   STRAND      126    129
FT   HELIX       130    133
FT   TURN        134    138
FT   STRAND      141    143
FT   HELIX       146    148
FT   STRAND      153    155
FT   STRAND      173    175
FT   STRAND      177    179
FT   HELIX       181    189
FT   STRAND      192    203
FT   STRAND      214    225
FT   HELIX       230    244
FT   STRAND      251    255
FT   STRAND      261    271
FT   TURN        272    275
FT   STRAND      276    286
FT   HELIX       288    300
FT   STRAND      311    318
FT   HELIX       319    327
FT   HELIX       332    336
FT   HELIX       340    343
FT   HELIX       344    346
SQ   SEQUENCE   350 AA;  39259 MW;  DEE0237F7CD9A461 CRC64;
     MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR GQELNAIKAA
     LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL HPITLMEREL VEIFRALGYQ
     AVEGPEVESE FFNFDALNIP EHHPARDMWD TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS
     PMQVRYMVAH TPPFRIVVPG RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL
     AQALFGPDSK VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER
     LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL
//