ID A0A090I8U6_METFO Unreviewed; 564 AA. AC A0A090I8U6; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 22-FEB-2023, entry version 36. DE RecName: Full=Arginine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00123}; DE EC=6.1.1.19 {ECO:0000256|HAMAP-Rule:MF_00123}; DE AltName: Full=Arginyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00123}; DE Short=ArgRS {ECO:0000256|HAMAP-Rule:MF_00123}; GN Name=argS {ECO:0000256|HAMAP-Rule:MF_00123, GN ECO:0000313|EMBL:CEA13682.1}; GN ORFNames=DSM1535_1348 {ECO:0000313|EMBL:CEA13682.1}; OS Methanobacterium formicicum. OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanobacterium. OX NCBI_TaxID=2162 {ECO:0000313|EMBL:CEA13682.1, ECO:0000313|Proteomes:UP000032423}; RN [1] {ECO:0000313|Proteomes:UP000032423} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1535 {ECO:0000313|Proteomes:UP000032423}; RX PubMed=25270020; DOI=10.1016/j.jbiotec.2014.09.018; RA Maus I., Stantscheff R., Wibberg D., Stolze Y., Winkler A., Puhler A., RA Konig H., Schluter A.; RT "Complete genome sequence of the methanogenic neotype strain RT Methanobacterium formicicum MF."; RL J. Biotechnol. 192:40-41(2014). 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:0000256|ARBA:ARBA00001766, CC ECO:0000256|HAMAP-Rule:MF_00123}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00123, CC ECO:0000256|RuleBase:RU363038}. 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; LN515531; CEA13682.1; -; Genomic_DNA. DR AlphaFoldDB; A0A090I8U6; -. DR EnsemblBacteria; CEA13682; CEA13682; DSM1535_1348. DR KEGG; mfi:DSM1535_1348; -. DR PATRIC; fig|2162.9.peg.1380; -. DR Proteomes; UP000032423; 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 PANTHER; PTHR11956:SF5; ARGININE--TRNA LIGASE, CYTOPLASMIC; 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 TIGRFAMs; TIGR00456; argS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146, KW ECO:0000256|HAMAP-Rule:MF_00123}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00123}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00123}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00123}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00123}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00123}. FT DOMAIN 7..88 FT /note="Arginyl tRNA synthetase N-terminal" FT /evidence="ECO:0000259|SMART:SM01016" FT DOMAIN 447..564 FT /note="DALR anticodon binding" FT /evidence="ECO:0000259|SMART:SM00836" FT MOTIF 122..132 FT /note="'HIGH' region" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00123" SQ SEQUENCE 564 AA; 63910 MW; B7020BADE98C30C2 CRC64; MYKKLENKAI ESVQNTIQTL GWEEPSEIKF EIPPNPNMGD MATSVAFQLA STLKKSPVDI AQSIAGNLEV KSPFKTVETK GPYINFFFDP ELFSRMVLES VQEDYGLLEE KNEKIILEHT SANPNGPLHI GHIRNAIIGD SLARTLRSAG YQVETQYYVN DMGRQIAMIV WGLQNLDYQM DPKGRGDVEI GKLYFQVNQE LKAKPEIKGQ IDSILKTYEE ENPPELESMF KKVVRKCLDG VEDTSRRMNI VHDDFIWESQ FVRDGSMEKI LEALDEYTTQ NEVLYLDLTD YGIEKELILT RSDGTSLYST RDLAYHLFKS QNSDQVVDIL GSDHKLAIDQ LKIALGLVGG KSPDVVFYEF ITLPEGSMST RRGVFISVDE LIDEATQRAR AELETRRPEL GEDEKNNIAK IIGVGAIRYY ISRLSPEKHI VFKWDEALSF ERGCASIQYA HARACKLLEK VSEFNPSKVD MDSLDFQNMD TLEIDLLKTL ARFSTIIEDS ARDLRVHPVA QYALEVAGAF NKFYKSVPVI GSDKELLRLL LVDKSRITIR NALDLLGIES PSSM //