ID   SYFA_BLOPB              Reviewed;         331 AA.
AC   Q492V1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=BPEN_366;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000016; AAZ40991.1; -; Genomic_DNA.
DR   RefSeq; YP_277866.1; -.
DR   GeneID; 3563040; -.
DR   GenomeReviews; CP000016_GR; BPEN_366.
DR   KEGG; bpn:BPEN_366; -.
DR   HOGENOM; Q492V1; -.
DR   OMA; Q492V1; FRASYFP.
DR   BioCyc; CBLO291272:BPEN_366-MON; -.
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    331       Phenylalanyl-tRNA synthetase alpha chain.
FT                                /FTId=PRO_0000231966.
FT   METAL       254    254       Magnesium (By similarity).
SQ   SEQUENCE   331 AA;  38623 MW;  0B0AD09644B76BC1 CRC64;
     MSLDPVKKLV ILAKSNIMQS NNMDALEAIR IKFLGKKGYL NQHIKNLNDT SLDIKPKLGA
     AINQAKEDIY TLLIERKNIL QSKNIKNTLI TDTLDVTLPG RLSDIGTHHP ITSTIKRMKI
     FFNTLGFSVI HGPEIEDDYF NFDALNIPKY HPSRDEHDTF WFDEKRLLRT HTSGVQIRAM
     INKTPPIRII SFGRVYRKDY DQHHTPMFHQ MEGLIVDSNV NFSYLKKILY DFLYNFFETD
     IILRFRPSYF PFTEPSAEID VMKKQETGNW LELLGCGMVH PKILHHVDID TEKFSGFAFG
     IGIERLTMLQ YNIDDIRVFF KNDLQFLDQF K
//