ID SYFA_RHIE6 Reviewed; 360 AA.
AC B3PYE2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 01-MAY-2013, entry version 35.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=pheS; OrderedLocusNames=RHECIAT_CH0000299;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) 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 subunits (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily.
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DR EMBL; CP001074; ACE89293.1; -; Genomic_DNA.
DR RefSeq; YP_001976471.1; NC_010994.1.
DR STRING; 491916.RHECIAT_CH0000299; -.
DR EnsemblBacteria; ACE89293; ACE89293; RHECIAT_CH0000299.
DR GeneID; 6398173; -.
DR KEGG; rec:RHECIAT_CH0000299; -.
DR PATRIC; 23094068; VBIRhiEtl120572_0301.
DR eggNOG; COG0016; -.
DR HOGENOM; HOG000242675; -.
DR KO; K01889; -.
DR OMA; LTHTPMF; -.
DR ProtClustDB; PRK00488; -.
DR BioCyc; RETL491916:GH4T-2052-MONOMER; -.
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; Phe_tRNA_synth_alpha1; 1; -.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR004188; Phe-tRNA_ligase_II_N.
DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR010978; tRNA-bd_arm.
DR Pfam; PF02912; Phe_tRNA-synt_N; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF46589; tRNA_binding_arm; 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 1 360 Phenylalanine--tRNA ligase alpha subunit.
FT /FTId=PRO_1000114904.
FT METAL 260 260 Magnesium (By similarity).
SQ SEQUENCE 360 AA; 40214 MW; 3129FCB6C466E775 CRC64;
MSDIDQLNSS LLAEIAATND EPALEAVRVA ALGKKGSISE LLKTLGAMTP EERQTRGAAI
NALKNAVTDA IAERKSVLKM AAVNARLKAE TVDVSLPVRS SPAERGRIHP ISQIVDEITA
IFADMGFSIA EGPDIETDYY NFTALNFPEG HPAREMHDTF FFNPDENGER KVLRTHTSPV
QVRTMEAQKP PIRIIIPGKT YRQDSDATHS PMFHQVEGLV IDKKANVANI RWVLEEFCKT
FFEVDSVTMR FRPSFFPFTE PSFEVDIQCD RSGPIVKFGE GTDWMEILGC GMVHPNVLRY
GGLDPDEYQG FAWGMGLDRI AMLKYGMPDL RDFFNADVRW MTHYGFRPLD MPTLFGGLSA
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