ID D2S8R2_GEOOG Unreviewed; 355 AA. AC D2S8R2; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 88. 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 OrderedLocusNames=Gobs_3033 {ECO:0000313|EMBL:ADB75643.1}; OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC OS A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20). OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales; OC Geodermatophilaceae; Geodermatophilus. OX NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB75643.1, ECO:0000313|Proteomes:UP000001382}; RN [1] {ECO:0000313|EMBL:ADB75643.1, ECO:0000313|Proteomes:UP000001382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 / RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382}; RX PubMed=21304698; RA Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T., RA Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L., RA Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Geodermatophilus obscurus type strain (G- RT 20)."; RL Stand. Genomic Sci. 2:158-167(2010). RN [2] {ECO:0000313|Proteomes:UP000001382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 / RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., RA Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Geodermatophilus obscurus DSM 43160."; RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases. 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; CP001867; ADB75643.1; -; Genomic_DNA. DR RefSeq; WP_012949073.1; NC_013757.1. DR AlphaFoldDB; D2S8R2; -. DR STRING; 526225.Gobs_3033; -. DR KEGG; gob:Gobs_3033; -. DR eggNOG; COG0016; Bacteria. DR HOGENOM; CLU_025086_0_0_11; -. DR OrthoDB; 9800719at2; -. DR Proteomes; UP000001382; 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: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}; 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:UP000001382}. FT DOMAIN 135..328 FT /note="Aminoacyl-transfer RNA synthetases class-II family FT profile" FT /evidence="ECO:0000259|PROSITE:PS50862" FT BINDING 273 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 355 AA; 39141 MW; 0E3F0BE6D02A10AE CRC64; MSGANDPYDP KQVAALSPES LDDAVAEAQR AFAGAGDLEQ LAAVRPAHLG DRAPVLLARR ELGALPPAAR ADAGKRVNAA RVAVTEAYET RRAELEAERD ARVLAEERVD VTLPWDRLPR GARHPLTTLT DRIADIFVGM GYEVAEGPEL EAEWLNFDAL NIGRDHPART MMDTFFVAPE DSGLVLRTHT SPVQARTMLS RTPPIYIVAP GRVYRTDELD ATHLPVFHQV EGLAVDRGLT MAHLRGTLDH LARSLFGADA VTRWRPSYFP FTEPSAEFDV WFPEHRDGPR WVEWGGCGMV NPRVLVACGI DPEEYSGFAF GMGIERALQF RSAVGDMRHF AEGDVRFTSA FGVEQ //