ID Q189P4_CLOD6 Unreviewed; 339 AA. AC Q189P4; DT 25-JUL-2006, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 2. DT 27-MAR-2024, entry version 126. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281}; DE EC=6.1.1.20 {ECO:0000256|HAMAP-Rule:MF_00281}; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000256|HAMAP-Rule:MF_00281}; DE Short=PheRS {ECO:0000256|HAMAP-Rule:MF_00281}; GN Name=pheS {ECO:0000256|HAMAP-Rule:MF_00281, GN ECO:0000313|EMBL:CAJ67532.2}; GN OrderedLocusNames=CD630_06990 {ECO:0000313|EMBL:CAJ67532.2}; OS Clostridioides difficile (strain 630) (Peptoclostridium difficile). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae; OC Clostridioides. OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ67532.2, ECO:0000313|Proteomes:UP000001978}; RN [1] {ECO:0000313|EMBL:CAJ67532.2, ECO:0000313|Proteomes:UP000001978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=630 {ECO:0000313|EMBL:CAJ67532.2, RC ECO:0000313|Proteomes:UP000001978}; RX PubMed=16804543; DOI=10.1038/ng1830; RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N., RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H., RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N., RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A., RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K., RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L., RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.; RT "The multidrug-resistant human pathogen Clostridium difficile has a highly RT mobile, mosaic genome."; RL Nat. Genet. 38:779-786(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + CC L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, CC Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, CC ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; CC Evidence={ECO:0000256|ARBA:ARBA00000395, ECO:0000256|HAMAP- CC Rule:MF_00281}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00281}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP- CC Rule:MF_00281}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000256|ARBA:ARBA00011209, ECO:0000256|HAMAP-Rule:MF_00281}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00281}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. CC Phe-tRNA synthetase alpha subunit type 1 subfamily. CC {ECO:0000256|ARBA:ARBA00010207, ECO:0000256|HAMAP-Rule:MF_00281}. 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; AM180355; CAJ67532.2; -; Genomic_DNA. DR RefSeq; WP_003436795.1; NZ_JAUPES010000005.1. DR RefSeq; YP_001087175.2; NC_009089.1. DR AlphaFoldDB; Q189P4; -. DR STRING; 272563.CD630_06990; -. DR EnsemblBacteria; CAJ67532; CAJ67532; CD630_06990. DR GeneID; 66353201; -. DR KEGG; cdf:CD630_06990; -. DR KEGG; pdc:CDIF630_00814; -. DR PATRIC; fig|272563.120.peg.719; -. DR eggNOG; COG0016; Bacteria. DR OrthoDB; 9800719at2; -. DR PhylomeDB; Q189P4; -. DR BioCyc; PDIF272563:G12WB-809-MONOMER; -. DR Proteomes; UP000001978; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProt. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00496; PheRS_alpha_core; 1. DR HAMAP; MF_00281; Phe_tRNA_synth_alpha1; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL. 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 NCBIfam; TIGR00468; pheS; 1. DR PANTHER; PTHR11538:SF41; PHENYLALANINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11538; PHENYLALANYL-TRNA SYNTHETASE; 1. DR Pfam; PF02912; Phe_tRNA-synt_N; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR SUPFAM; SSF46589; tRNA-binding arm; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00281}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00281}; Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00281}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00281}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00281}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00281}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00281}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00281}; Reference proteome {ECO:0000313|Proteomes:UP000001978}. FT DOMAIN 111..330 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT COILED 65..92 FT /evidence="ECO:0000256|SAM:Coils" FT BINDING 254 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="shared with beta subunit" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00281" SQ SEQUENCE 339 AA; 38004 MW; 16B501BEA3EE3C32 CRC64; MQEKLLALRE AALAEIKEAQ SIESVESLRV KYLGKKGEIT AILKEMGKLS AEERPVVGKV ANEVRENIEL SINSKKEEIN AIEKERKLKE EVIDVTQPGK VLKVGKKHPI TQIIDEVTDI FIGMGFSIAE GPEVETVENN FDALNAPKDH PSRDMSDTFY INDGVLLRTQ TSPVQVRTMR SQELPIKVIA PGRCFRSDSP DATHSPMFHQ IEGLVVGKDV TMAEFKGTMD IFVEKLFGSD IKTKFRPHNF PFTEPSAEVD VTCFKCGGKG CPMCKYEGWI EILGSGMVHP NVLRNCGIDP EVYSGFAFGV GVERLAMLKY EIDDIRLLFE NDMRFLNQF //