ID   SYFA_ANAVT              Reviewed;         330 AA.
AC   Q3MB99;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=Ava_2115;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000117; ABA21737.1; -; Genomic_DNA.
DR   RefSeq; YP_322632.1; -.
DR   GeneID; 3680373; -.
DR   GenomeReviews; CP000117_GR; Ava_2115.
DR   KEGG; ava:Ava_2115; -.
DR   NMPDR; fig|240292.3.peg.1714; -.
DR   HOGENOM; Q3MB99; -.
DR   OMA; Q3MB99; FRASYFP.
DR   BioCyc; AVAR240292:AVA_2115-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    330       Phenylalanyl-tRNA synthetase alpha chain.
FT                                /FTId=PRO_0000231959.
FT   METAL       257    257       Magnesium (By similarity).
SQ   SEQUENCE   330 AA;  37120 MW;  15E63CCC5DB6723A CRC64;
     MTSNLEAQLL ALRQEGEQAI AAADTLERLE ELRVSYLGKK GQLGALLRSM GQMSAEERPK
     IGAIANTVKE ALQASLDKQR ESLESAQIQA QLDAETLDVT MPGIYKPQGR IHPLNGIIDR
     ALDVFVGLGY TVAQGLEMET DYYNFEALNT PPDHPARDMQ DTFYLPDGNL LRTHTSSVQI
     RYMEKEEPPI HIVAPGRVYR RDNVDATHSA VFHQIELLAI DEGLTFTDLK GTIKVFLQAM
     FGDLPIRFRA SYFPFTEPSA EVDLQWNGRW LEVMGCGMVD PNVMKSVGYD PEIYTGFAAG
     FGVERFAMVL HQIDDIRRLY ASDLRFLRQF
//