ID SYR_METNO Reviewed; 590 AA. AC B8I9T2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 73. 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=Mnod_2178; OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Methylobacteriaceae; Methylobacterium. OX NCBI_TaxID=460265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J., RA Richardson P.; RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060."; RL Submitted (JAN-2009) 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; CP001349; ACL57160.1; -; Genomic_DNA. DR RefSeq; WP_015928846.1; NC_011894.1. DR AlphaFoldDB; B8I9T2; -. DR SMR; B8I9T2; -. DR STRING; 460265.Mnod_2178; -. DR KEGG; mno:Mnod_2178; -. DR eggNOG; COG0018; Bacteria. DR HOGENOM; CLU_006406_0_1_5; -. DR OrthoDB; 9803211at2; -. DR Proteomes; UP000008207; 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; 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; 2. 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..590 FT /note="Arginine--tRNA ligase" FT /id="PRO_1000198921" FT MOTIF 130..140 FT /note="'HIGH' region" SQ SEQUENCE 590 AA; 64111 MW; A32BAF0E6FDDAFA0 CRC64; MNIFAAFEER IGEALASLTR AGQLPEGLDL GRVVVEPPRD PSHGDLATNA ALVLAKEART NPKALAERLA AELRSDPRVT EASVAGPGFL NLRLAPQVYG DVVRAALRAG EAFGRGAKQP GLVNVEYVSA NPTGPMHVGH GRGAVFGDAL ANLLVAAGRE VVREYYINDA GAQVDVLARS AFLRYREALG EEIGTIPEGL YPGDYLKPVG AMLAKTHGRS LLGKPEAEWL PLVREAAIGA MMERIREDLA ALGIRHDVFF SERTLQEGGK EGGEGGAVAR LIEALRARDL VYVGRLPPPK GQLPEDWEDR DQTLFRSTAF GDDIDRPLLK SDGSYTYFAS DIAYHASKVE RGATELIDVL GADHGGYVKR MQAAVRAVSD GRASLDVKLC QLVRLLRGGE PVKMSKRAGE FVTLREVIDE VGRDPVRFMM LYRKNDATLD FDLAKVVEQS KDNPVFYVQY AHARTASVFR QAREAFPGED LSAEALAGAD LSLLTDSGEA EIMRLIAQYP RVVESAGSAH EPHRLAFYLY ELASAFHSFW NKGKDLPQLR FVNQTDRMST LSRLALVAAL RGVLASGLGI LGVTAPDEMR //