ID   SYFA_ALCBS              Reviewed;         339 AA.
AC   Q0VNG2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=ABO_1838;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL17286.1; -; Genomic_DNA.
DR   RefSeq; YP_693558.1; -.
DR   GeneID; 4211602; -.
DR   GenomeReviews; AM286690_GR; ABO_1838.
DR   KEGG; abo:ABO_1838; -.
DR   NMPDR; fig|393595.12.peg.1844; -.
DR   HOGENOM; Q0VNG2; -.
DR   OMA; Q0VNG2; FRASYFP.
DR   BioCyc; ABOR393595:ABO_1838-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    339       Phenylalanyl-tRNA synthetase alpha chain.
FT                                /FTId=PRO_1000006796.
FT   METAL       253    253       Magnesium (By similarity).
SQ   SEQUENCE   339 AA;  37628 MW;  92703B603C38344C CRC64;
     MENLNALVDA ALAEVEQAGD IRALDDVRVK YLGKKGEISA LMKGLGKLSA EERPQAGAVI
     NEGKQKVQDA IADRKSAMEE AALKQQLASE TVDVTLPGRG ELPGGLHPVN RMRRRIEDFF
     LRLGFDISEG PEVEDDFHNF EALNIPSHHP ARAMHDTFYF GDGRLLRTHT SPVQVRVMEQ
     GKPPFRIIAP GRVYRCDSDL THTPMFHQVE GLLVDKGITF ADLRGTVAEF LRYTFEVEDL
     PVRFRPSYFP FTEPSAEVDV GCVSCGGEGC RVCSHTGWIE IMGCGMVHPT VLEAGGVDAE
     EYSGFAFGMG IERIAMLRYG VNDLRLFFEN DTRFLSQFG
//