ID SYR_ALBFT Reviewed; 565 AA. AC Q220N0; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 18-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 93. 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}; GN OrderedLocusNames=Rfer_0773; OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) OS (Rhodoferax ferrireducens). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Rhodoferax. OX NCBI_TaxID=338969; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-621 / DSM 15236 / T118; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000267; ABD68523.1; -; Genomic_DNA. DR RefSeq; WP_011463096.1; NC_007908.1. DR AlphaFoldDB; Q220N0; -. DR SMR; Q220N0; -. DR STRING; 338969.Rfer_0773; -. DR KEGG; rfr:Rfer_0773; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_4; -. DR OrthoDB; 9803211at2; -. DR Proteomes; UP000008332; 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..565 FT /note="Arginine--tRNA ligase" FT /id="PRO_0000242078" FT MOTIF 128..138 FT /note="'HIGH' region" SQ SEQUENCE 565 AA; 62274 MW; 6E620EA2B9614948 CRC64; MLSVKIELLE ALHQALEKLS PGAGSKAVFE SPKVAAHGDL ATTAAMQLAK PLKLNPRQLA ENLRAELLVR APFERWVEAI DIAGPGFINI KLKPEAKQQT VREVLSQGQQ FGSQPGTGKR MLVEFVSANP TGPLHVGHGR QAALGDAICN LYQTQGWAVY REFYYNDAGV QIGTLASSTQ LRARGFKPGD PEWPSGENAA AYNGDYIADI AADYLAKKTV HSDDRAFTAS GDVEALDDIR LFAVAYLRHE QDLDLKAFAV HFDNYYLESS LYLSGKVDDV VKRLHDAGKT YEHDGALWLK STEYGDDKDR VMRKGDGSYT YFVPDVAYHI SKWERGFEKV VNIQGTDHHG TIARVRAGLQ AANVGIPKGY PDYVLHTMVR VVRGGEEVKI SKRAGSYVTL RDLIEWTSKD AVRFFLLSRK PDTEYTFDVD LAVAKNNDNP VYYVQYAHAR ICSVLAAWRE KEGGDVASLG QADLSPLQSP QALALLLLLA KYPEMLTAAA AGFAPHDVTF YLRELAACYH SYYDAERILV DDDLIKRARL ALVAATAQVL HNGLAVLGVS APQKM //