ID C5J2N6_LACPN Unreviewed; 152 AA. AC C5J2N6; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 05-JUL-2017, entry version 19. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|SAAS:SAAS00694257}; DE EC=6.1.1.20 {ECO:0000256|SAAS:SAAS00694265}; DE Flags: Fragment; OS Lactobacillus plantarum. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1590 {ECO:0000313|EMBL:ACS14133.1}; RN [1] {ECO:0000313|EMBL:ACS14133.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IMAU20015 {ECO:0000313|EMBL:ACS14133.1}; RA Yu J., Sun Z.H., Liu W.J., Zhang J.C., Zhang H.P.; RT "Genetic Classification and Distinguishing of Lactobacillus Species RT Based on Different Partial hsp60, pheS and tuf Gene Sequences."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC {ECO:0000256|SAAS:SAAS00694269}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00694270}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|SAAS:SAAS00694237}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00694264}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Phe-tRNA synthetase alpha subunit type 1 subfamily. CC {ECO:0000256|SAAS:SAAS00694266}. 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; FJ983856; ACS14133.1; -; Genomic_DNA. DR eggNOG; ENOG4105CSS; Bacteria. DR eggNOG; COG0016; LUCA. 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; IPR022911; Phe_tRNA_ligase_alpha1_bac. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR PANTHER; PTHR11538:SF52; PTHR11538:SF52; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|SAAS:SAAS00694272}; KW ATP-binding {ECO:0000256|SAAS:SAAS00694245}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00694273}; KW Ligase {ECO:0000256|SAAS:SAAS00694260}; KW Magnesium {ECO:0000256|SAAS:SAAS00694251}; KW Metal-binding {ECO:0000256|SAAS:SAAS00694267}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00694255}; KW Protein biosynthesis {ECO:0000256|SAAS:SAAS00694248}. FT DOMAIN 1 151 tRNA-synt_2d. {ECO:0000259|Pfam:PF01409}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACS14133.1}. FT NON_TER 152 152 {ECO:0000313|EMBL:ACS14133.1}. SQ SEQUENCE 152 AA; 17019 MW; CCFD06B25405312D CRC64; DMQDTFYITK DVLLRTQTSA DQPRSLENHD FSKGPLKVLS PGRVYRRDTD DATHSHQFHQ IEGLVVDKHI TMADLKGTLI LVAKTLFGDQ FDVRLRPSFF PFTEPSVEAD VTCFNCNGKG CAICKQTGWI EVLGAGMVHP HVLEMSGIDP EE //