ID SYFA_GEOSM Reviewed; 338 AA. AC C6DYJ1; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 01-MAY-2013, entry version 27. 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=GM21_2226; OS Geobacter sp. (strain M21). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443144; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M21; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Lovley D.; RT "Complete sequence of Geobacter sp. M21."; RL Submitted (JUL-2009) 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001661; ACT18275.1; -; Genomic_DNA. DR RefSeq; YP_003022033.1; NC_012918.1. DR STRING; 443144.GM21_2226; -. DR EnsemblBacteria; ACT18275; ACT18275; GM21_2226. DR GeneID; 8137564; -. DR KEGG; gem:GM21_2226; -. DR PATRIC; 22018896; VBIGeoSp56140_2173. DR eggNOG; COG0016; -. DR HOGENOM; HOG000242675; -. DR KO; K01889; -. DR OMA; LTHTPMF; -. DR ProtClustDB; PRK00488; -. DR BioCyc; GSP443144:GHKM-2265-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 1 338 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_1000204828. FT METAL 253 253 Magnesium (By similarity). SQ SEQUENCE 338 AA; 37518 MW; EA2E1117285F03D0 CRC64; MKDKLEALLD QALSELAQAS TEEGVQELRV KYLGKKGELT SVMKGLGALT PEERPIIGQV VNTVKGKLEE GFELRGGEIR EAVKSARLSA ERIDVTLPGR RRPLGSKHPI TLVTEEIASI FGALGFAVAE GPEIELDFYN FEALNLPKDH PARDMQDTFY FGESVLLRTH TSPVQIRTML KQPPPVRIIA PGTVYRCDSD ATHSPMFHQV EGLMVDKGIT FGDLKGILTL FISQLFGSDI GVRLRPSFFP FTEPSAEVDI ACVICRGKGC RVCKETGWLE ILGAGMVDPE VYRHVGYDSE LYTGFAFGMG IERIAMLKYG IADMRLLFEN DLRFLKQF //