ID SYR_OCEIH Reviewed; 556 AA. AC Q8EM45; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Arginine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00123}; DE EC=6.1.1.19 {ECO:0000255|HAMAP-Rule:MF_00123}; DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00123}; DE Short=ArgRS {ECO:0000255|HAMAP-Rule:MF_00123}; GN Name=argS {ECO:0000255|HAMAP-Rule:MF_00123}; OrderedLocusNames=OB3015; OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / OS KCTC 3954 / HTE831). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus. OX NCBI_TaxID=221109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831; RX PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge RT and its unexpected adaptive capabilities to extreme environments."; RL Nucleic Acids Res. 30:3927-3935(2002). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl- CC tRNA(Arg); Xref=Rhea:RHEA:20301, Rhea:RHEA-COMP:9658, Rhea:RHEA- CC COMP:9673, ChEBI:CHEBI:30616, ChEBI:CHEBI:32682, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78513, ChEBI:CHEBI:456215; CC EC=6.1.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_00123}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00123}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00123}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00123}. 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; BA000028; BAC14971.1; -; Genomic_DNA. DR RefSeq; WP_011067411.1; NC_004193.1. DR AlphaFoldDB; Q8EM45; -. DR SMR; Q8EM45; -. DR STRING; 221109.gene:10735267; -. DR KEGG; oih:OB3015; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_9; -. DR OrthoDB; 9805987at2; -. DR PhylomeDB; Q8EM45; -. DR Proteomes; UP000000822; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd07956; Anticodon_Ia_Arg; 1. DR CDD; cd00671; ArgRS_core; 1. DR Gene3D; 3.30.1360.70; Arginyl tRNA synthetase N-terminal domain; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00123; Arg_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR036695; Arg-tRNA-synth_N_sf. DR InterPro; IPR035684; ArgRS_core. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd. DR NCBIfam; TIGR00456; argS; 1. DR PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC-RELATED; 1. DR PANTHER; PTHR11956; ARGINYL-TRNA SYNTHETASE; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM01016; Arg_tRNA_synt_N; 1. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF55190; Arginyl-tRNA synthetase (ArgRS), N-terminal 'additional' domain; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..556 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000151585" FT MOTIF 132..142 FT /note="'HIGH' region" SQ SEQUENCE 556 AA; 62504 MW; 39D99952AC2C3005 CRC64; MNVLEQTEQK LKEQIHHAVI HAELATEDQV PDIILEKPKD KAHGDFATNI AMQLARVAKK APRQIADDIA SKLNKSEASV EKVEIAGPGF INFFMKQDFL GEVIDTVLSA GDNYGKSTGG NGEKVQVEFV SVNPTGDLHL GHARNAAFGD VLCNVFAAAG YEVEREYYIN DAGNQINNLG LSVEARYLQE IGQDVDMPED GYQGQAIIEI AKELVKKDGE KWADKDHEER LDFFKEYGLK ASLRNIESDL KDFRVEFDHW FSERSLFKDG QIDDTLAVLD DGGYTFEKDG ALWFKTTEFG DDKDRVLIKG DGNYTYLTPD IAYHKNKLDR GFDRIINVWG SDHHGYIPRM RAALQALGYP VEKFDVKIIQ MVNLFEAGEK VKMSKRTGKA VSLRELMDEV GIDAVRYYFV ARSNDSQLDF DMDLAKSQSN DNPVYYAQYA HARICTMLSQ AKSKGFNTEA EFDASLLTAE KELDLLKKIG ELPQMIVDAA DKHTPHKVTQ YIFELATLLH SFYNAEKVLD ADNEARTHAR IALMKAVRQT LANAMTIIGI SAPEKM //