ID E9LHG2_9LACO Unreviewed; 111 AA. AC E9LHG2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 05-DEC-2018, entry version 22. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|SAAS:SAAS00896469}; DE EC=6.1.1.20 {ECO:0000256|SAAS:SAAS00896486}; DE Flags: Fragment; GN Name=pheS {ECO:0000313|EMBL:ADW23136.1}; OS Lactobacillus vini. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=238015 {ECO:0000313|EMBL:ADW23136.1}; RN [1] {ECO:0000313|EMBL:ADW23136.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TR7.5.7 {ECO:0000313|EMBL:ADW23136.1}; RX PubMed=21092306; DOI=10.1186/1471-2180-10-298; RA Lucena B.T., Dos Santos B.M., Moreira J.L., Moreira A.P., Nunes A.C., RA Azevedo V., Miyoshi A., Thompson F.L., de Morais M.A.; RT "Diversity of lactic acid bacteria of the bioethanol process."; RL BMC Microbiol. 10:298-298(2010). RN [2] {ECO:0000313|EMBL:ADW23136.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TR7.5.7 {ECO:0000313|EMBL:ADW23136.1}; RA de Lucena B.T.L., dos Santos B.M., Moreira J.L.S., Moreira A.P.B., RA Nunes A.C., Azevedo V.A., Thompson F.L., de Morais M.A.Jr.; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + CC H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78531, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699; CC EC=6.1.1.20; Evidence={ECO:0000256|SAAS:SAAS00896454}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00896426}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|SAAS:SAAS00896463}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00896423}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily. CC {ECO:0000256|SAAS:SAAS00896416}. 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; HQ009778; ADW23136.1; -; Genomic_DNA. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR PANTHER; PTHR11538:SF48; PTHR11538:SF48; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|SAAS:SAAS01110915, KW ECO:0000313|EMBL:ADW23136.1}; KW ATP-binding {ECO:0000256|SAAS:SAAS01110882}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00896401}; KW Ligase {ECO:0000256|SAAS:SAAS01110936}; KW Magnesium {ECO:0000256|SAAS:SAAS00896467}; KW Metal-binding {ECO:0000256|SAAS:SAAS00896465}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS01110884}; KW Protein biosynthesis {ECO:0000256|SAAS:SAAS01110938}. FT DOMAIN 12 88 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE: FT PS50862}. FT NON_TER 1 1 {ECO:0000313|EMBL:ADW23136.1}. FT NON_TER 111 111 {ECO:0000313|EMBL:ADW23136.1}. SQ SEQUENCE 111 AA; 12449 MW; 0F0F3840543CD85E CRC64; TNLEKHDFSQ GPLKMISPGK VYRRDTDDAT HSHQFHQVEG LVIDKHVTMA DLKGTLEKIA QTVFGAKRQI RLRPSYFPFT EPSVEVDVSC FKCGGKGCQV CKQTGWIEVL G //